DrugMAP Full Data Download File Title - DrugMAP drug metabolizing enzyme (DME) information in raw format Version 1.01 (2022.07.20) Provided by Lab of Innovative Drug Reasearch and Bioinformatics (IDRB) College of Pharmaceutical Sciences Zhejiang University https://idrblab.org/ Any question about data provided here, please contact with: Dr. Li (lifengcheng@zju.edu.cn) and Dr. Yin (yinjiayi@zju.edu.cn) ID: DME ID DN: DME Name GN: Gene Name SN: Synonyms UC: Uniprot AC RD: Represent Drug GI: Gene ID E1: EC 1 E2: EC 2 E3: EC 3 EC: EC ID RC: Reactome Pathway KG: KEGG Pathway PD: PDB ID SQ: Sequence TD: Tissue Distribution FC: Function KD: Kingdom PL: Phylum CL: Class OD: Order FM: Family GE: Genus SP: Species SU: Subspecies DE4LYSA ID DE4LYSA DE4LYSA DN Cytochrome P450 3A4 (CYP3A4) DE4LYSA GN CYP3A4 DE4LYSA SN Cytochrome P450 family 3 subfamily A member 4; Quinine 3-monooxygenase; 1,4-cineole 2-exo-monooxygenase; 1,8-cineole 2-exo-monooxygenase; Albendazole monooxygenase (sulfoxide-forming); Albendazole sulfoxidase; CYP3A3; CYP3A4; CYPIIIA3; CYPIIIA4; Cholesterol 25-hydroxylase; Cytochrome P450 3A3; Cytochrome P450 HLp; Cytochrome P450 NF-25; Cytochrome P450-PCN1; Nifedipine oxidase DE4LYSA UC CP3A4_HUMAN DE4LYSA RD Bosutinib DE4LYSA GI 1576 DE4LYSA E1 1: Oxidoreductase DE4LYSA E2 1.14: Oxygen paired donor oxidoreductase DE4LYSA E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE4LYSA EC 1.14.14.55 DE4LYSA RC Aflatoxin activation and detoxification:R-HSA-5423646; Biosynthesis of maresin-like SPMs:R-HSA-9027307; Xenobiotics:R-HSA-211981 DE4LYSA KG Bile secretion:hsa04976; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Linoleic acid metabolism:hsa00591; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DE4LYSA PD 1W0F; 1W0G; 2J0D; 2V0M; 3NXU; 3TJS; 3UA1; 4D6Z; 4D75 DE4LYSA SQ MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVNETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGGLLQPEKPVVLKVESRDGTVSGA DE4LYSA TD Primarily distributed in intestine and liver. DE4LYSA FC This enzyme is involved in the metabolism of sterols, steroid hormones, retinoids and fatty acids. It exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta- estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C-16 position and plays a role in the metabolism of androgens, particularly in oxidative deactivation of testosterone. It also metabolizes testosterone to less biologically active 2beta- and 6beta- hydroxytestosterones. It catalyzes bisallylic hydroxylation of polyunsaturated fatty acids (PUFA) and the epoxidation of double bonds of PUFA with a preference for the last double bond. It metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 8,9-, 11,12-, and 14,15- epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs) and plays a role in the metabolism of retinoids.In addition, it displays high catalytic activity for oxidation of all-trans-retinol to all-trans-retinal, a rate- limiting step for the biosynthesis of all-trans-retinoic acid (atRA) and further metabolizes atRA toward 4-hydroxyretinoate and may play a role in hepatic atRA clearance. It is also responsible for oxidative metabolism of xenobiotics. It metabolizes the majority of the administered drugs; catalyzes sulfoxidation of the anthelmintics albendazole and fenbendazole and hydroxylates antimalarial drug quinine. DE4LYSA KD 33208: Metazoa DE4LYSA PL 7711: Chordata DE4LYSA CL 40674: Mammalia DE4LYSA OD 9443: Primates DE4LYSA FM 9604: Hominidae DE4LYSA GE 9605: Homo DE4LYSA SP 9606: Homo sapiens DEVDYN7 ID DEVDYN7 DEVDYN7 DN Cytochrome P450 2E1 (CYP2E1) DEVDYN7 GN CYP2E1 DEVDYN7 SN Cytochrome P450 family 2 subfamily E member 1; 4-nitrophenol 2-hydroxylase; Cytochrome P450-J; CYP2E; CYP2E1; CYPIIE1 DEVDYN7 UC CP2E1_HUMAN DEVDYN7 RD Eszopiclone DEVDYN7 GI 1571 DEVDYN7 E1 1: Oxidoreductase DEVDYN7 E2 1.14: Oxygen paired donor oxidoreductase DEVDYN7 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEVDYN7 EC 1.14.14.1 DEVDYN7 RC Biosynthesis of maresin-like SPMs:R-HSA-9027307; CYP2E1 reactions:R-HSA-211999; Xenobiotics:R-HSA-211981 DEVDYN7 KG Arachidonic acid metabolism:hsa00590; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Linoleic acid metabolism:hsa00591; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Non-alcoholic fatty liver disease (NAFLD):hsa04932; Steroid hormone biosynthesis:hsa00140 DEVDYN7 PD 3E4E; 3E6I; 3GPH; 3KOH; 3LC4; 3T3Z DEVDYN7 SQ MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRLAQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGPTWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVIADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVAEVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRFITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGKFKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGCIPPRYKLCVIPRS DEVDYN7 TD Primarily distributed in liver. DEVDYN7 FC This enzyme is involved in the metabolism of fatty acids. It catalyzes the hydroxylation of carbon-hydrogen bonds and hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids.In addition, it may be involved in the oxidative metabolism of xenobiotics. DEVDYN7 KD 33208: Metazoa DEVDYN7 PL 7711: Chordata DEVDYN7 CL 40674: Mammalia DEVDYN7 OD 9443: Primates DEVDYN7 FM 9604: Hominidae DEVDYN7 GE 9605: Homo DEVDYN7 SP 9606: Homo sapiens DECB0K3 ID DECB0K3 DECB0K3 DN Cytochrome P450 2D6 (CYP2D6) DECB0K3 GN CYP2D6 DECB0K3 SN Cytochrome P450 family 2 subfamily D member 6; Cytochrome P450-DB1; Debrisoquine 4-hydroxylase; CYP2D6; CYP2DL1; CYPIID6 DECB0K3 UC CP2D6_HUMAN DECB0K3 RD Carvedilol DECB0K3 GI 1565 DECB0K3 E1 1: Oxidoreductase DECB0K3 E2 1.14: Oxygen paired donor oxidoreductase DECB0K3 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DECB0K3 EC 1.14.14.1 DECB0K3 RC Biosynthesis of maresin-like SPMs:R-HSA-9027307; CYP2E1 reactions:R-HSA-211999; Fatty acids:R-HSA-211935; Miscellaneous substrates:R-HSA-211958; Xenobiotics:R-HSA-211981 DECB0K3 KG Drug metabolism - cytochrome P450:hsa00982; Endocrine resistance:hsa01522; Metabolism of xenobiotics by cytochrome P450:hsa00980; Serotonergic synapse:hsa04726 DECB0K3 PD 3TBG; 3TDA; 4WNT; 4WNU; 4WNV; 4WNW; 4XRY; 4XRZ; 5TFT DECB0K3 SQ MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGVFAFLVSPSPYELCAVPR DECB0K3 TD Primarily distributed in liver. DECB0K3 FC This enzyme is involved in the metabolism of fatty acids, steroids and retinoids. It catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). It also metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 20-hydroxyeicosatetraenoic acid ethanolamide (20-HETE-EA) and 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs). In addition, it catalyzes the hydroxylation of carbon-hydrogen bonds and metabolizes cholesterol toward 25- hydroxycholesterol. It catalyzes the oxidative transformations of all-trans retinol to all-trans retina and also involved in the oxidative metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants. DECB0K3 KD 33208: Metazoa DECB0K3 PL 7711: Chordata DECB0K3 CL 40674: Mammalia DECB0K3 OD 9443: Primates DECB0K3 FM 9604: Hominidae DECB0K3 GE 9605: Homo DECB0K3 SP 9606: Homo sapiens DE5IED8 ID DE5IED8 DE5IED8 DN Cytochrome P450 2C9 (CYP2C9) DE5IED8 GN CYP2C9 DE5IED8 SN Cytochrome P450 family 2 subfamily C member 9; (R)-limonene 6-monooxygenase; (S)-limonene 6-monooxygenase; (S)-limonene 7-monooxygenase; Cytochrome P-450MP; Cytochrome P450 MP-4; Cytochrome P450 MP-8; Cytochrome P450 PB-1; CYP2C10; CYP2C9; CYPIIC9 DE5IED8 UC CP2C9_HUMAN DE5IED8 RD Candesartan cilexetil DE5IED8 GI 1559 DE5IED8 E1 1: Oxidoreductase DE5IED8 E2 1.14: Oxygen paired donor oxidoreductase DE5IED8 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE5IED8 EC 1.14.14.1 DE5IED8 RC Biosynthesis of maresin-like SPMs:R-HSA-9027307; CYP2E1 reactions:R-HSA-211999; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE):R-HSA-2142816; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET):R-HSA-2142670; Xenobiotics:R-HSA-211981 DE5IED8 KG Arachidonic acid metabolism:hsa00590; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Linoleic acid metabolism:hsa00591; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Serotonergic synapse:hsa04726 DE5IED8 PD 1R9O; 4NZ2; 5A5I; 5A5J; 5K7K; 5W0C; 5X23; 5X24; 5XXI DE5IED8 SQ MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFMKSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYIDLLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFKKSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVPPFYQLCFIPV DE5IED8 TD Primarily distributed in liver. DE5IED8 FC This enzyme is involved in the metabolism of various endogenous substrates, including fatty acids and steroids. It catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) and hydroxylation of carbon-hydrogen bonds.It metabolizes cholesterol toward 25-hydroxycholesterol and catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA). It also metabolizes plant monoterpenes such as limonene; oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol and metabolizes drugs such as S- warfarin, diclofenac, phenytoin, tolbutamide and losartan. DE5IED8 KD 33208: Metazoa DE5IED8 PL 7711: Chordata DE5IED8 CL 40674: Mammalia DE5IED8 OD 9443: Primates DE5IED8 FM 9604: Hominidae DE5IED8 GE 9605: Homo DE5IED8 SP 9606: Homo sapiens DE6OQ3W ID DE6OQ3W DE6OQ3W DN Cytochrome P450 1A1 (CYP1A1) DE6OQ3W GN CYP1A1 DE6OQ3W SN Cytochrome P450 family 1 subfamily A member 1; Hydroperoxy icosatetraenoate dehydratase; Cytochrome P450-C; Cytochrome P450-P1; Cytochrome P450 form 6; CYP1A1; CYPIA1 DE6OQ3W UC CP1A1_HUMAN DE6OQ3W RD Prazosin DE6OQ3W GI 1543 DE6OQ3W E1 1: Oxidoreductase DE6OQ3W E2 1.14: Oxygen paired donor oxidoreductase DE6OQ3W E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE6OQ3W EC 1.14.14.1 DE6OQ3W RC Biosynthesis of protectins:R-HSA-9018681; PPARA activates gene expression:R-HSA-1989781; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE):R-HSA-2142816; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET):R-HSA-2142670; Xenobiotics:R-HSA-211981 DE6OQ3W KG Chemical carcinogenesis:hsa05204; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Ovarian steroidogenesis:hsa04913; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140; Tryptophan metabolism:hsa00380 DE6OQ3W PD 4I8V; 6DWM; 6DWN DE6OQ3W SQ MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPHLALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQSMSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAGPGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPILRYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANVQLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLSDRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKLWVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEFSVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS DE6OQ3W TD Primarily distributed in liver, lung and urinary bladder. DE6OQ3W FC This enzyme is involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. It catalyzes the hydroxylation of carbon-hydrogen bonds and exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16- alpha positions. It also displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation and Catalyzes the epoxidation of double bonds of certain PUFA. DE6OQ3W KD 33208: Metazoa DE6OQ3W PL 7711: Chordata DE6OQ3W CL 40674: Mammalia DE6OQ3W OD 9443: Primates DE6OQ3W FM 9604: Hominidae DE6OQ3W GE 9605: Homo DE6OQ3W SP 9606: Homo sapiens DEYGVN4 ID DEYGVN4 DEYGVN4 DN UDP-glucuronosyltransferase 1A1 (UGT1A1) DEYGVN4 GN UGT1A1 DEYGVN4 SN UDP-glucuronosyltransferase family 1 member A1; UDP-glucuronosyltransferase 1-A; UDP-glucuronosyltransferase 1-1; Bilirubin-specific UDPGT isozyme 1; UDPGT 1-1; UGT-1A; GNT1; UGT1; UGT1*1; UGT1-01; UGT1.1; UGT1A; UGT1A1; hUG-BR1 DEYGVN4 UC UD11_HUMAN DEYGVN4 RD Diflunisal DEYGVN4 GI 54658 DEYGVN4 E1 2: Transferase DEYGVN4 E2 2.4: Glycosyltransferases DEYGVN4 E3 2.4.1: Hexosyltransferase DEYGVN4 EC 2.4.1.17 DEYGVN4 RC Defective UGT1A1 causes hyperbilirubinemia:R-HSA-5579002; Glucuronidation:R-HSA-156588 DEYGVN4 KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEYGVN4 SQ MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVLAPDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDSAMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLEFEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQREVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH DEYGVN4 TD Primarily distributed in intestine and liver. DEYGVN4 FC This enzyme catalyzes the glucuronidation of 17beta-estradiol, 17alpha-ethinylestradiol, 1-hydroxypyrene, 4-methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone. DEYGVN4 KD 33208: Metazoa DEYGVN4 PL 7711: Chordata DEYGVN4 CL 40674: Mammalia DEYGVN4 OD 9443: Primates DEYGVN4 FM 9604: Hominidae DEYGVN4 GE 9605: Homo DEYGVN4 SP 9606: Homo sapiens DE4ZHS1 ID DE4ZHS1 DE4ZHS1 DN Glutathione S-transferase alpha-1 (GSTA1) DE4ZHS1 GN GSTA1 DE4ZHS1 SN Glutathione S-transferase A1; Androst-5-ene-3,17-dione isomerase; 13-hydroperoxyoctadecadienoate peroxidase; GST HA subunit 1; GST class-alpha member 1; GST-epsilon; N-terminally processed glutathione S-transferase A1; GSTA1; GSTA1-1; GTH1 DE4ZHS1 UC GSTA1_HUMAN DE4ZHS1 RD Cisplatin DE4ZHS1 GI 2938 DE4ZHS1 E1 2: Transferase DE4ZHS1 E2 2.5: Alkyl/aryl transferase DE4ZHS1 E3 2.5.1: Alkyl/aryl transferase DE4ZHS1 EC 2.5.1.18 DE4ZHS1 RC Glutathione conjugation:R-HSA-156590 DE4ZHS1 KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DE4ZHS1 PD 1GSF; 1GUH; 1K3L; 1K3O; 1K3Y; 1LBK; 1PKW; 1PKZ; 1PL1 DE4ZHS1 SQ MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF DE4ZHS1 TD Primarily distributed in adrenal gland, intestine, kidney, liver and testis. DE4ZHS1 FC This enzyme catalyzes the isomerization of D5-androstene-3,17-dione (AD) into D4-androstene- 3,17-dione. Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)- hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE, it is also involved in the metabolism of oxidized linoleic acid. DE4ZHS1 KD 33208: Metazoa DE4ZHS1 PL 7711: Chordata DE4ZHS1 CL 40674: Mammalia DE4ZHS1 OD 9443: Primates DE4ZHS1 FM 9604: Hominidae DE4ZHS1 GE 9605: Homo DE4ZHS1 SP 9606: Homo sapiens DEGTFWK ID DEGTFWK DEGTFWK DN Mephenytoin 4-hydroxylase (CYP2C19) DEGTFWK GN CYP2C19 DEGTFWK SN Fenbendazole monooxygenase (4'-hydroxylating); Cytochrome P450 2C19; Cytochrome P450-11A; Cytochrome P450-254C; CYP2C19; CYPIIC17; CYPIIC19 DEGTFWK UC CP2CJ_HUMAN DEGTFWK RD Glipizide DEGTFWK GI 1557 DEGTFWK E1 1: Oxidoreductase DEGTFWK E2 1.14: Oxygen paired donor oxidoreductase DEGTFWK E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEGTFWK EC 1.14.14.1 DEGTFWK RC CYP2E1 reactions:R-HSA-211999; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE):R-HSA-2142816; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET):R-HSA-2142670; Xenobiotics:R-HSA-211981 DEGTFWK KG Arachidonic acid metabolism:hsa00590; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Linoleic acid metabolism:hsa00591; Metabolic pathways:hsa01100; Serotonergic synapse:hsa04726 DEGTFWK PD 4GQS DEGTFWK SQ MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKIYGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICSIIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFMESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTETTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYIDLIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFKKSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVPPFYQLCFIPV DEGTFWK TD Primarily distributed in intestine and liver. DEGTFWK FC This enzyme is involved in the metabolism of polyunsaturated fatty acids (PUFA). It catalyzes the hydroxylation of carbon-hydrogen bonds and hydroxylates PUFA specifically at the omega-1 position. Besides, it also catalyzes the epoxidation of double bonds of PUFA and metabolizes plant monoterpenes such as limonene. It is also responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine. DEGTFWK KD 33208: Metazoa DEGTFWK PL 7711: Chordata DEGTFWK CL 40674: Mammalia DEGTFWK OD 9443: Primates DEGTFWK FM 9604: Hominidae DEGTFWK GE 9605: Homo DEGTFWK SP 9606: Homo sapiens DEJVYAZ ID DEJVYAZ DEJVYAZ DN Cytochrome P450 2A6 (CYP2A6) DEJVYAZ GN CYP2A6 DEJVYAZ SN Cytochrome P450 family 2 subfamily A member 6; Coumarin 7-hydroxylase; Cytochrome P450 IIA3; Cytochrome P450(I); CYP2A3; CYP2A6; CYPIIA6 DEJVYAZ UC CP2A6_HUMAN DEJVYAZ RD Clofibrate DEJVYAZ GI 1548 DEJVYAZ E1 1: Oxidoreductase DEJVYAZ E2 1.14: Oxygen paired donor oxidoreductase DEJVYAZ E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEJVYAZ EC 1.14.14.1 DEJVYAZ RC CYP2E1 reactions:R-HSA-211999; Xenobiotics:R-HSA-211981 DEJVYAZ KG Caffeine metabolism:hsa00232; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830 DEJVYAZ PD 2FDU; 2FDV; 2FDW; 2FDY; 3EBS; 3T3Q; 3T3R; 4EJJ; 4RUI DEJVYAZ SQ MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSNGERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSNVISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQLLQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFIGGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEKGQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGFATIPRNYTMSFLPR DEJVYAZ TD Primarily distributed in liver. DEJVYAZ FC This enzyme exhibits a high coumarin 7-hydroxylase activity. It can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. It is also competent in the metabolic activation of aflatoxin B1. DEJVYAZ KD 33208: Metazoa DEJVYAZ PL 7711: Chordata DEJVYAZ CL 40674: Mammalia DEJVYAZ OD 9443: Primates DEJVYAZ FM 9604: Hominidae DEJVYAZ GE 9605: Homo DEJVYAZ SP 9606: Homo sapiens DEJGDUW ID DEJGDUW DEJGDUW DN Cytochrome P450 1A2 (CYP1A2) DEJGDUW GN CYP1A2 DEJGDUW SN Cytochrome P450 family 1 subfamily A member 2; Cytochrome P450 4; Cytochrome P450-P3; Cytochrome P(3)450; CYP1A2; CYPIA2 DEJGDUW UC CP1A2_HUMAN DEJGDUW RD Aprepitant DEJGDUW GI 1544 DEJGDUW E1 1: Oxidoreductase DEJGDUW E2 1.14: Oxygen paired donor oxidoreductase DEJGDUW E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEJGDUW EC 1.14.14.1 DEJGDUW RC Aflatoxin activation and detoxification:R-HSA-5423646; Aromatic amines can be N-hydroxylated or N-dealkylated by CYP1A2:R-HSA-211957; Biosynthesis of maresin-like SPMs:R-HSA-9027307; Biosynthesis of protectins:R-HSA-9018681; Methylation:R-HSA-156581; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE):R-HSA-2142816; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET):R-HSA-2142670 DEJGDUW KG Caffeine metabolism:hsa00232; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Linoleic acid metabolism:hsa00591; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140; Tryptophan metabolism:hsa00380 DEJGDUW PD 2HI4 DEJGDUW SQ MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLSDRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPELWEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHVQARLRFSIN DEJGDUW TD Primarily distributed in liver. DEJGDUW FC This enzyme is involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. It catalyzes the hydroxylation of carbon-hydrogen bonds and exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta- estradiol (E2), namely 2-hydroxy E1 and E2. It metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. It also plays a role in the oxidative metabolism of xenobiotics and catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Specificlly, it metabolizes caffeine via N3-demethylation. DEJGDUW KD 33208: Metazoa DEJGDUW PL 7711: Chordata DEJGDUW CL 40674: Mammalia DEJGDUW OD 9443: Primates DEJGDUW FM 9604: Hominidae DEJGDUW GE 9605: Homo DEJGDUW SP 9606: Homo sapiens DEIBDNY ID DEIBDNY DEIBDNY DN Cytochrome P450 3A5 (CYP3A5) DEIBDNY GN CYP3A5 DEIBDNY SN Cytochrome P450 family 3 subfamily A member 5; Cytochrome P450-PCN3; CYP3A5; CYPIIIA5 DEIBDNY UC CP3A5_HUMAN DEIBDNY RD Lorlatinib DEIBDNY GI 1577 DEIBDNY E1 1: Oxidoreductase DEIBDNY E2 1.14: Oxygen paired donor oxidoreductase DEIBDNY E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEIBDNY EC 1.14.14.1 DEIBDNY RC Aflatoxin activation and detoxification:R-HSA-5423646; Xenobiotics:R-HSA-211981 DEIBDNY KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEIBDNY PD 5VEU DEIBDNY SQ MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKFDTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISLAEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYSMDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSLFPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSIIFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVVNETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFSKKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQGLLQPEKPIVLKVDSRDGTLSGE DEIBDNY TD Primarily distributed in intestine, liver and stomach. DEIBDNY FC This enzyme is involved in the metabolism of steroid hormones and vitamins. It catalyzes the hydroxylation of carbon-hydrogen bonds and exhibits high catalytic activity for the formation of catechol estrogens from 17beta- estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2. It also catalyzes 6beta-hydroxylation of the steroid hormones testosterone, progesterone, and androstenedione and the oxidative conversion of all-trans- retinol to all-trans-retinal. It further metabolizes all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in hepatic atRA clearance. It is also involved in the oxidative metabolism of xenobiotics, including calcium channel blocking drug nifedipine and immunosuppressive drug cyclosporine. DEIBDNY KD 33208: Metazoa DEIBDNY PL 7711: Chordata DEIBDNY CL 40674: Mammalia DEIBDNY OD 9443: Primates DEIBDNY FM 9604: Hominidae DEIBDNY GE 9605: Homo DEIBDNY SP 9606: Homo sapiens DE9QHP6 ID DE9QHP6 DE9QHP6 DN Cytochrome P450 1B1 (CYP1B1) DE9QHP6 GN CYP1B1 DE9QHP6 SN Cytochrome P450 family 1 subfamily B member 1; P450 1B1; CP1B; GLC3A; P4501B1; ASGD6; CYP1B1; CYPIB1 DE9QHP6 UC CP1B1_HUMAN DE9QHP6 RD Progesterone DE9QHP6 GI 1545 DE9QHP6 E1 1: Oxidoreductase DE9QHP6 E2 1.14: Oxygen paired donor oxidoreductase DE9QHP6 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE9QHP6 EC 1.14.14.1 DE9QHP6 RC Defective CYP1B1 causes Glaucoma:R-HSA-5579000; Endogenous sterols:R-HSA-211976; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE):R-HSA-2142816; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET):R-HSA-2142670 DE9QHP6 KG Chemical carcinogenesis:hsa05204; Metabolism of xenobiotics by cytochrome P450:hsa00980; MicroRNAs in cancer:hsa05206; Ovarian steroidogenesis:hsa04913; Steroid hormone biosynthesis:hsa00140; Tryptophan metabolism:hsa00380 DE9QHP6 PD 3PM0; 6IQ5 DE9QHP6 SQ MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLIGNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAFASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVALLVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSLVDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSAEKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAELDQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVVFVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQLFLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKETCQ DE9QHP6 TD Primarily distributed in blood and lung. DE9QHP6 FC This enzyme is involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. It exhibits catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2- and 4-hydroxy E1 and E2 and displays a predominant hydroxylase activity toward E2 at the C-4 position. It metabolizes testosterone and progesterone to B or D ring hydroxylated metabolites. It catalyzes the epoxidation of double bonds of certain PUFA; converts arachidonic acid toward epoxyeicosatrienoic acid (EpETrE) regioisomers, 8,9-, 11,12-, and 14,15- EpETrE. Additionally, it displays dehydratase activity toward oxygenated eicosanoids hydroperoxyeicosatetraenoates (HpETEs). Also it is involved in the oxidative metabolism of xenobiotics, particularly converting polycyclic aromatic hydrocarbons and heterocyclic aryl amines procarcinogens to DNA-damaging products. DE9QHP6 KD 33208: Metazoa DE9QHP6 PL 7711: Chordata DE9QHP6 CL 40674: Mammalia DE9QHP6 OD 9443: Primates DE9QHP6 FM 9604: Hominidae DE9QHP6 GE 9605: Homo DE9QHP6 SP 9606: Homo sapiens DE492CE ID DE492CE DE492CE DN Prostaglandin G/H synthase 2 (COX-2) DE492CE GN PTGS2 DE492CE SN Prostaglandin H2 synthase 2; Prostaglandin-endoperoxide synthase 2; Cyclooxygenase-2; PGH synthase 2; COX-2; COX2; PGHS-2; PHS II; PTGS2 DE492CE UC PGH2_HUMAN DE492CE RD Etoposide DE492CE GI 5743 DE492CE E1 1: Oxidoreductase DE492CE E2 1.14: Oxygen paired donor oxidoreductase DE492CE E3 1.14.99: Oxygen paired donor oxidoreductase DE492CE EC 1.14.99.1 DE492CE RC Biosynthesis of DHA-derived SPMs:R-HSA-9018677; Biosynthesis of DPAn-3 SPMs:R-HSA-9025094; Biosynthesis of EPA-derived SPMs:R-HSA-9018679; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives:R-HSA-9027604; Interleukin-10 signaling:R-HSA-6783783; Interleukin-4 and Interleukin-13 signaling:R-HSA-6785807; Nicotinamide salvaging:R-HSA-197264; Synthesis of 15-eicosatetraenoic acid derivatives:R-HSA-2142770; Synthesis of Prostaglandins (PG) and Thromboxanes (TX):R-HSA-2162123 DE492CE KG Alzheimer's disease:hsa05010; Arachidonic acid metabolism:hsa00590; C-type lectin receptor signaling pathway:hsa04625; Chemical carcinogenesis:hsa05204; Human cytomegalovirus infection:hsa05163; Human papillomavirus infection:hsa05165; IL-17 signaling pathway:hsa04657; Kaposi sarcoma-associated herpesvirus infection:hsa05167; Leishmaniasis:hsa05140; Metabolic pathways:hsa01100; MicroRNAs in cancer:hsa05206; NF-kappa B signaling pathway:hsa04064; Ovarian steroidogenesis:hsa04913; Oxytocin signaling pathway:hsa04921; Pathways in cancer:hsa05200; Regulation of lipolysis in adipocytes:hsa04923; Retrograde endocannabinoid signaling:hsa04723; Serotonergic synapse:hsa04726; Small cell lung cancer:hsa05222; TNF signaling pathway:hsa04668; VEGF signaling pathway:hsa04370 DE492CE PD 1V0X; 5F19; 5F1A; 5IKQ; 5IKR; 5IKT; 5IKV; 5KIR DE492CE SQ MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADYGYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKYQIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRVAGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEVGFQIINTASIQSLICNNVKGCPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKERSTEL DE492CE TD Primarily distributed in ductus deferens and seminal vesicle. DE492CE FC This enzyme converts arachidonate to prostaglandin H2 (PGH2). DE492CE KD 33208: Metazoa DE492CE PL 7711: Chordata DE492CE CL 40674: Mammalia DE492CE OD 9443: Primates DE492CE FM 9604: Hominidae DE492CE GE 9605: Homo DE492CE SP 9606: Homo sapiens DEQX145 ID DEQX145 DEQX145 DN Aromatase (CYP19A1) DEQX145 GN CYP19A1 DEQX145 SN Cytochrome P-450AROM; Cytochrome P450 19A1; Estrogen synthase; ARO1; CYAR; CYP19; CYP19A1; CYPXIX DEQX145 UC CP19A_HUMAN DEQX145 RD Nandrolone DEQX145 GI 1588 DEQX145 E1 1: Oxidoreductase DEQX145 E2 1.14: Oxygen paired donor oxidoreductase DEQX145 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEQX145 EC 1.14.14.14 DEQX145 RC Defective CYP19A1 causes Aromatase excess syndrome (AEXS):R-HSA-5579030; Endogenous sterols:R-HSA-211976; Estrogen biosynthesis:R-HSA-193144 DEQX145 KG Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Steroid hormone biosynthesis:hsa00140 DEQX145 PD 3S79; 3S7S; 4GL5; 4GL7; 4KQ8; 5JKV; 5JKW; 5JL6; 5JL7 DEQX145 SQ MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLISHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDETKNMLEMIFTPRNSDRCLEH DEQX145 TD Primarily distributed in placenta. DEQX145 FC This enzyme catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively. It catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo/19-aldehyde derivatives, followed by a third oxidative aromatization step that involves C1-beta hydrogen abstraction combined with cleavage of the C10-C19 bond to yield a phenolic A ring and formic acid. Alternatively, the third oxidative reaction yields a 19-norsteroid and formic acid. Additionally, it converts dihydrotestosterone to delta1,10-dehydro 19- nordihydrotestosterone and also displays 2-hydroxylase activity toward estrone. DEQX145 KD 33208: Metazoa DEQX145 PL 7711: Chordata DEQX145 CL 40674: Mammalia DEQX145 OD 9443: Primates DEQX145 FM 9604: Hominidae DEQX145 GE 9605: Homo DEQX145 SP 9606: Homo sapiens DENP5RY ID DENP5RY DENP5RY DN Quinone reductase 1 (NQO1) DENP5RY GN NQO1 DENP5RY SN Menadione reductase; NAD(P)H dehydrogenase [quinone] 1; Azoreductase; DT-diaphorase; NAD(P)H:quinone oxidoreductase 1; Phylloquinone reductase; DIA4; DTD; QR1; NMOR1; NQO1 DENP5RY UC NQO1_HUMAN DENP5RY RD Carboplatin DENP5RY GI 1728 DENP5RY E1 1: Oxidoreductase DENP5RY E2 1.6: NADH/NADPH oxidoreductase DENP5RY E3 1.6.5: Quinone acceptor oxidoreductase DENP5RY EC 1.6.5.2 DENP5RY RC Regulation of ornithine decarboxylase (ODC):R-HSA-350562 DENP5RY KG Fluid shear stress and atherosclerosis:hsa05418; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Pathways in cancer:hsa05200; Ubiquinone and other terpenoid-quinone biosynthesis:hsa00130 DENP5RY PD 1GG5; 1H66; 1H69; 1KBO; 1KBQ; 1QBG; 2F1O; 3JSX; 4CET DENP5RY SQ MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVFIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKKEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK DENP5RY TD Primarily distributed in stomach. DENP5RY FC This enzyme serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways. DENP5RY KD 33208: Metazoa DENP5RY PL 7711: Chordata DENP5RY CL 40674: Mammalia DENP5RY OD 9443: Primates DENP5RY FM 9604: Hominidae DENP5RY GE 9605: Homo DENP5RY SP 9606: Homo sapiens DEPKLMQ ID DEPKLMQ DEPKLMQ DN Cytochrome P450 2B6 (CYP2B6) DEPKLMQ GN CYP2B6 DEPKLMQ SN Cytochrome P450 family 2 subfamily B member 6; Cytochrome P450 IIB1; CYP2B6; CYPIIB6 DEPKLMQ UC CP2B6_HUMAN DEPKLMQ RD Hydrocodone bitartrate DEPKLMQ GI 1555 DEPKLMQ E1 1: Oxidoreductase DEPKLMQ E2 1.14: Oxygen paired donor oxidoreductase DEPKLMQ E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEPKLMQ EC 1.14.14.1 DEPKLMQ RC CYP2E1 reactions:R-HSA-211999; Fatty acids:R-HSA-211935; Xenobiotics:R-HSA-211981 DEPKLMQ KG Arachidonic acid metabolism:hsa00590; Drug metabolism - cytochrome P450:hsa00982; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830 DEPKLMQ PD 3QU8; 3UA5; 4I91; 4RQL; 4RRT; 4ZV8; 5UAP; 5UDA; 5UEC DEPKLMQ SQ MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFREKYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNRWKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIICSIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQEINAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGTETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFSDLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGALKKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKIPPTYQIRFLPR DEPKLMQ TD Primarily distributed in liver, lung and heart right ventricle. DEPKLMQ FC This enzyme is involved in the metabolism of endocannabinoids and steroids. It catalyzes the epoxidation of double bonds of arachidonoylethanolamide (anandamide) to 8,9-, 11,12-, and 14,15- epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs). It hydroxylates steroid hormones, including testosterone at C-16 and estrogens at C-2 and plays a role in the oxidative metabolism of xenobiotics, including plant lipids and drugs. DEPKLMQ KD 33208: Metazoa DEPKLMQ PL 7711: Chordata DEPKLMQ CL 40674: Mammalia DEPKLMQ OD 9443: Primates DEPKLMQ FM 9604: Hominidae DEPKLMQ GE 9605: Homo DEPKLMQ SP 9606: Homo sapiens DEXISVQ ID DEXISVQ DEXISVQ DN Asparagine synthetase (ASNS) DEXISVQ GN ASNS DEXISVQ SN Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; ASNS; TS11 DEXISVQ UC ASNS_HUMAN DEXISVQ RD L-glutamine DEXISVQ GI 440 DEXISVQ E1 6: Ligase DEXISVQ E2 6.3: Carbon-nitrogen ligase DEXISVQ E3 6.3.5: Carbon-nitrogen ligase DEXISVQ EC 6.3.5.4 DEXISVQ RC ATF4 activates genes in response to endoplasmic reticulum stress:R-HSA-380994; Aspartate and asparagine metabolism:R-HSA-8963693 DEXISVQ KG Alanine, aspartate and glutamate metabolism:hsa00250; Biosynthesis of amino acids:hsa01230; Metabolic pathways:hsa01100 DEXISVQ PD 6GQ3 DEXISVQ SQ MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPKWINATDPSARTLTHYKSAVKA DEXISVQ TD Primarily distributed in pancreas. DEXISVQ FC This enzyme is a chiefly cytoplasmic enzyme that generates asparagine from aspartate. DEXISVQ KD 33208: Metazoa DEXISVQ PL 7711: Chordata DEXISVQ CL 40674: Mammalia DEXISVQ OD 9443: Primates DEXISVQ FM 9604: Hominidae DEXISVQ GE 9605: Homo DEXISVQ SP 9606: Homo sapiens DES5XRU ID DES5XRU DES5XRU DN Cytochrome P450 2C8 (CYP2C8) DES5XRU GN CYP2C8 DES5XRU SN Cytochrome P450 family 2 subfamily C member 8; Cytochrome P450 IIC2; Cytochrome P450 MP-12; Cytochrome P450 MP-20; Cytochrome P450 form 1; S-mephenytoin 4-hydroxylase; CYP2C8; CYPIIC8 DES5XRU UC CP2C8_HUMAN DES5XRU RD Lorlatinib DES5XRU GI 1558 DES5XRU E1 1: Oxidoreductase DES5XRU E2 1.14: Oxygen paired donor oxidoreductase DES5XRU E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DES5XRU EC 1.14.14.1 DES5XRU RC Biosynthesis of maresin-like SPMs:R-HSA-9027307; CYP2E1 reactions:R-HSA-211999; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE):R-HSA-2142816; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET):R-HSA-2142670; Xenobiotics:R-HSA-211981 DES5XRU KG Arachidonic acid metabolism:hsa00590; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Linoleic acid metabolism:hsa00591; Metabolic pathways:hsa01100; Retinol metabolism:hsa00830; Serotonergic synapse:hsa04726 DES5XRU PD 1PQ2; 2NNH; 2NNI; 2NNJ; 2VN0 DES5XRU SQ MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKVYGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRWKEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICSVVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALTRSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSDLVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLPPSYQICFIPV DES5XRU TD Primarily distributed in liver. DES5XRU FC This enzyme is involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. It primarily catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) with a preference for the last double bond and catalyzes the hydroxylation of carbon-hydrogen bonds. It also metabolizes all trans-retinoic acid toward its 4-hydroxylated form and displays 16-alpha hydroxylase activity toward estrogen steroid hormones, 17beta-estradiol (E2) and estrone (E1). In addition, it plays a role in the oxidative metabolism of xenobiotics. It is the principal enzyme responsible for the metabolism of the anti-cancer drug paclitaxel (taxol). DES5XRU KD 33208: Metazoa DES5XRU PL 7711: Chordata DES5XRU CL 40674: Mammalia DES5XRU OD 9443: Primates DES5XRU FM 9604: Hominidae DES5XRU GE 9605: Homo DES5XRU SP 9606: Homo sapiens DE98XPV ID DE98XPV DE98XPV DN Cholesterol desmolase (CYP11A1) DE98XPV GN CYP11A1 DE98XPV SN Cytochrome P450 11A1; Cytochrome P450(scc); Mitochondrial cholesterol side-chain cleavage enzyme; CYP11A; CYP11A1; CYPXIA1 DE98XPV UC CP11A_HUMAN DE98XPV RD Vitamin D DE98XPV GI 1583 DE98XPV E1 1: Oxidoreductase DE98XPV E2 1.14: Oxygen paired donor oxidoreductase DE98XPV E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE98XPV EC 1.14.15.6 DE98XPV RC Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR):R-HSA-5579026; Endogenous sterols:R-HSA-211976; Pregnenolone biosynthesis:R-HSA-196108 DE98XPV KG Aldosterone synthesis and secretion:hsa04925; Cortisol synthesis and secretion:hsa04927; Cushing syndrome:hsa04934; Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Steroid hormone biosynthesis:hsa00140 DE98XPV PD 3N9Y; 3N9Z; 3NA0; 3NA1 DE98XPV SQ MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRGILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAARHQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIYALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINMLENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ DE98XPV TD Primarily distributed in adrenal gland and placenta. DE98XPV FC This enzyme catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones. It catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R- hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal. DE98XPV KD 33208: Metazoa DE98XPV PL 7711: Chordata DE98XPV CL 40674: Mammalia DE98XPV OD 9443: Primates DE98XPV FM 9604: Hominidae DE98XPV GE 9605: Homo DE98XPV SP 9606: Homo sapiens DEN0GVQ ID DEN0GVQ DEN0GVQ DN Beta-HSD adrenal and gonadal type (HSD3B2) DEN0GVQ GN HSD3B2 DEN0GVQ SN Progesterone reductase; 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2; 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II; 3-beta-HSD II; 3-beta-HSD adrenal and gonadal type; 3-beta-hydroxy-5-ene steroid dehydrogenase; 3-beta-hydroxy-Delta(5)-steroid dehydrogenase; HSD3B2; HSDB3B DEN0GVQ UC 3BHS2_HUMAN DEN0GVQ RD Norethindrone acetate DEN0GVQ GI 3284 DEN0GVQ E1 1: Oxidoreductase DEN0GVQ E2 1.1: CH-OH donor oxidoreductase DEN0GVQ E3 1.1.1: NAD/NADP oxidoreductase DEN0GVQ EC 1.1.1.145 DEN0GVQ RC Androgen biosynthesis:R-HSA-193048; Glucocorticoid biosynthesis:R-HSA-194002; Mineralocorticoid biosynthesis:R-HSA-193993 DEN0GVQ KG Aldosterone synthesis and secretion:hsa04925; Cortisol synthesis and secretion:hsa04927; Cushing syndrome:hsa04934; Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Steroid hormone biosynthesis:hsa00140 DEN0GVQ SQ MGWSCLVTGAGGLLGQRIVRLLVEEKELKEIRALDKAFRPELREEFSKLQNRTKLTVLEGDILDEPFLKRACQDVSVVIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLYTCALRPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALRDPKKAPSVRGQFYYISDDTPHQSYDNLNYILSKEFGLRLDSRWSLPLTLMYWIGFLLEVVSFLLSPIYSYQPPFNRHTVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLVDRHKETLKSKTQ DEN0GVQ TD Primarily distributed in adrenal gland, testis and ovary. DEN0GVQ FC This enzyme catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. DEN0GVQ KD 33208: Metazoa DEN0GVQ PL 7711: Chordata DEN0GVQ CL 40674: Mammalia DEN0GVQ OD 9443: Primates DEN0GVQ FM 9604: Hominidae DEN0GVQ GE 9605: Homo DEN0GVQ SP 9606: Homo sapiens DERD86B ID DERD86B DERD86B DN Cytochrome P450 3A7 (CYP3A7) DERD86B GN CYP3A7 DERD86B SN Cytochrome P450 family 3 subfamily A member 7; Cytochrome P450-HFLA; CYP3A7; CYPIIIA7; P450HLp2 DERD86B UC CP3A7_HUMAN DERD86B RD Atazanavir DERD86B GI 1551 DERD86B E1 1: Oxidoreductase DERD86B E2 1.14: Oxygen paired donor oxidoreductase DERD86B E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DERD86B EC 1.14.14.1 DERD86B RC Xenobiotics:R-HSA-211981 DERD86B KG Chemical carcinogenesis:hsa05204; Metabolic pathways:hsa01100; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DERD86B SQ MDLIPNLAVETWLLLAVSLILLYLYGTRTHGLFKKLGIPGPTPLPFLGNALSFRKGYWTFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGGLLLTEKPIVLKAESRDETVSGA DERD86B TD Primarily distributed in liver. DERD86B FC This enzyme is involved in the metabolism of steroid hormones and vitamins during embryogenesis. It catalyzes the hydroxylation of carbon-hydrogen bonds and metabolizes 3beta- hydroxyandrost-5-en-17-one (dehydroepiandrosterone, DHEA) and exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1), particularly D- ring hydroxylated estrone at the C16-alpha position. It mainly hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in atRA clearance during fetal development. And it is also involved in the oxidative metabolism of xenobiotics including anticonvulsants. DERD86B KD 33208: Metazoa DERD86B PL 7711: Chordata DERD86B CL 40674: Mammalia DERD86B OD 9443: Primates DERD86B FM 9604: Hominidae DERD86B GE 9605: Homo DERD86B SP 9606: Homo sapiens DEB3CV1 ID DEB3CV1 DEB3CV1 DN UDP-glucuronosyltransferase 2B7 (UGT2B7) DEB3CV1 GN UGT2B7 DEB3CV1 SN UDP-glucuronosyltransferase family 2 member B7; 3,4-catechol estrogen-specific UDPGT; UDP-glucuronosyltransferase 2B9; UDPGT 2B7; UDPGT 2B9; UDPGTh-2; UGT2B7; UGTB2B9 DEB3CV1 UC UD2B7_HUMAN DEB3CV1 RD Zidovudine DEB3CV1 GI 7364 DEB3CV1 E1 2: Transferase DEB3CV1 E2 2.4: Glycosyltransferases DEB3CV1 E3 2.4.1: Hexosyltransferase DEB3CV1 EC 2.4.1.17 DEB3CV1 RC Glucuronidation:R-HSA-156588 DEB3CV1 KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEB3CV1 PD 2O6L DEB3CV1 SQ MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSASILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFGDITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTFEKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVLGRPTTLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSGENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTMSSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND DEB3CV1 TD Primarily distributed in kidney and liver. DEB3CV1 FC This enzyme is uniquely specific for 3,4-catechol estrogens and estriol which suggests it may play an important role in regulating the level and activity of these potent and active estrogen metabolites. And it is also active with androsterone, hyodeoxycholic acid and tetrachlorocatechol (in vitro). DEB3CV1 KD 33208: Metazoa DEB3CV1 PL 7711: Chordata DEB3CV1 CL 40674: Mammalia DEB3CV1 OD 9443: Primates DEB3CV1 FM 9604: Hominidae DEB3CV1 GE 9605: Homo DEB3CV1 SP 9606: Homo sapiens DE073H6 ID DE073H6 DE073H6 DN Prostaglandin G/H synthase 1 (COX-1) DE073H6 GN PTGS1 DE073H6 SN Prostaglandin H2 synthase 1; Prostaglandin-endoperoxide synthase 1; Cyclooxygenase-1; PGH synthase 1; COX-1; COX1; PGHS-1; PHS 1; PTGS1 DE073H6 UC PGH1_HUMAN DE073H6 RD Candesartan cilexetil DE073H6 GI 5742 DE073H6 E1 1: Oxidoreductase DE073H6 E2 1.14: Oxygen paired donor oxidoreductase DE073H6 E3 1.14.99: Oxygen paired donor oxidoreductase DE073H6 EC 1.14.99.1 DE073H6 RC COX reactions:R-HSA-140180; Synthesis of Prostaglandins (PG) and Thromboxanes (TX):R-HSA-2162123 DE073H6 KG Arachidonic acid metabolism:hsa00590; Metabolic pathways:hsa01100; Platelet activation:hsa04611; Regulation of lipolysis in adipocytes:hsa04923; Serotonergic synapse:hsa04726 DE073H6 SQ MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTVRSNLIPSPPTYNSAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTEL DE073H6 TD Primarily distributed in smooth muscle and urinary bladder. DE073H6 FC This enzyme converts arachidonate to prostaglandin H2 (PGH2). DE073H6 KD 33208: Metazoa DE073H6 PL 7711: Chordata DE073H6 CL 40674: Mammalia DE073H6 OD 9443: Primates DE073H6 FM 9604: Hominidae DE073H6 GE 9605: Homo DE073H6 SP 9606: Homo sapiens DE3C1JY ID DE3C1JY DE3C1JY DN Nitric oxide synthase inducible (NOS2) DE3C1JY GN NOS2 DE3C1JY SN Peptidyl-cysteine S-nitrosylase NOS2; Hepatocyte NOS; Inducible nitric oxide synthase; Inducible NO synthase; Inducible NOS; NOS2A; NOS type II; NOS2; HEP-NOS; iNOS DE3C1JY UC NOS2_HUMAN DE3C1JY RD Doxorubicin DE3C1JY GI 4843 DE3C1JY E1 1: Oxidoreductase DE3C1JY E2 1.14: Oxygen paired donor oxidoreductase DE3C1JY E3 1.14.13: NADH/NADPH donor oxidoreductase DE3C1JY EC 1.14.13.39 DE3C1JY RC Interleukin-4 and Interleukin-13 signaling:R-HSA-6785807; Nitric oxide stimulates guanylate cyclase:R-HSA-392154; Peroxisomal protein import:R-HSA-9033241; ROS and RNS production in phagocytes:R-HSA-1222556 DE3C1JY KG Alzheimer's disease:hsa05010; Amoebiasis:hsa05146; Apelin signaling pathway:hsa04371; Arginine and proline metabolism:hsa00330; Arginine biosynthesis:hsa00220; Calcium signaling pathway:hsa04020; Chagas disease (American trypanosomiasis):hsa05142; HIF-1 signaling pathway:hsa04066; Leishmaniasis:hsa05140; Metabolic pathways:hsa01100; Pathways in cancer:hsa05200; Peroxisome:hsa04146; Pertussis:hsa05133; Relaxin signaling pathway:hsa04926; Small cell lung cancer:hsa05222; Toxoplasmosis:hsa05145; Tuberculosis:hsa05152 DE3C1JY PD 1NSI; 2LL6; 2NSI; 3E7G; 3EJ8; 4CX7; 4NOS; 5TP6; 5XN3 DE3C1JY SQ MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPLVETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVTILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPGNGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGDELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDLSKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQPALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQLLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQLPILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCFVRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPDEDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLYVCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDRVAVQPSSLEMSAL DE3C1JY TD Primarily distributed in liver, retina, intestine and lymphoid tissue. DE3C1JY FC This enzyme has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. DE3C1JY KD 33208: Metazoa DE3C1JY PL 7711: Chordata DE3C1JY CL 40674: Mammalia DE3C1JY OD 9443: Primates DE3C1JY FM 9604: Hominidae DE3C1JY GE 9605: Homo DE3C1JY SP 9606: Homo sapiens DE85D2P ID DE85D2P DE85D2P DN UDP-glucuronosyltransferase 1A9 (UGT1A9) DE85D2P GN UGT1A9 DE85D2P SN UDP-glucuronosyltransferase family 1 member A9; UDP-glucuronosyltransferase 1-I; UDP-glucuronosyltransferase 1-9; UDPGT 1-9; UGT-1I; UGT1*9; UGT1-09; UGT1.9; UGT1A9; UGT1I; lugP4 DE85D2P UC UD19_HUMAN DE85D2P RD Regorafenib DE85D2P GI 54600 DE85D2P E1 2: Transferase DE85D2P E2 2.4: Glycosyltransferases DE85D2P E3 2.4.1: Hexosyltransferase DE85D2P EC 2.4.1.17 DE85D2P RC Glucuronidation:R-HSA-156588; PPARA activates gene expression:R-HSA-1989781 DE85D2P KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DE85D2P SQ MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMPEVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLFFSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEGAQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVTEYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH DE85D2P TD Primarily distributed in liver and kidney. DE85D2P FC This enzyme has specificity for phenols. DE85D2P KD 33208: Metazoa DE85D2P PL 7711: Chordata DE85D2P CL 40674: Mammalia DE85D2P OD 9443: Primates DE85D2P FM 9604: Hominidae DE85D2P GE 9605: Homo DE85D2P SP 9606: Homo sapiens DE708H2 ID DE708H2 DE708H2 DN Nitric oxide synthase endothelial (NOS3) DE708H2 GN NOS3 DE708H2 SN Peptidyl-cysteine S-nitrosylase NOS3; Endothelial NOS; Endothelial nitric oxide synthase; EC-NOS; cNOS; eNOS; NOS type III; NOS3; NOSIII DE708H2 UC NOS3_HUMAN DE708H2 RD Doxorubicin DE708H2 GI 4846 DE708H2 E1 1: Oxidoreductase DE708H2 E2 1.14: Oxygen paired donor oxidoreductase DE708H2 E3 1.14.13: NADH/NADPH donor oxidoreductase DE708H2 EC 1.14.13.39 DE708H2 RC Extra-nuclear estrogen signaling:R-HSA-9009391; NOSIP mediated eNOS trafficking:R-HSA-203754; NOSTRIN mediated eNOS trafficking:R-HSA-203641; Nitric oxide stimulates guanylate cyclase:R-HSA-392154; ROS and RNS production in phagocytes:R-HSA-1222556; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation:R-HSA-1474151; VEGFR2 mediated vascular permeability:R-HSA-5218920; eNOS activation:R-HSA-203615 DE708H2 KG AGE-RAGE signaling pathway in diabetic complications:hsa04933; Apelin signaling pathway:hsa04371; Arginine and proline metabolism:hsa00330; Arginine biosynthesis:hsa00220; Calcium signaling pathway:hsa04020; Estrogen signaling pathway:hsa04915; Fluid shear stress and atherosclerosis:hsa05418; HIF-1 signaling pathway:hsa04066; Insulin resistance:hsa04931; Metabolic pathways:hsa01100; Oxytocin signaling pathway:hsa04921; PI3K-Akt signaling pathway:hsa04151; Platelet activation:hsa04611; Relaxin signaling pathway:hsa04926; Sphingolipid signaling pathway:hsa04071; VEGF signaling pathway:hsa04370; cGMP-PKG signaling pathway:hsa04022 DE708H2 PD 1M9M; 1M9Q; 1M9R; 1NIW; 2LL7; 2MG5; 2N8J; 3EAH; 3NOS DE708H2 SQ MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLTQPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAPEQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDDPPELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWKGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAARDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATILVRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGPPPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRYEEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVLAYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAPFRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSREPDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDTNSP DE708H2 TD Primarily distributed in lymphoid, placenta, liver and kidney. DE708H2 FC This enzyme is one of three isoforms that synthesize nitric oxide (NO). It is a dimer containing two identical monomers of 134 kD constituted by a reductase domain, which displays binding sites for nicotinamide adenine dinucleotide phosphate (NADPH), flavin mononucleotide (FMN), and flavin adenine dinucleotide (FAD), and an oxidase domain, which displays binding sites for heme group, zinc, the cofactor tetrahydrobiopterin (BH4), and the substrate L-arginine. NO is synthesized by eNOS from L-arginine and molecular oxygen, which binds to the heme group of eNOS, is reduced and finally incorporated into L-arginine to form NO and L-citrulline. DE708H2 KD 33208: Metazoa DE708H2 PL 7711: Chordata DE708H2 CL 40674: Mammalia DE708H2 OD 9443: Primates DE708H2 FM 9604: Hominidae DE708H2 GE 9605: Homo DE708H2 SP 9606: Homo sapiens DEB30C5 ID DEB30C5 DEB30C5 DN Carboxylesterase 1 (CES1) DEB30C5 GN CES1 DEB30C5 SN Liver carboxylesterase 1; Methylumbelliferyl-acetate deacetylase 1; Monocyte/macrophage serine esterase; Acyl-coenzyme A:cholesterol acyltransferase; Brain carboxylesterase hBr1; Cocaine carboxylesterase; Egasyn; Retinyl ester hydrolase; Serine esterase 1; TGH; Triacylglycerol hydrolase; hCE-1; ACAT; CE-1; CES1; HMSE; REH; SES1 DEB30C5 UC EST1_HUMAN DEB30C5 RD Irinotecan hydrochloride DEB30C5 GI 1066 DEB30C5 E1 3: Hydrolases DEB30C5 E2 3.1: Ester bond hydrolase DEB30C5 E3 3.1.1: Carboxylic ester hydrolase DEB30C5 EC 3.1.1.1 DEB30C5 RC Metabolism of Angiotensinogen to Angiotensins:R-HSA-2022377; Phase I - Functionalization of compounds:R-HSA-211945 DEB30C5 KG Drug metabolism - other enzymes:hsa00983 DEB30C5 PD 1MX9; 1YA4; 1YA8; 1YAH; 1YAJ; 2DQY; 2DQZ; 2DR0; 2H7C DEB30C5 SQ MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIPMQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLKDKEVAFWTNLFAKKAVEKPPQTEHIEL DEB30C5 TD Primarily distributed in liver with lower levels in heart and lung. DEB30C5 FC This enzyme is involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. It hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. It also hydrolyzes the methyl ester group of cocaine to form benzoylecgonine and catalyzes the transesterification of cocaine to form cocaethylene. DEB30C5 KD 33208: Metazoa DEB30C5 PL 7711: Chordata DEB30C5 CL 40674: Mammalia DEB30C5 OD 9443: Primates DEB30C5 FM 9604: Hominidae DEB30C5 GE 9605: Homo DEB30C5 SP 9606: Homo sapiens DE0P6LK ID DE0P6LK DE0P6LK DN Sulfotransferase 2A1 (SULT2A1) DE0P6LK GN SULT2A1 DE0P6LK SN Sulfotransferase family cytosolic 2A member 1; Bile salt sulfotransferase; Dehydroepiandrosterone sulfotransferase; Hydroxysteroid Sulfotransferase; DHEA-ST; HST; ST2; ST2A1; ST2A3; STD; SULT2A1 DE0P6LK UC ST2A1_HUMAN DE0P6LK RD Abiraterone acetate DE0P6LK GI 6822 DE0P6LK E1 2: Transferase DE0P6LK E2 2.8: Sulfotransferase DE0P6LK E3 2.8.2: Sulfotransferase DE0P6LK EC 2.8.2.14 DE0P6LK RC Cytosolic sulfonation of small molecules:R-HSA-156584; PPARA activates gene expression:R-HSA-1989781 DE0P6LK KG Bile secretion:hsa04976; Chemical carcinogenesis:hsa05204; Metabolism of xenobiotics by cytochrome P450:hsa00980 DE0P6LK PD 1EFH; 1J99; 1OV4; 2QP3; 2QP4; 3F3Y; 4IFB DE0P6LK SQ MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSKGDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLMRNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFLLLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVVDKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE DE0P6LK TD Primarily distributed in liver and adrenal. Also expressed at lower level in kidney. DE0P6LK FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands. DE0P6LK KD 33208: Metazoa DE0P6LK PL 7711: Chordata DE0P6LK CL 40674: Mammalia DE0P6LK OD 9443: Primates DE0P6LK FM 9604: Hominidae DE0P6LK GE 9605: Homo DE0P6LK SP 9606: Homo sapiens DE3N2FM ID DE3N2FM DE3N2FM DN NADPH-cytochrome P450 reductase (CPR) DE3N2FM GN POR DE3N2FM SN NADPH--cytochrome P450 reductase; P450R; CPR; CYPOR; POR DE3N2FM UC NCPR_HUMAN DE3N2FM RD Daunorubicin DE3N2FM GI 5447 DE3N2FM E1 1: Oxidoreductase DE3N2FM E2 1.6: NADH/NADPH oxidoreductase DE3N2FM E3 1.6.2: Heme protein acceptor oxidoreductase DE3N2FM EC 1.6.2.4 DE3N2FM RC Cytochrome P450 - arranged by substrate type:R-HSA-211897 DE3N2FM PD 1B1C; 3FJO; 3QE2; 3QFC; 3QFR; 3QFS; 3QFT; 5EMN; 5FA6 DE3N2FM SQ MGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTLTSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEHFNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWPAVCEHFGVEATGEESSIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHPFPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWVVEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYETKAGRINKGVATNWLRAKEPAGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPFIGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQSHKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVDYIKKLMTKGRYSLDVWS DE3N2FM TD Primarily distributed in liver. DE3N2FM FC This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes and can also provide electron transfer to heme oxygenase and cytochrome B5. DE3N2FM KD 33208: Metazoa DE3N2FM PL 7711: Chordata DE3N2FM CL 40674: Mammalia DE3N2FM OD 9443: Primates DE3N2FM FM 9604: Hominidae DE3N2FM GE 9605: Homo DE3N2FM SP 9606: Homo sapiens DEYWLRK ID DEYWLRK DEYWLRK DN Sulfotransferase 1A1 (SULT1A1) DEYWLRK GN SULT1A1 DEYWLRK SN Sulfotransferase family cytosolic 1A member 1; Aryl sulfotransferase 1A1; Aryl sulfotransferase 1; Thermostable phenol sulfotransferase; Phenol sulfotransferase 1; Phenol-sulfating phenol sulfotransferase 1; Ts-PST; HAST1/HAST2; OK/SW-cl.88; P-PST 1; ST1A1; STP; STP1; SULT1A1 DEYWLRK UC ST1A1_HUMAN DEYWLRK RD Liothyronine DEYWLRK GI 6817 DEYWLRK E1 2: Transferase DEYWLRK E2 2.8: Sulfotransferase DEYWLRK E3 2.8.2: Sulfotransferase DEYWLRK EC 2.8.2.1 DEYWLRK RC Cytosolic sulfonation of small molecules:R-HSA-156584 DEYWLRK KG Chemical carcinogenesis:hsa05204 DEYWLRK PD 2D06; 3QVU; 3QVV; 3U3J; 3U3K; 3U3M; 3U3O; 3U3R; 4GRA DEYWLRK SQ MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKAPGIPSGMETLKDTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVHPEPGTWDSFLEKFMVGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDFVVQHTSFKEMKKNPMTNYTTVPQEFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL DEYWLRK TD Primarily distributed in liver. Also expressed in lung, adrenal, brain, platelets and skin. DEYWLRK FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. It also has estrogen sulfotransferase activity and is responsible for the sulfonation and activation of minoxidil. It mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products. DEYWLRK KD 33208: Metazoa DEYWLRK PL 7711: Chordata DEYWLRK CL 40674: Mammalia DEYWLRK OD 9443: Primates DEYWLRK FM 9604: Hominidae DEYWLRK GE 9605: Homo DEYWLRK SP 9606: Homo sapiens DERE4TU ID DERE4TU DERE4TU DN Monoamine oxidase type A (MAO-A) DERE4TU GN MAOA DERE4TU SN Amine oxidase [flavin-containing] A; Monoamine oxidase A; MAO-A; MAOA DERE4TU UC AOFA_HUMAN DERE4TU RD Sumatriptan succinate DERE4TU GI 4128 DERE4TU E1 1: Oxidoreductase DERE4TU E2 1.4: CH-NH2 donor oxidoreductase DERE4TU E3 1.4.3: Oxygen acceptor oxidoreductase DERE4TU EC 1.4.3.4 DERE4TU RC Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB:R-HSA-141333; Defective MAOA causes Brunner syndrome (BRUNS):R-HSA-5579012; Enzymatic degradation of Dopamine by monoamine oxidase:R-HSA-379398; Enzymatic degradation of dopamine by COMT:R-HSA-379397; Interleukin-4 and Interleukin-13 signaling:R-HSA-6785807; Metabolism of serotonin:R-HSA-380612; Norepinephrine Neurotransmitter Release Cycle:R-HSA-181430 DERE4TU KG Alcoholism:hsa05034; Amphetamine addiction:hsa05031; Arginine and proline metabolism:hsa00330; Cocaine addiction:hsa05030; Dopaminergic synapse:hsa04728; Drug metabolism - cytochrome P450:hsa00982; Glycine, serine and threonine metabolism:hsa00260; Histidine metabolism:hsa00340; Metabolic pathways:hsa01100; Phenylalanine metabolism:hsa00360; Serotonergic synapse:hsa04726; Tryptophan metabolism:hsa00380; Tyrosine metabolism:hsa00350 DERE4TU PD 1H8Q; 2BXR; 2BXS; 2Z5X; 2Z5Y DERE4TU SQ MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKDVPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS DERE4TU TD Primarily distributed in heart, liver, duodenum, blood vessels and kidney. DERE4TU FC This enzyme catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine. DERE4TU KD 33208: Metazoa DERE4TU PL 7711: Chordata DERE4TU CL 40674: Mammalia DERE4TU OD 9443: Primates DERE4TU FM 9604: Hominidae DERE4TU GE 9605: Homo DERE4TU SP 9606: Homo sapiens DEAWHS8 ID DEAWHS8 DEAWHS8 DN Aldehyde oxidase (AOX1) DEAWHS8 GN AOX1 DEAWHS8 SN Azaheterocycle hydroxylase; Aldehyde oxidase 1; AO; AOX1 DEAWHS8 UC AOXA_HUMAN DEAWHS8 RD Zaleplon DEAWHS8 GI 316 DEAWHS8 E1 1: Oxidoreductase DEAWHS8 E2 1.2: Aldehyde/oxo donor oxidoreductase DEAWHS8 E3 1.2.3: Oxygen acceptor oxidoreductase DEAWHS8 EC 1.2.3.1 DEAWHS8 RC Vitamins B6 activation to pyridoxal phosphate:R-HSA-964975 DEAWHS8 KG Drug metabolism - cytochrome P450:hsa00982; Jak-STAT signaling pathway:hsa04630; Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760; Retinol metabolism:hsa00830; Tryptophan metabolism:hsa00380; Tyrosine metabolism:hsa00350; Valine, leucine and isoleucine degradation:hsa00280; Vitamin B6 metabolism:hsa00750 DEAWHS8 PD 4UHW; 4UHX; 5EPG; 6Q6Q DEAWHS8 SQ MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPGMVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCCLDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSERMMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHAYNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHIISRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSRKWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKLIGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPVHYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYCDDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAEKFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPERKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKYIQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGEDMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKFPNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEIDQTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGSRAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETVPNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVGYFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAIDIGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSNTLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFTKMIPRDEPGSYVPWNVPI DEAWHS8 TD Primarily distributed in liver. Also expressed in adipose tissue and at lower levels in lung, skeletal muscle and pancreas. DEAWHS8 FC This enzyme has broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. It plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. It also participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. DEAWHS8 KD 33208: Metazoa DEAWHS8 PL 7711: Chordata DEAWHS8 CL 40674: Mammalia DEAWHS8 OD 9443: Primates DEAWHS8 FM 9604: Hominidae DEAWHS8 GE 9605: Homo DEAWHS8 SP 9606: Homo sapiens DEBS639 ID DEBS639 DEBS639 DN Vitamin D(3) 25-hydroxylase (CYP27A1) DEBS639 GN CYP27A1 DEBS639 SN Sterol 27-hydroxylase; Cytochrome P-450C27/25; Mitochondrial sterol 26-hydroxylase; Cytochrome P450 27; 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase; CYP27; CYP27A1 DEBS639 UC CP27A_HUMAN DEBS639 RD Doxercalciferol DEBS639 GI 1593 DEBS639 E1 1: Oxidoreductase DEBS639 E2 1.14: Oxygen paired donor oxidoreductase DEBS639 E3 1.14.15: Iron-sulfur protein donor oxidoreductase DEBS639 EC 1.14.15.15 DEBS639 RC Defective CYP27A1 causes Cerebrotendinous xanthomatosis (CTX):R-HSA-5578996; Endogenous sterols:R-HSA-211976; Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DEBS639 KG Cholesterol metabolism:hsa04979; Metabolic pathways:hsa01100; PPAR signaling pathway:hsa03320; Primary bile acid biosynthesis:hsa00120 DEBS639 PD 1MFX DEBS639 SQ MAALGCARLRWALRGAGRGLCPHGARAKAAIPAALPSDKATGAPGAGPGVRRRQRSLEEIPRLGQLRFFFQLFVQGYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQFLQRQC DEBS639 TD Primarily distributed in liver. DEBS639 FC This enzyme catalyzes regio- and stereospecific hydroxylation of cholesterol and its derivatives. It hydroxylates (with R stereochemistry) the terminal methyl group of cholesterol side-chain in a three step reaction to yield at first a C26 alcohol, then a C26 aldehyde and finally a C26 acid. It plays a role in cholestanol metabolism in the cerebellum. It also hydroxylates retinal 7- ketocholesterol, a noxious oxysterol with pro-inflammatory and pro- apoptotic effects, and may play a role in its elimination from the retinal pigment epithelium. It catalyzes 25-hydroxylation of vitamin D3 that is required for its conversion to a functionally active form. DEBS639 KD 33208: Metazoa DEBS639 PL 7711: Chordata DEBS639 CL 40674: Mammalia DEBS639 OD 9443: Primates DEBS639 FM 9604: Hominidae DEBS639 GE 9605: Homo DEBS639 SP 9606: Homo sapiens DEL5N6Y ID DEL5N6Y DEL5N6Y DN UDP-glucuronosyltransferase 1A10 (UGT1A10) DEL5N6Y GN UGT1A10 DEL5N6Y SN UDP-glucuronosyltransferase family 1 member A10; UDP-glucuronosyltransferase 1-J; UDP-glucuronosyltransferase 1-10; UDPGT 1-10; UGT-1J; UGT1*10; UGT1-10; UGT1.10; UGT1A10; UGT1J DEL5N6Y UC UD110_HUMAN DEL5N6Y RD Etodolac DEL5N6Y GI 54575 DEL5N6Y E1 2: Transferase DEL5N6Y E2 2.4: Glycosyltransferases DEL5N6Y E3 2.4.1: Hexosyltransferase DEL5N6Y EC 2.4.1.17 DEL5N6Y RC Glucuronidation:R-HSA-156588 DEL5N6Y KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEL5N6Y SQ MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEGAQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH DEL5N6Y TD Primarily distributed in liver, colon, esophagus, gallbladder, intestine and stomach. DEL5N6Y FC This enzyme is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. DEL5N6Y KD 33208: Metazoa DEL5N6Y PL 7711: Chordata DEL5N6Y CL 40674: Mammalia DEL5N6Y OD 9443: Primates DEL5N6Y FM 9604: Hominidae DEL5N6Y GE 9605: Homo DEL5N6Y SP 9606: Homo sapiens DEASG0Q ID DEASG0Q DEASG0Q DN Thymidylate synthase (TYMS) DEASG0Q GN TYMS DEASG0Q SN Dihydrofolate reductase-thymidylate synthase; OK/SW-cl.29; TS; TSase; TYMS DEASG0Q UC TYSY_HUMAN DEASG0Q RD Methotrexate DEASG0Q GI 7298 DEASG0Q E1 2: Transferase DEASG0Q E2 2.1: Methylase DEASG0Q E3 2.1.1: Methyltransferase DEASG0Q EC 2.1.1.45 DEASG0Q RC G1/S-Specific Transcription:R-HSA-69205; Interconversion of nucleotide di- and triphosphates:R-HSA-499943 DEASG0Q KG Antifolate resistance:hsa01523; Metabolic pathways:hsa01100; One carbon pool by folate:hsa00670; Pyrimidine metabolism:hsa00240 DEASG0Q PD 1JUJ; 1YPV; 2ONB; 2RD8; 3OB7; 4E28; 4FGT; 5X69; 6OJU DEASG0Q SQ MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV DEASG0Q TD Primarily distributed in bone marrow and lymphoid tissue. DEASG0Q FC This enzyme contributes to the de novo mitochondrial thymidylate biosynthesis pathway. DEASG0Q KD 33208: Metazoa DEASG0Q PL 7711: Chordata DEASG0Q CL 40674: Mammalia DEASG0Q OD 9443: Primates DEASG0Q FM 9604: Hominidae DEASG0Q GE 9605: Homo DEASG0Q SP 9606: Homo sapiens DEKEDRC ID DEKEDRC DEKEDRC DN Cytidine aminohydrolase (CDA) DEKEDRC GN CDA DEKEDRC SN Cytidine deaminase; Cytidine aminohydrolase/deaminase; CDA; CDD DEKEDRC UC CDD_HUMAN DEKEDRC RD Azacitidine DEKEDRC GI 978 DEKEDRC E1 3: Hydrolases DEKEDRC E2 3.5: Carbon-nitrogen hydrolase DEKEDRC E3 3.5.4: Cyclic amidine hydrolase DEKEDRC EC 3.5.4.5 DEKEDRC RC Neutrophil degranulation:R-HSA-6798695; Pyrimidine salvage:R-HSA-73614 DEKEDRC KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DEKEDRC PD 1MQ0 DEKEDRC SQ MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQKTQ DEKEDRC TD Primarily distributed in blood and bone marrow. DEKEDRC FC This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. DEKEDRC KD 33208: Metazoa DEKEDRC PL 7711: Chordata DEKEDRC CL 40674: Mammalia DEKEDRC OD 9443: Primates DEKEDRC FM 9604: Hominidae DEKEDRC GE 9605: Homo DEKEDRC SP 9606: Homo sapiens DEDH7FP ID DEDH7FP DEDH7FP DN Corticosteroid 11-beta-dehydrogenase 2 (HSD11B2) DEDH7FP GN HSD11B2 DEDH7FP SN NAD-dependent 11-beta-hydroxysteroid dehydrogenase; Short chain dehydrogenase/reductase family 9C member 3; Corticosteroid 11-beta-dehydrogenase isozyme 2; 11-beta-hydroxysteroid dehydrogenase type 2; 11-beta-hydroxysteroid dehydrogenase type II; 11-DH2; 11-HSD type II; 11-beta-HSD; 11-beta-HSD type II; 11-beta-HSD2; HSD11B2; HSD11K; SDR9C3 DEDH7FP UC DHI2_HUMAN DEDH7FP RD Beclomethasone dipropionate DEDH7FP GI 3291 DEDH7FP E1 1: Oxidoreductase DEDH7FP E2 1.1: CH-OH donor oxidoreductase DEDH7FP E3 1.1.1: NAD/NADP oxidoreductase DEDH7FP EC 1.1.1.B40 DEDH7FP RC Glucocorticoid biosynthesis:R-HSA-194002 DEDH7FP KG Aldosterone-regulated sodium reabsorption:hsa04960; Metabolic pathways:hsa01100; Steroid hormone biosynthesis:hsa00140 DEDH7FP SQ MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALAVLAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDSMGFTVLATVLELNSPGAIELRTCCSPRLRLLQMDLTKPGDISRVLEFTKAHTTSTGLWGLVNNAGHNEVVADAELSPVATFRSCMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPCLGAYGTSKAAVALLMDTFSCELLPWGVKVSIIQPGCFKTESVRNVGQWEKRKQLLLANLPQELLQAYGKDYIEHLHGQFLHSLRLAMSDLTPVVDAITDALLAARPRRRYYPGQGLGLMYFIHYYLPEGLRRRFLQAFFISHCLPRALQPGQPGTTPPQDAAQDPNLSPGPSPAVAR DEDH7FP TD Primarily distributed in intestine, kidney and salivary gland. DEDH7FP FC This enzyme catalyzes the conversion of cortisol to the inactive metabolite cortisone. DEDH7FP KD 33208: Metazoa DEDH7FP PL 7711: Chordata DEDH7FP CL 40674: Mammalia DEDH7FP OD 9443: Primates DEDH7FP FM 9604: Hominidae DEDH7FP GE 9605: Homo DEDH7FP SP 9606: Homo sapiens DESD26P ID DESD26P DESD26P DN UDP-glucuronosyltransferase 1A6 (UGT1A6) DESD26P GN UGT1A6 DESD26P SN UDP-glucuronosyltransferase family 1 member A6; UDP-glucuronosyltransferase 1-F; UDP-glucuronosyltransferase 1-6; Phenol-metabolizing UDP-glucuronosyltransferase; UDPGT 1-6; UGT-1F; UGT1*6; UGT1-06; UGT1.6; UGT1A6; UGT1F DESD26P UC UD16_HUMAN DESD26P RD Naproxen DESD26P GI 54578 DESD26P E1 2: Transferase DESD26P E2 2.4: Glycosyltransferases DESD26P E3 2.4.1: Hexosyltransferase DESD26P EC 2.4.1.17 DESD26P RC Glucuronidation:R-HSA-156588 DESD26P KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DESD26P SQ MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVVPEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIGLYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEHTFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRDVDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH DESD26P TD Primarily distributed in kidney, liver and urinary bladder. DESD26P FC This enzyme has specificity for phenols. DESD26P KD 33208: Metazoa DESD26P PL 7711: Chordata DESD26P CL 40674: Mammalia DESD26P OD 9443: Primates DESD26P FM 9604: Hominidae DESD26P GE 9605: Homo DESD26P SP 9606: Homo sapiens DEZMWRE ID DEZMWRE DEZMWRE DN Cytochrome P450 2C18 (CYP2C18) DEZMWRE GN CYP2C18 DEZMWRE SN Cytochrome P450 family 2 subfamily C member 18; Cytochrome P450-6b/29c; CYP2C18; CYPIIC18 DEZMWRE UC CP2CI_HUMAN DEZMWRE RD Warfarin sodium DEZMWRE GI 1562 DEZMWRE E1 1: Oxidoreductase DEZMWRE E2 1.14: Oxygen paired donor oxidoreductase DEZMWRE E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEZMWRE EC 1.14.14.1 DEZMWRE RC Xenobiotics:R-HSA-211981 DEZMWRE KG Chemical carcinogenesis:hsa05204; Metabolic pathways:hsa01100; Retinol metabolism:hsa00830; Serotonergic synapse:hsa04726 DEZMWRE PD 2CIK; 2H6P DEZMWRE SQ MDPAVALVLCLSCLFLLSLWRQSSGRGRLPSGPTPLPIIGNILQLDVKDMSKSLTNFSKVYGPVFTVYFGLKPIVVLHGYEAVKEALIDHGEEFSGRGSFPVAEKVNKGLGILFSNGKRWKEIRRFCLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNASPCDPTFILGCAPCNVICSVIFHDRFDYKDQRFLNLMEKFNENLRILSSPWIQVCNNFPALIDYLPGSHNKIAENFAYIKSYVLERIKEHQESLDMNSARDFIDCFLIKMEQEKHNQQSEFTVESLIATVTDMFGAGTETTSTTLRYGLLLLLKYPEVTAKVQEEIECVVGRNRSPCMQDRSHMPYTDAVVHEIQRYIDLLPTNLPHAVTCDVKFKNYLIPKGTTIITSLTSVLHNDKEFPNPEMFDPGHFLDKSGNFKKSDYFMPFSAGKRMCMGEGLARMELFLFLTTILQNFNLKSQVDPKDIDITPIANAFGRVPPLYQLCFIPV DEZMWRE TD Primarily distributed in intestine and liver. DEZMWRE FC This enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. DEZMWRE KD 33208: Metazoa DEZMWRE PL 7711: Chordata DEZMWRE CL 40674: Mammalia DEZMWRE OD 9443: Primates DEZMWRE FM 9604: Hominidae DEZMWRE GE 9605: Homo DEZMWRE SP 9606: Homo sapiens DEFJOAG ID DEFJOAG DEFJOAG DN Transglutaminase K (TGM1) DEFJOAG GN TGM1 DEFJOAG SN Protein-glutamine gamma-glutamyltransferase K; Transglutaminase-1; Protein-glutamine gamma-glutamyltransferase 1; Epidermal TGase; TGase K; TGase-1; KTG; TG(K); TGK; TGM1 DEFJOAG UC TGM1_HUMAN DEFJOAG RD L-glutamine DEFJOAG GI 7051 DEFJOAG E1 2: Transferase DEFJOAG E2 2.3: Acyltransferase DEFJOAG E3 2.3.2: Aminoacyltransferase DEFJOAG EC 2.3.2.13 DEFJOAG RC Formation of the cornified envelope:R-HSA-6809371 DEFJOAG PD 2XZZ DEFJOAG SQ MMDGPRSDVGRWGGNPLQPPTTPSPEPEPEPDGRSRRGGGRSFWARCCGCCSCRNAADDDWGPEPSDSRGRGSSSGTRRPGSRGSDSRRPVSRGSGVNAAGDGTIREGMLVVNGVDLLSSRSDQNRREHHTDEYEYDELIVRRGQPFHMLLLLSRTYESSDRITLELLIGNNPEVGKGTHVIIPVGKGGSGGWKAQVVKASGQNLNLRVHTSPNAIIGKFQFTVRTQSDAGEFQLPFDPRNEIYILFNPWCPEDIVYVDHEDWRQEYVLNESGRIYYGTEAQIGERTWNYGQFDHGVLDACLYILDRRGMPYGGRGDPVNVSRVISAMVNSLDDNGVLIGNWSGDYSRGTNPSAWVGSVEILLSYLRTGYSVPYGQCWVFAGVTTTVLRCLGLATRTVTNFNSAHDTDTSLTMDIYFDENMKPLEHLNHDSVWNFHVWNDCWMKRPDLPSGFDGWQVVDATPQETSSGIFCCGPCSVESIKNGLVYMKYDTPFIFAEVNSDKVYWQRQDDGSFKIVYVEEKAIGTLIVTKAISSNMREDITYLYKHPEGSDAERKAVETAAAHGSKPNVYANRGSAEDVAMQVEAQDAVMGQDLMVSVMLINHSSSRRTVKLHLYLSVTFYTGVSGTIFKETKKEVELAPGASDRVTMPVAYKEYRPHLVDQGAMLLNVSGHVKESGQVLAKQHTFRLRTPDLSLTLLGAAVVGQECEVQIVFKNPLPVTLTNVVFRLEGSGLQRPKILNVGDIGGNETVTLRQSFVPVRPGPRQLIASLDSPQLSQVHGVIQVDVAPAPGDGGFFSDAGGDSHLGETIPMASRGGA DEFJOAG TD Primarily distributed in esophagus, lymphoid tissue and tongue. DEFJOAG FC This enzyme catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. DEFJOAG KD 33208: Metazoa DEFJOAG PL 7711: Chordata DEFJOAG CL 40674: Mammalia DEFJOAG OD 9443: Primates DEFJOAG FM 9604: Hominidae DEFJOAG GE 9605: Homo DEFJOAG SP 9606: Homo sapiens DEK6079 ID DEK6079 DEK6079 DN Glutathione S-transferase pi (GSTP1) DEK6079 GN GSTP1 DEK6079 SN Glutathione S-transferase Pi; Glutathione S-transferase P; FAEES3; GST class-pi; GST3; GSTP1; GSTP1-1 DEK6079 UC GSTP1_HUMAN DEK6079 RD Busulfan DEK6079 GI 2950 DEK6079 E1 2: Transferase DEK6079 E2 2.5: Alkyl/aryl transferase DEK6079 E3 2.5.1: Alkyl/aryl transferase DEK6079 EC 2.5.1.18 DEK6079 RC Detoxification of Reactive Oxygen Species:R-HSA-3299685; Glutathione conjugation:R-HSA-156590; Neutrophil degranulation:R-HSA-6798695 DEK6079 KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524; Prostate cancer:hsa05215 DEK6079 PD 12GS; 13GS; 14GS; 16GS; 17GS; 18GS; 19GS; 1AQV; 1AQW DEK6079 SQ MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ DEK6079 TD Low tissue/organ specificity. DEK6079 FC This enzyme conjugates reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. DEK6079 KD 33208: Metazoa DEK6079 PL 7711: Chordata DEK6079 CL 40674: Mammalia DEK6079 OD 9443: Primates DEK6079 FM 9604: Hominidae DEK6079 GE 9605: Homo DEK6079 SP 9606: Homo sapiens DE4EGMZ ID DE4EGMZ DE4EGMZ DN Dihydrofolate reductase (DHFR) DE4EGMZ GN DHFR DE4EGMZ SN Tetrahydrofolate:NADP+ oxidoreductase; 5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase; 7,8-dihydrofolate reductase; DHFR DE4EGMZ UC DYR_HUMAN DE4EGMZ RD Methotrexate DE4EGMZ GI 1719 DE4EGMZ E1 1: Oxidoreductase DE4EGMZ E2 1.5: CH-NH donor oxidoreductase DE4EGMZ E3 1.5.1: NAD/NADP acceptor oxidoreductase DE4EGMZ EC 1.5.1.3 DE4EGMZ RC G1/S-Specific Transcription:R-HSA-69205; Metabolism of folate and pterines:R-HSA-196757; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation:R-HSA-1474151 DE4EGMZ KG Antifolate resistance:hsa01523; Folate biosynthesis:hsa00790; Metabolic pathways:hsa01100; One carbon pool by folate:hsa00670 DE4EGMZ PD 1DLR; 1DLS; 1DRF; 1HFP; 1HFQ; 1HFR; 1KMS; 1KMV; 1MVS DE4EGMZ SQ MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND DE4EGMZ TD Low tissue/organ specificity. DE4EGMZ FC This enzyme converts dihydrofolate into tetrahydrofolate, a methyl group shuttle required for the de novo synthesis of pyrimidines, thymidylic acid, and certain amino acids. DE4EGMZ KD 33208: Metazoa DE4EGMZ PL 7711: Chordata DE4EGMZ CL 40674: Mammalia DE4EGMZ OD 9443: Primates DE4EGMZ FM 9604: Hominidae DE4EGMZ GE 9605: Homo DE4EGMZ SP 9606: Homo sapiens DEGQTXO ID DEGQTXO DEGQTXO DN Aldo-keto reductase 1C3 (AKR1C3) DEGQTXO GN AKR1C3 DEGQTXO SN Aldo-keto reductase family 1 member C3; Chlordecone reductase homolog HAKRb; DD-3; DD3; Dihydrodiol dehydrogenase 3; Dihydrodiol dehydrogenase type I; HA1753; HSD17B5; KIAA0119; PGFS; Prostaglandin F synthase; Testosterone 17-beta-dehydrogenase 5; 17-beta-HSD 5; 17-beta-hydroxysteroid dehydrogenase type 5; 3-alpha-HSD type 2; 3-alpha-HSD type II, brain; 3-alpha-hydroxysteroid dehydrogenase type 2; AKR1C3 DEGQTXO UC AK1C3_HUMAN DEGQTXO RD Doxorubicin DEGQTXO GI 8644 DEGQTXO E1 1: Oxidoreductase DEGQTXO E2 1.1: CH-OH donor oxidoreductase DEGQTXO E3 1.1.1: NAD/NADP oxidoreductase DEGQTXO EC 1.1.1.357 DEGQTXO RC RA biosynthesis pathway:R-HSA-5365859; Retinoid metabolism and transport:R-HSA-975634; Synthesis of Prostaglandins (PG) and Thromboxanes (TX):R-HSA-2162123; Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DEGQTXO KG Arachidonic acid metabolism:hsa00590; Folate biosynthesis:hsa00790; Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Steroid hormone biosynthesis:hsa00140 DEGQTXO PD 1S1P; 1S1R; 1S2A; 1S2C; 1XF0; 1ZQ5; 2F38; 2FGB; 3R43 DEGQTXO SQ MDSKHQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPMSLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLDRNLHYFNSDSFASHPNYPYSDEY DEGQTXO TD Primarily distributed in blood and intestine. DEGQTXO FC This enzyme catalyzes the conversion of aldehydes and ketones to alcohols. It catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9-alpha,11-beta-PGF2 to PGD2 and functions as a bi-directional 3-alpha-, 17-beta- and 20-alpha HSD. Besides, it can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites and preferentially transforms androstenedione (4-dione) to testosterone. DEGQTXO KD 33208: Metazoa DEGQTXO PL 7711: Chordata DEGQTXO CL 40674: Mammalia DEGQTXO OD 9443: Primates DEGQTXO FM 9604: Hominidae DEGQTXO GE 9605: Homo DEGQTXO SP 9606: Homo sapiens DEPTJ3D ID DEPTJ3D DEPTJ3D DN Steroid 5-alpha-reductase 2 (SRD5A2) DEPTJ3D GN SRD5A2 DEPTJ3D SN Alpha-reductase steroid 2; 3-oxo-5-alpha-steroid 4-dehydrogenase 2; 5 alpha-SR2; S5AR 2; SR type 2; SRD5A2; Type II 5-alpha reductase DEPTJ3D UC S5A2_HUMAN DEPTJ3D RD Testosterone cypionate DEPTJ3D GI 6716 DEPTJ3D E1 1: Oxidoreductase DEPTJ3D E2 1.3: CH-CH donor oxidoreductase DEPTJ3D E3 1.3.1: NAD/NADP acceptor oxidoreductase DEPTJ3D EC 1.3.1.22 DEPTJ3D RC Androgen biosynthesis:R-HSA-193048 DEPTJ3D KG Prostate cancer:hsa05215; Steroid hormone biosynthesis:hsa00140 DEPTJ3D SQ MQVQCQQSPVLAGSATLVALGALALYVAKPSGYGKHTESLKPAATRLPARAAWFLQELPSFAVPAGILARQPLSLFGPPGTVLLGLFCVHYFHRTFVYSLLNRGRPYPAILILRGTAFCTGNGVLQGYYLIYCAEYPDGWYTDIRFSLGVFLFILGMGINIHSDYILRQLRKPGEISYRIPQGGLFTYVSGANFLGEIIEWIGYALATWSLPALAFAFFSLCFLGLRAFHHHRFYLKMFEDYPKSRKALIPFIF DEPTJ3D TD Primarily distributed in epididymis, liver and prostate. DEPTJ3D FC This enzyme converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5- alpha-3-oxosteroids. DEPTJ3D KD 33208: Metazoa DEPTJ3D PL 7711: Chordata DEPTJ3D CL 40674: Mammalia DEPTJ3D OD 9443: Primates DEPTJ3D FM 9604: Hominidae DEPTJ3D GE 9605: Homo DEPTJ3D SP 9606: Homo sapiens DEF2WXN ID DEF2WXN DEF2WXN DN UDP-glucuronosyltransferase 1A3 (UGT1A3) DEF2WXN GN UGT1A3 DEF2WXN SN UDP-glucuronosyltransferase family 1 member A3; UDP-glucuronosyltransferase 1-C; UDP-glucuronosyltransferase 1-3; UDPGT 1-3; UGT-1C; UGT1*3; UGT1-03; UGT1.3; UGT1A3; UGT1C DEF2WXN UC UD13_HUMAN DEF2WXN RD Lorlatinib DEF2WXN GI 54659 DEF2WXN E1 2: Transferase DEF2WXN E2 2.4: Glycosyltransferases DEF2WXN E3 2.4.1: Hexosyltransferase DEF2WXN EC 2.4.1.17 DEF2WXN RC Glucuronidation:R-HSA-156588; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis:R-HSA-9623433 DEF2WXN KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEF2WXN SQ MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVVLTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNMSLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDLDFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQREVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH DEF2WXN TD Primarily distributed in liver. Also expressed in kidney, colon and small intestine. DEF2WXN FC This enzyme is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. DEF2WXN KD 33208: Metazoa DEF2WXN PL 7711: Chordata DEF2WXN CL 40674: Mammalia DEF2WXN OD 9443: Primates DEF2WXN FM 9604: Hominidae DEF2WXN GE 9605: Homo DEF2WXN SP 9606: Homo sapiens DETK9CN ID DETK9CN DETK9CN DN DOPA decarboxylase (DDC) DETK9CN GN DDC DETK9CN SN Aromatic-L-amino-acid decarboxylase; Tryptophan decarboxylase; 5-hydroxytryptophan decarboxylase; AADC; DDC DETK9CN UC DDC_HUMAN DETK9CN RD Droxidopa DETK9CN GI 1644 DETK9CN E1 4: Lyases DETK9CN E2 4.1: Carbon-carbon lyase DETK9CN E3 4.1.1: Carboxy-lyase DETK9CN EC 4.1.1.28 DETK9CN RC Catecholamine biosynthesis:R-HSA-209905; Serotonin and melatonin biosynthesis:R-HSA-209931 DETK9CN KG Alcoholism:hsa05034; Amphetamine addiction:hsa05031; Cocaine addiction:hsa05030; Dopaminergic synapse:hsa04728; Metabolic pathways:hsa01100; Phenylalanine metabolism:hsa00360; Serotonergic synapse:hsa04726; Tryptophan metabolism:hsa00380; Tyrosine metabolism:hsa00350 DETK9CN PD 3RBF; 3RBL; 3RCH DETK9CN SQ MNASEFRRRGKEMVDYMANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDVEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIMEKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMVATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVNEALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE DETK9CN TD Primarily distributed in intestine and kidney. DETK9CN FC This enzyme catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine. DETK9CN KD 33208: Metazoa DETK9CN PL 7711: Chordata DETK9CN CL 40674: Mammalia DETK9CN OD 9443: Primates DETK9CN FM 9604: Hominidae DETK9CN GE 9605: Homo DETK9CN SP 9606: Homo sapiens DETHCPD ID DETHCPD DETHCPD DN Carboxylesterase 2 (CES2) DETHCPD GN CES2 DETHCPD SN Cocaine esterase; Methylumbelliferyl-acetate deacetylase 2; hCE-2; CE-2; CES2; ICE DETHCPD UC EST2_HUMAN DETHCPD RD Rufinamide DETHCPD GI 8824 DETHCPD E1 3: Hydrolases DETHCPD E2 3.1: Ester bond hydrolase DETHCPD E3 3.1.1: Carboxylic ester hydrolase DETHCPD EC 3.1.1.1 DETHCPD RC Phase I - Functionalization of compounds:R-HSA-211945 DETHCPD KG Drug metabolism - other enzymes:hsa00983 DETHCPD SQ MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPALQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKKALPQKIQELEEPEERHTEL DETHCPD TD Primarily distributed in esophagus, intestine and liver. DETHCPD FC This enzyme is involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. It shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine. It also hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogenous lipids such as triacylglycerol. DETHCPD KD 33208: Metazoa DETHCPD PL 7711: Chordata DETHCPD CL 40674: Mammalia DETHCPD OD 9443: Primates DETHCPD FM 9604: Hominidae DETHCPD GE 9605: Homo DETHCPD SP 9606: Homo sapiens DEJPZHB ID DEJPZHB DEJPZHB DN Glutamine amidotransferase (GMPS) DEJPZHB GN GMPS DEJPZHB SN GMP synthase [glutamine-hydrolyzing]; GMP synthetase; GMPS DEJPZHB UC GUAA_HUMAN DEJPZHB RD L-glutamine DEJPZHB GI 8833 DEJPZHB E1 6: Ligase DEJPZHB E2 6.3: Carbon-nitrogen ligase DEJPZHB E3 6.3.5: Carbon-nitrogen ligase DEJPZHB EC 6.3.5.2 DEJPZHB RC Purine ribonucleoside monophosphate biosynthesis:R-HSA-73817 DEJPZHB KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Purine metabolism:hsa00230 DEJPZHB PD 2VPI; 2VXO DEJPZHB SQ MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE DEJPZHB TD Low tissue/organ specificity. DEJPZHB FC This enzyme is involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division. DEJPZHB KD 33208: Metazoa DEJPZHB PL 7711: Chordata DEJPZHB CL 40674: Mammalia DEJPZHB OD 9443: Primates DEJPZHB FM 9604: Hominidae DEJPZHB GE 9605: Homo DEJPZHB SP 9606: Homo sapiens DEOEB3Q ID DEOEB3Q DEOEB3Q DN Transglutaminase E (TGM3) DEOEB3Q GN TGM3 DEOEB3Q SN Protein-glutamine gamma-glutamyltransferase E; Transglutaminase-3; Protein-glutamine gamma-glutamyltransferase 3; Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain; Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain; TG(E); TGE; TGM3; TGase E; TGase-3 DEOEB3Q UC TGM3_HUMAN DEOEB3Q RD L-glutamine DEOEB3Q GI 7053 DEOEB3Q E1 2: Transferase DEOEB3Q E2 2.3: Acyltransferase DEOEB3Q E3 2.3.2: Aminoacyltransferase DEOEB3Q EC 2.3.2.13 DEOEB3Q PD 1L9M; 1L9N; 1NUD; 1NUF; 1NUG DEOEB3Q SQ MAALGVQSINWQTAFNRQAHHTDKFSSQELILRRGQNFQVLMIMNKGLGSNERLEFIVSTGPYPSESAMTKAVFPLSNGSSGGWSAVLQASNGNTLTISISSPASAPIGRYTMALQIFSQGGISSVKLGTFILLFNPWLNVDSVFMGNHAEREEYVQEDAGIIFVGSTNRIGMIGWNFGQFEEDILSICLSILDRSLNFRRDAATDVASRNDPKYVGRVLSAMINSNDDNGVLAGNWSGTYTGGRDPRSWNGSVEILKNWKKSGFSPVRYGQCWVFAGTLNTALRSLGIPSRVITNFNSAHDTDRNLSVDVYYDPMGNPLDKGSDSVWNFHVWNEGWFVRSDLGPSYGGWQVLDATPQERSQGVFQCGPASVIGVREGDVQLNFDMPFIFAEVNADRITWLYDNTTGKQWKNSVNSHTIGRYISTKAVGSNARMDVTDKYKYPEGSDQERQVFQKALGKLKPNTPFAATSSMGLETEEQEPSIIGKLKVAGMLAVGKEVNLVLLLKNLSRDTKTVTVNMTAWTIIYNGTLVHEVWKDSATMSLDPEEEAEHPIKISYAQYEKYLKSDNMIRITAVCKVPDESEVVVERDIILDNPTLTLEVLNEARVRKPVNVQMLFSNPLDEPVRDCVLMVEGSGLLLGNLKIDVPTLGPKEGSRVRFDILPSRSGTKQLLADFSCNKFPAIKAMLSIDVAE DEOEB3Q TD Primarily distributed in esophagus, lymphoid tissue and tongue. DEOEB3Q FC This enzyme catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. It is involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. And it catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold. DEOEB3Q KD 33208: Metazoa DEOEB3Q PL 7711: Chordata DEOEB3Q CL 40674: Mammalia DEOEB3Q OD 9443: Primates DEOEB3Q FM 9604: Hominidae DEOEB3Q GE 9605: Homo DEOEB3Q SP 9606: Homo sapiens DEYEK78 ID DEYEK78 DEYEK78 DN Nitric oxide synthase brain (NOS1) DEYEK78 GN NOS1 DEYEK78 SN Peptidyl-cysteine S-nitrosylase NOS1; Neuronal NOS; Brain nitric oxide synthase; Constitutive NOS; bNOS; nNOS; N-NOS; NC-NOS; NOS type I; NOS1 DEYEK78 UC NOS1_HUMAN DEYEK78 RD Doxorubicin DEYEK78 GI 4842 DEYEK78 E1 1: Oxidoreductase DEYEK78 E2 1.14: Oxygen paired donor oxidoreductase DEYEK78 E3 1.14.13: NADH/NADPH donor oxidoreductase DEYEK78 EC 1.14.13.39 DEYEK78 RC Ion homeostasis:R-HSA-5578775; Nitric oxide stimulates guanylate cyclase:R-HSA-392154; ROS and RNS production in phagocytes:R-HSA-1222556 DEYEK78 KG Alzheimer's disease:hsa05010; Amyotrophic lateral sclerosis (ALS):hsa05014; Apelin signaling pathway:hsa04371; Arginine and proline metabolism:hsa00330; Arginine biosynthesis:hsa00220; Calcium signaling pathway:hsa04020; Circadian entrainment:hsa04713; Long-term depression:hsa04730; Metabolic pathways:hsa01100; Phagosome:hsa04145; Relaxin signaling pathway:hsa04926; Salivary secretion:hsa04970 DEYEK78 PD 4UH5; 4UH6; 4V3U; 5ADF; 5ADG; 5ADI; 5FVU; 5FVV; 5FVW DEYEK78 SQ MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAPRPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQVDRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQEERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGVISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS DEYEK78 TD Primarily distributed in brain and skeletal muscle. DEYEK78 FC This enzyme has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. DEYEK78 KD 33208: Metazoa DEYEK78 PL 7711: Chordata DEYEK78 CL 40674: Mammalia DEYEK78 OD 9443: Primates DEYEK78 FM 9604: Hominidae DEYEK78 GE 9605: Homo DEYEK78 SP 9606: Homo sapiens DEGH1QU ID DEGH1QU DEGH1QU DN Tryptophan oxygenase (TRPO) DEGH1QU GN TDO2 DEGH1QU SN Tryptamin 2,3-dioxygenase; Tryptophan 2,3-dioxygenase; Tryptophan pyrrolase; Tryptophanase; TDO; TDO2; TO; TRPO DEGH1QU UC T23O_HUMAN DEGH1QU RD TRP-01 DEGH1QU GI 6999 DEGH1QU E1 1: Oxidoreductase DEGH1QU E2 1.13: Oxygen single donor oxidoreductase DEGH1QU E3 1.13.11: Oxygen single donor oxidoreductase DEGH1QU EC 1.13.11.11 DEGH1QU RC Tryptophan catabolism:R-HSA-71240 DEGH1QU KG Metabolic pathways:hsa01100; Tryptophan metabolism:hsa00380 DEGH1QU PD 4PW8; 5TI9; 5TIA; 6A4I DEGH1QU SQ MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSETKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSVILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHYRDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIRIQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYREEPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYKVFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD DEGH1QU TD Primarily distributed in liver. DEGH1QU FC This enzyme catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. It catalyzes the oxidative cleavage of the indole moiety. DEGH1QU KD 33208: Metazoa DEGH1QU PL 7711: Chordata DEGH1QU CL 40674: Mammalia DEGH1QU OD 9443: Primates DEGH1QU FM 9604: Hominidae DEGH1QU GE 9605: Homo DEGH1QU SP 9606: Homo sapiens DENZ6B1 ID DENZ6B1 DENZ6B1 DN UDP-glucuronosyltransferase 2B15 (UGT2B15) DENZ6B1 GN UGT2B15 DENZ6B1 SN UDP-glucuronosyltransferase family 2 member B15; UDP-glucuronosyltransferase 2B8; HLUG4; UDPGT 2B15; UDPGT 2B8; UDPGTh-3; UGT2B15; UGT2B8 DENZ6B1 UC UDB15_HUMAN DENZ6B1 RD Lorazepam DENZ6B1 GI 7366 DENZ6B1 E1 2: Transferase DENZ6B1 E2 2.4: Glycosyltransferases DENZ6B1 E3 2.4.1: Hexosyltransferase DENZ6B1 EC 2.4.1.17 DENZ6B1 RC Glucuronidation:R-HSA-156588 DENZ6B1 KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DENZ6B1 SQ MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSASTLVNASKSSAIKLEVYPTSLTKNYLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEYYDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYTFEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEVLGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRTMSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD DENZ6B1 TD Primarily distributed in gallbladder, intestine and liver. DENZ6B1 FC This enzyme displays activity toward several classes of xenobiotic substrates, including simple phenolic compounds, 7- hydroxylated coumarins, flavonoids, anthraquinones, and certain drugs and their hydroxylated metabolites. And it also catalyzes the glucuronidation of endogenous estrogens and androgens. DENZ6B1 KD 33208: Metazoa DENZ6B1 PL 7711: Chordata DENZ6B1 CL 40674: Mammalia DENZ6B1 OD 9443: Primates DENZ6B1 FM 9604: Hominidae DENZ6B1 GE 9605: Homo DENZ6B1 SP 9606: Homo sapiens DEOXTPZ ID DEOXTPZ DEOXTPZ DN Methylenetetrahydrofolate reductase (MTHFR) DEOXTPZ GN MTHFR DEOXTPZ SN Methylene tetrahydrofolate reductase; Methylenetetra hydrofolate reductase; MTHFR DEOXTPZ UC MTHR_HUMAN DEOXTPZ RD Methotrexate DEOXTPZ GI 4524 DEOXTPZ E1 1: Oxidoreductase DEOXTPZ E2 1.5: CH-NH donor oxidoreductase DEOXTPZ E3 1.5.1: NAD/NADP acceptor oxidoreductase DEOXTPZ EC 1.5.1.20 DEOXTPZ RC Metabolism of folate and pterines:R-HSA-196757 DEOXTPZ KG Antifolate resistance:hsa01523; Carbon metabolism:hsa01200; Metabolic pathways:hsa01100; One carbon pool by folate:hsa00670 DEOXTPZ PD 6FCX DEOXTPZ SQ MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYCGLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVKHIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFVKACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIELAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREEDVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKMWGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGILTINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHLVNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYEEESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP DEOXTPZ TD Low tissue/organ specificity. DEOXTPZ FC This enzyme catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a co-substrate for homocysteine remethylation to methionine. DEOXTPZ KD 33208: Metazoa DEOXTPZ PL 7711: Chordata DEOXTPZ CL 40674: Mammalia DEOXTPZ OD 9443: Primates DEOXTPZ FM 9604: Hominidae DEOXTPZ GE 9605: Homo DEOXTPZ SP 9606: Homo sapiens DERQCJM ID DERQCJM DERQCJM DN Hexosephosphate aminotransferase 2 (GFPT2) DERQCJM GN GFPT2 DERQCJM SN Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2; Glutamine:fructose-6-phosphate amidotransferase 2; D-fructose-6-phosphate amidotransferase 2; GFAT 2; GFAT2; GFPT2 DERQCJM UC GFPT2_HUMAN DERQCJM RD L-glutamine DERQCJM GI 9945 DERQCJM E1 2: Transferase DERQCJM E2 2.6: Transaminase DERQCJM E3 2.6.1: Transaminase DERQCJM EC 2.6.1.16 DERQCJM RC Synthesis of UDP-N-acetyl-glucosamine:R-HSA-446210 DERQCJM KG Alanine, aspartate and glutamate metabolism:hsa00250; Amino sugar and nucleotide sugar metabolism:hsa00520; Insulin resistance:hsa04931; Metabolic pathways:hsa01100 DERQCJM SQ MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKRGKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMKRLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSASDDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE DERQCJM TD Primarily distributed in heart, placenta and spinal cord. DERQCJM FC This enzyme is most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. DERQCJM KD 33208: Metazoa DERQCJM PL 7711: Chordata DERQCJM CL 40674: Mammalia DERQCJM OD 9443: Primates DERQCJM FM 9604: Hominidae DERQCJM GE 9605: Homo DERQCJM SP 9606: Homo sapiens DEV3T4A ID DEV3T4A DEV3T4A DN Catechol O-methyltransferase (COMT) DEV3T4A GN COMT DEV3T4A SN Catecholamine degradation enzyme; Catecholestrogen degradation enzyme; COMT; HEL-S-98n DEV3T4A UC COMT_HUMAN DEV3T4A RD Epinephrine hydrochloride DEV3T4A GI 1312 DEV3T4A E1 2: Transferase DEV3T4A E2 2.1: Methylase DEV3T4A E3 2.1.1: Methyltransferase DEV3T4A EC 2.1.1.6 DEV3T4A RC Enzymatic degradation of Dopamine by monoamine oxidase:R-HSA-379398; Enzymatic degradation of dopamine by COMT:R-HSA-379397; Methylation:R-HSA-156581 DEV3T4A KG Dopaminergic synapse:hsa04728; Metabolic pathways:hsa01100; Steroid hormone biosynthesis:hsa00140; Tyrosine metabolism:hsa00350 DEV3T4A PD 3BWY; 4PYI; 4PYJ; 4PYK; 4XUC; 4XUD; 4XUE; 5LSA; 6I3C DEV3T4A SQ MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP DEV3T4A TD Primarily distributed in liver. Also expressed in brain, placenta, lymphocytes and erythrocytes. DEV3T4A FC This enzyme catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. It also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. DEV3T4A KD 33208: Metazoa DEV3T4A PL 7711: Chordata DEV3T4A CL 40674: Mammalia DEV3T4A OD 9443: Primates DEV3T4A FM 9604: Hominidae DEV3T4A GE 9605: Homo DEV3T4A SP 9606: Homo sapiens DE9JFMC ID DE9JFMC DE9JFMC DN NADPH-dependent carbonyl reductase 1 (CBR1) DE9JFMC GN CBR1 DE9JFMC SN Prostaglandin 9-ketoreductase; Prostaglandin-E(2) 9-reductase; Short chain dehydrogenase/reductase family 21C member 1; 15-hydroxyprostaglandin dehydrogenase [NADP(+)]; Carbonyl reductase [NADPH] 1; CBR; CBR1; CRN; SDR21C1 DE9JFMC UC CBR1_HUMAN DE9JFMC RD Fenofibric acid DE9JFMC GI 873 DE9JFMC E1 1: Oxidoreductase DE9JFMC E2 1.1: CH-OH donor oxidoreductase DE9JFMC E3 1.1.1: NAD/NADP oxidoreductase DE9JFMC EC 1.1.1.184 DE9JFMC RC Synthesis of Prostaglandins (PG) and Thromboxanes (TX):R-HSA-2162123 DE9JFMC KG Arachidonic acid metabolism:hsa00590; Chemical carcinogenesis:hsa05204; Folate biosynthesis:hsa00790; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980 DE9JFMC PD 1WMA; 2PFG; 3BHI; 3BHJ; 3BHM; 4Z3D DE9JFMC SQ MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW DE9JFMC TD Primarily distributed in intestine. DE9JFMC FC This enzyme has broad substrate specificity. It catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. It can also catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Besides, it can convert prostaglandin E2 to prostaglandin F2- alpha and catalyzes the reduction of S-nitrosoglutathione. DE9JFMC KD 33208: Metazoa DE9JFMC PL 7711: Chordata DE9JFMC CL 40674: Mammalia DE9JFMC OD 9443: Primates DE9JFMC FM 9604: Hominidae DE9JFMC GE 9605: Homo DE9JFMC SP 9606: Homo sapiens DEMF740 ID DEMF740 DEMF740 DN Cytochrome P450 4B1 (CYP4B1) DEMF740 GN CYP4B1 DEMF740 SN Cytochrome P450 family 4 subfamily B member 1; CYP4B1; CYPIVB1; Cytochrome P450-HP DEMF740 UC CP4B1_HUMAN DEMF740 RD Midazolam hydrochloride DEMF740 GI 1580 DEMF740 E1 1: Oxidoreductase DEMF740 E2 1.14: Oxygen paired donor oxidoreductase DEMF740 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEMF740 EC 1.14.14.1 DEMF740 RC Eicosanoids:R-HSA-211979; Fatty acids:R-HSA-211935; Miscellaneous substrates:R-HSA-211958; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DEMF740 SQ MVPSFLSLSFSSLGLWASGLILVLGFLKLIHLLLRRQTLAKAMDKFPGPPTHWLFGHALEIQETGSLDKVVSWAHQFPYAHPLWFGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQWIGRGLLVLEGPKWLQHRKLLTPGFHYDVLKPYVAVFTESTRIMLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQLVLRSKNGFHLHLKPLGPGSGK DEMF740 TD Primarily distributed in liver and lung. DEMF740 FC This enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. DEMF740 KD 33208: Metazoa DEMF740 PL 7711: Chordata DEMF740 CL 40674: Mammalia DEMF740 OD 9443: Primates DEMF740 FM 9604: Hominidae DEMF740 GE 9605: Homo DEMF740 SP 9606: Homo sapiens DE14JZK ID DE14JZK DE14JZK DN Cathepsin A (CTSA) DE14JZK GN CTSA DE14JZK SN Carboxypeptidase C; Carboxypeptidase L; Lysosomal protective protein; Lysosomal protective protein 20 kDa chain; Lysosomal protective protein 32 kDa chain; CTSA; PPCA; PPGB; Protective protein cathepsin A; Protective protein for beta-galactosidase DE14JZK UC PPGB_HUMAN DE14JZK RD Tenofovir alafenamide DE14JZK GI 5476 DE14JZK E1 3: Hydrolases DE14JZK E2 3.4: Peptidase DE14JZK E3 3.4.16: Serine carboxypeptidase DE14JZK EC 3.4.16.5 DE14JZK RC Defective NEU1 causes sialidosis:R-HSA-4341670; Glycosphingolipid metabolism:R-HSA-1660662; MHC class II antigen presentation:R-HSA-2132295; Neutrophil degranulation:R-HSA-6798695; Sialic acid metabolism:R-HSA-4085001 DE14JZK KG Lysosome:hsa04142; Renin-angiotensin system:hsa04614 DE14JZK PD 3BP7; 3BXN; 4AZ0; 4AZ3; 4CI9; 4CIA; 4CIB; 4MWS; 4MWT DE14JZK SQ MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY DE14JZK TD Primarily distributed in adrenal. DE14JZK FC This enzyme is a carboxypeptidase and can deamidate tachykinins. DE14JZK KD 33208: Metazoa DE14JZK PL 7711: Chordata DE14JZK CL 40674: Mammalia DE14JZK OD 9443: Primates DE14JZK FM 9604: Hominidae DE14JZK GE 9605: Homo DE14JZK SP 9606: Homo sapiens DED2FW3 ID DED2FW3 DED2FW3 DN Aldo-keto reductase 1A1 (AKR1A1) DED2FW3 GN AKR1A1 DED2FW3 SN Aldo-keto reductase family 1 member A1; Glucuronate reductase; Glucuronolactone reductase; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; AKR1A1; ALDR1; ALR DED2FW3 UC AK1A1_HUMAN DED2FW3 RD Doxorubicin DED2FW3 GI 10327 DED2FW3 E1 1: Oxidoreductase DED2FW3 E2 1.1: CH-OH donor oxidoreductase DED2FW3 E3 1.1.1: NAD/NADP oxidoreductase DED2FW3 EC 1.1.1.2 DED2FW3 RC Formation of xylulose-5-phosphate:R-HSA-5661270; Glutathione conjugation:R-HSA-156590 DED2FW3 KG Glycerolipid metabolism:hsa00561; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Pentose and glucuronate interconversions:hsa00040 DED2FW3 PD 2ALR DED2FW3 SQ MAASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVPMLTVDGKRVPRDAGHPLYPFNDPY DED2FW3 TD Primarily distributed in kidney, salivary gland and liver. DED2FW3 FC This enzyme catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. It displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde. It functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. It can reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. It is also involved in the detoxification of lipid-derived aldehydes like acrolein. It plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs, including the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN). DED2FW3 KD 33208: Metazoa DED2FW3 PL 7711: Chordata DED2FW3 CL 40674: Mammalia DED2FW3 OD 9443: Primates DED2FW3 FM 9604: Hominidae DED2FW3 GE 9605: Homo DED2FW3 SP 9606: Homo sapiens DE7OAB3 ID DE7OAB3 DE7OAB3 DN N-acetyltransferase 1 (NAT1) DE7OAB3 GN NAT1 DE7OAB3 SN Arylamine N-acetyltransferase 1; N-acetyltransferase type 1; Arylamide acetylase 1; Monomorphic arylamine N-acetyltransferase; MNAT; NAT-1; AAC1; NAT1 DE7OAB3 UC ARY1_HUMAN DE7OAB3 RD Procainamide hydrochloride DE7OAB3 GI 9 DE7OAB3 E1 2: Transferase DE7OAB3 E2 2.3: Acyltransferase DE7OAB3 E3 2.3.1: Acyltransferase DE7OAB3 EC 2.3.1.5 DE7OAB3 RC Acetylation:R-HSA-156582 DE7OAB3 KG Caffeine metabolism:hsa00232; Chemical carcinogenesis:hsa05204; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100 DE7OAB3 PD 2DSS; 2GWU; 2IJA; 2PQT DE7OAB3 SQ MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVVRRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYIVDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDLLEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLTHRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI DE7OAB3 TD Primarily distributed in intestine. DE7OAB3 FC This enzyme participates in the detoxification of a plethora of hydrazine and arylamine drugs. It catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens. DE7OAB3 KD 33208: Metazoa DE7OAB3 PL 7711: Chordata DE7OAB3 CL 40674: Mammalia DE7OAB3 OD 9443: Primates DE7OAB3 FM 9604: Hominidae DE7OAB3 GE 9605: Homo DE7OAB3 SP 9606: Homo sapiens DED5UR3 ID DED5UR3 DED5UR3 DN Sulfotransferase 1B1 (SULT1B1) DED5UR3 GN SULT1B1 DED5UR3 SN Sulfotransferase family cytosolic 1B member 1; Sulfotransferase 1B2; Thyroid hormone sulfotransferase; ST1B1; ST1B2; SULT1B1; SULT1B2 DED5UR3 UC ST1B1_HUMAN DED5UR3 RD Rotigotine DED5UR3 GI 27284 DED5UR3 E1 2: Transferase DED5UR3 E2 2.8: Sulfotransferase DED5UR3 E3 2.8.2: Sulfotransferase DED5UR3 EC 2.8.2.1 DED5UR3 RC Cytosolic sulfonation of small molecules:R-HSA-156584 DED5UR3 PD 2Z5F; 3CKL DED5UR3 SQ MLSPKDILRKDLKLVHGYPMTCAFASNWEKIEQFHSRPDDIVIATYPKSGTTWVSEIIDMILNDGDIEKCKRGFITEKVPMLEMTLPGLRTSGIEQLEKNPSPRIVKTHLPTDLLPKSFWENNCKMIYLARNAKDVSVSYYHFDLMNNLQPFPGTWEEYLEKFLTGKVAYGSWFTHVKNWWKKKEEHPILFLYYEDMKENPKEEIKKIIRFLEKNLNDEILDRIIHHTSFEVMKDNPLVNYTHLPTTVMDHSKSPFMRKGTAGDWKNYFTVAQNEKFDAIYETEMSKTALQFRTEI DED5UR3 TD Primarily distributed in liver, peripheral blood leukocytes, colon, small intestine and spleen. DED5UR3 FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. It can also result in bioactivation to form active metabolites. It sulfates dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine, reverse triiodothyronine and thyroxine. DED5UR3 KD 33208: Metazoa DED5UR3 PL 7711: Chordata DED5UR3 CL 40674: Mammalia DED5UR3 OD 9443: Primates DED5UR3 FM 9604: Hominidae DED5UR3 GE 9605: Homo DED5UR3 SP 9606: Homo sapiens DEP76YL ID DEP76YL DEP76YL DN Dimethylaniline oxidase 3 (FMO3) DEP76YL GN FMO3 DEP76YL SN Dimethylaniline monooxygenase [N-oxide-forming] 3; FMO 3; FMO II; FMO form 2; FMO3; Hepatic flavin-containing monooxygenase 3; Trimethylamine monooxygenase DEP76YL UC FMO3_HUMAN DEP76YL RD Dasatinib DEP76YL GI 2328 DEP76YL E1 1: Oxidoreductase DEP76YL E2 1.14: Oxygen paired donor oxidoreductase DEP76YL E3 1.14.13: NADH/NADPH donor oxidoreductase DEP76YL EC 1.14.13.8 DEP76YL RC Defective FMO3 causes Trimethylaminuria (TMAU):R-HSA-5579019; FMO oxidises nucleophiles:R-HSA-217271 DEP76YL KG Drug metabolism - cytochrome P450:hsa00982 DEP76YL SQ MGKKVAIIGAGVSGLASIRSCLEEGLEPTCFEKSNDIGGLWKFSDHAEEGRASIYKSVFSNSSKEMMCFPDFPFPDDFPNFMHNSKIQEYIIAFAKEKNLLKYIQFKTFVSSVNKHPDFATTGQWDVTTERDGKKESAVFDAVMVCSGHHVYPNLPKESFPGLNHFKGKCFHSRDYKEPGVFNGKRVLVVGLGNSGCDIATELSRTAEQVMISSRSGSWVMSRVWDNGYPWDMLLVTRFGTFLKNNLPTAISDWLYVKQMNARFKHENYGLMPLNGVLRKEPVFNDELPASILCGIVSVKPNVKEFTETSAIFEDGTIFEGIDCVIFATGYSFAYPFLDESIIKSRNNEIILFKGVFPPLLEKSTIAVIGFVQSLGAAIPTVDLQSRWAAQVIKGTCTLPSMEDMMNDINEKMEKKRKWFGKSETIQTDYIVYMDELSSFIGAKPNIPWLFLTDPKLAMEVYFGPCSPYQFRLVGPGQWPGARNAILTQWDRSLKPMQTRVVGRLQKPCFFFHWLKLFAIPILLIAVFLVLT DEP76YL TD Primarily distributed in liver. DEP76YL FC This enzyme catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including drugs as well as dietary compounds. It plays an important role in the metabolism of trimethylamine (TMA), via the production of trimethylamine N-oxide (TMAO) metabolite. DEP76YL KD 33208: Metazoa DEP76YL PL 7711: Chordata DEP76YL CL 40674: Mammalia DEP76YL OD 9443: Primates DEP76YL FM 9604: Hominidae DEP76YL GE 9605: Homo DEP76YL SP 9606: Homo sapiens DEUWCVD ID DEUWCVD DEUWCVD DN Transglutaminase Y (TGM6) DEUWCVD GN TGM6 DEUWCVD SN Protein-glutamine gamma-glutamyltransferase Y; Transglutaminase-6; Protein-glutamine gamma-glutamyltransferase 6; Transglutaminase-3-like; TGase-3-like; TGase-6; TGase Y; TG6; TGM3L; TGM6; TGY DEUWCVD UC TGM3L_HUMAN DEUWCVD RD L-glutamine DEUWCVD GI 343641 DEUWCVD E1 2: Transferase DEUWCVD E2 2.3: Acyltransferase DEUWCVD E3 2.3.2: Aminoacyltransferase DEUWCVD EC 2.3.2.13 DEUWCVD SQ MAGIRVTKVDWQRSRNGAAHHTQEYPCPELVVRRGQSFSLTLELSRALDCEEILIFTMETGPRASEALHTKAVFQTSELERGEGWTAAREAQMEKTLTVSLASPPSAVIGRYLLSIRLSSHRKHSNRRLGEFVLLFNPWCAEDDVFLASEEERQEYVLSDSGIIFRGVEKHIRAQGWNYGQFEEDILNICLSILDRSPGHQNNPATDVSCRHNPIYVTRVISAMVNSNNDRGVVQGQWQGKYGGGTSPLHWRGSVAILQKWLKGRYKPVKYGQCWVFAGVLCTVLRCLGIATRVVSNFNSAHDTDQNLSVDKYVDSFGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYNGWQVLDATPQEESEGVFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDESRERVYSNTKKIGRCISTKAVGSDSRVDITDLYKYPEGSRKERQVYSKAVNRLFGVEASGRRIWIRRAGGRCLWRDDLLEPATKPSIAGKFKVLEPPMLGHDLRLALCLANLTSRAQRVRVNLSGATILYTRKPVAEILHESHAVRLGPQEEKRIPITISYSKYKEDLTEDKKILLAAMCLVTKGEKLLVEKDITLEDFITIKVLGPAMVGVAVTVEVTVVNPLIERVKDCALMVEGSGLLQEQLSIDVPTLEPQERASVQFDITPSKSGPRQLQVDLVSPHFPDIKGFVIVHVATAK DEUWCVD TD Primarily distributed in lymphoid tissue, skin and tongue. DEUWCVD FC This enzyme catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. DEUWCVD KD 33208: Metazoa DEUWCVD PL 7711: Chordata DEUWCVD CL 40674: Mammalia DEUWCVD OD 9443: Primates DEUWCVD FM 9604: Hominidae DEUWCVD GE 9605: Homo DEUWCVD SP 9606: Homo sapiens DEHKRDS ID DEHKRDS DEHKRDS DN Arylsulfatase B (ARSB) DEHKRDS GN ARSB DEHKRDS SN N-acetylgalactosamine-4-sulfatase; Arylsulfatase B component; ARSB; ASB; G4S DEHKRDS UC ARSB_HUMAN DEHKRDS RD Chondroitin sulfate DEHKRDS GI 411 DEHKRDS E1 3: Hydrolases DEHKRDS E2 3.1: Ester bond hydrolase DEHKRDS E3 3.1.6: Sulfuric ester hydrolase DEHKRDS EC 3.1.6.12 DEHKRDS RC CS/DS degradation:R-HSA-2024101; Glycosphingolipid metabolism:R-HSA-1660662; MPS VI - Maroteaux-Lamy syndrome:R-HSA-2206285; Neutrophil degranulation:R-HSA-6798695; The activation of arylsulfatases:R-HSA-1663150 DEHKRDS KG Glycosaminoglycan degradation:hsa00531; Lysosome:hsa04142; Metabolic pathways:hsa01100 DEHKRDS PD 1FSU DEHKRDS SQ MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLPEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM DEHKRDS TD Low tissue/organ specificity. DEHKRDS FC This enzyme removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation. DEHKRDS KD 33208: Metazoa DEHKRDS PL 7711: Chordata DEHKRDS CL 40674: Mammalia DEHKRDS OD 9443: Primates DEHKRDS FM 9604: Hominidae DEHKRDS GE 9605: Homo DEHKRDS SP 9606: Homo sapiens DE43MW5 ID DE43MW5 DE43MW5 DN Indoleamine 2,3-dioxygenase 1 (IDO1) DE43MW5 GN IDO1 DE43MW5 SN Indoleamine-pyrrole 2,3-dioxygenase; IDO; IDO-1; IDO1; INDO DE43MW5 UC I23O1_HUMAN DE43MW5 RD Melatonin DE43MW5 GI 3620 DE43MW5 E1 1: Oxidoreductase DE43MW5 E2 1.13: Oxygen single donor oxidoreductase DE43MW5 E3 1.13.11: Oxygen single donor oxidoreductase DE43MW5 EC 1.13.11.52 DE43MW5 RC Tryptophan catabolism:R-HSA-71240 DE43MW5 KG African trypanosomiasis:hsa05143; Metabolic pathways:hsa01100; Tryptophan metabolism:hsa00380 DE43MW5 PD 4PK5; 4PK6; 4U72; 4U74; 5EK2; 5EK3; 5EK4; 5ETW; 5WHR DE43MW5 SQ MAHAMENSWTISKEYHIDEEVGFALPNPQENLPDFYNDWMFIAKHLPDLIESGQLRERVEKLNMLSIDHLTDHKSQRLARLVLGCITMAYVWGKGHGDVRKVLPRNIAVPYCQLSKKLELPPILVYADCVLANWKKKDPNKPLTYENMDVLFSFRDGDCSKGFFLVSLLVEIAAASAIKVIPTVFKAMQMQERDTLLKALLEIASCLEKALQVFHQIHDHVNPKAFFSVLRIYLSGWKGNPQLSDGLVYEGFWEDPKEFAGGSAGQSSVFQCFDVLLGIQQTAGGGHAAQFLQDMRRYMPPAHRNFLCSLESNPSVREFVLSKGDAGLREAYDACVKALVSLRSYHLQIVTKYILIPASQQPKENKTSEDPSKLEAKGTGGTDLMNFLKTVRSTTEKSLLKEG DE43MW5 TD Primarily distributed in blood and placenta. DE43MW5 FC This enzyme catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. DE43MW5 KD 33208: Metazoa DE43MW5 PL 7711: Chordata DE43MW5 CL 40674: Mammalia DE43MW5 OD 9443: Primates DE43MW5 FM 9604: Hominidae DE43MW5 GE 9605: Homo DE43MW5 SP 9606: Homo sapiens DEXZA9U ID DEXZA9U DEXZA9U DN Cytochrome P450 2A13 (CYP2A13) DEXZA9U GN CYP2A13 DEXZA9U SN Cytochrome P450 family 2 subfamily A member 13; CYP2A13; CYPIIA13; CPAD; CYP2A DEXZA9U UC CP2AD_HUMAN DEXZA9U RD Testosterone cypionate DEXZA9U GI 1553 DEXZA9U E1 1: Oxidoreductase DEXZA9U E2 1.14: Oxygen paired donor oxidoreductase DEXZA9U E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEXZA9U EC 1.14.14.1 DEXZA9U RC Aflatoxin activation and detoxification:R-HSA-5423646; CYP2E1 reactions:R-HSA-211999; Fatty acids:R-HSA-211935; Xenobiotics:R-HSA-211981 DEXZA9U KG Chemical carcinogenesis:hsa05204; Metabolism of xenobiotics by cytochrome P450:hsa00980 DEXZA9U PD 2P85; 2PG5; 2PG6; 2PG7; 3T3S; 4EJG; 4EJH; 4EJI DEXZA9U SQ MLASGLLLVTLLACLTVMVLMSVWRQRKSRGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVLCGHDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSIATLRGFGVGKRGIEERIQEEAGFLIDALRGTHGANIDPTFFLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFSSVMKHLPGPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYTEAVIHEIQRFGDMLPMGLAHRVNKDTKFRDFFLPKGTEVFPMLGSVLRDPRFFSNPRDFNPQHFLDKKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPKDIDVSPKHVGFATIPRNYTMSFLPR DEXZA9U TD Primarily distributed in liver. Also expressed in a number of extrahepatictissues, including nasal mucosa, lung, trachea, brain, mammary gland,prostate, testis and uterus. DEXZA9U FC This enzyme exhibits a coumarin 7-hydroxylase activity and is active in the metabolic activation of hexamethylphosphoramide, N,N-dimethylaniline, 2'-methoxyacetophenone, N-nitrosomethylphenylamine, and the tobacco- specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. It possesses phenacetin O-deethylation activity. DEXZA9U KD 33208: Metazoa DEXZA9U PL 7711: Chordata DEXZA9U CL 40674: Mammalia DEXZA9U OD 9443: Primates DEXZA9U FM 9604: Hominidae DEXZA9U GE 9605: Homo DEXZA9U SP 9606: Homo sapiens DEL45C2 ID DEL45C2 DEL45C2 DN Iduronate 2-sulfatase (IDS) DEL45C2 GN IDS DEL45C2 SN Idursulfase; Alpha-L-iduronate sulfate sulfatase; Iduronate 2-sulfatase 14 kDa chain; Iduronate 2-sulfatase 42 kDa chain; IDS; SIDS DEL45C2 UC IDS_HUMAN DEL45C2 RD Chondroitin sulfate DEL45C2 GI 3423 DEL45C2 E1 3: Hydrolases DEL45C2 E2 3.1: Ester bond hydrolase DEL45C2 E3 3.1.6: Sulfuric ester hydrolase DEL45C2 EC 3.1.6.13 DEL45C2 RC CS/DS degradation:R-HSA-2024101; HS-GAG degradation:R-HSA-2024096; MPS II - Hunter syndrome:R-HSA-2206296 DEL45C2 KG Glycosaminoglycan degradation:hsa00531; Lysosome:hsa04142; Metabolic pathways:hsa01100 DEL45C2 PD 5FQL; 6IOZ DEL45C2 SQ MPPPRTGRGLLWLGLVLSSVCVALGSETQANSTTDALNVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDDLQLANSTIIAFTSDHGWALGEHGEWAKYSNFDVATHVPLIFYVPGRTASLPEAGEKLFPYLDPFDSASQLMEPGRQSMDLVELVSLFPTLAGLAGLQVPPRCPVPSFHVELCREGKNLLKHFRFRDLEEDPYLPGNPRELIAYSQYPRPSDIPQWNSDKPSLKDIKIMGYSIRTIDYRYTVWVGFNPDEFLANFSDIHAGELYFVDSDPLQDHNMYNDSQGGDLFQLLMP DEL45C2 TD Primarily distributed in liver, kidney, lung, and placenta. DEL45C2 FC This enzyme is involved in the degradation pathway of dermatan sulfate and heparan sulfate. DEL45C2 KD 33208: Metazoa DEL45C2 PL 7711: Chordata DEL45C2 CL 40674: Mammalia DEL45C2 OD 9443: Primates DEL45C2 FM 9604: Hominidae DEL45C2 GE 9605: Homo DEL45C2 SP 9606: Homo sapiens DEMI4VE ID DEMI4VE DEMI4VE DN Carboxylesterase 3 (CES3) DEMI4VE GN CES3 DEMI4VE SN Liver carboxylesterase 3; Liver carboxylesterase 31 homolog; CES3; UNQ869/PRO1887 DEMI4VE UC EST3_HUMAN DEMI4VE RD Irinotecan hydrochloride DEMI4VE GI 23491 DEMI4VE E1 3: Hydrolases DEMI4VE E2 3.1: Ester bond hydrolase DEMI4VE E3 3.1.1: Carboxylic ester hydrolase DEMI4VE EC 3.1.1.1 DEMI4VE RC LDL clearance:R-HSA-8964038; Phase I - Functionalization of compounds:R-HSA-211945 DEMI4VE SQ MERAVRVESGVLVGVVCLLLACPATATGPEVAQPEVDTTLGRVRGRQVGVKGTDRLVNVFLGIPFAQPPLGPDRFSAPHPAQPWEGVRDASTAPPMCLQDVESMNSSRFVLNGKQQIFSVSEDCLVLNVYSPAEVPAGSGRPVMVWVHGGALITGAATSYDGSALAAYGDVVVVTVQYRLGVLGFFSTGDEHAPGNQGFLDVVAALRWVQENIAPFGGDLNCVTVFGGSAGGSIISGLVLSPVAAGLFHRAITQSGVITTPGIIDSHPWPLAQKIANTLACSSSSPAEMVQCLQQKEGEELVLSKKLKNTIYPLTVDGTVFPKSPKELLKEKPFHSVPFLMGVNNHEFSWLIPRGWGLLDTMEQMSREDMLAISTPVLTSLDVPPEMMPTVIDEYLGSNSDAQAKCQAFQEFMGDVFINVPTVSFSRYLRDSGSPVFFYEFQHRPSSFAKIKPAWVKADHGAEGAFVFGGPFLMDESSRLAFPEATEEEKQLSLTMMAQWTHFARTGDPNSKALPPWPQFNQAEQYLEINPVPRAGQKFREAWMQFWSETLPSKIQQWHQKQKNRKAQEDL DEMI4VE TD Primarily distributed in intestine and liver. DEMI4VE FC This enzyme is involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. It shows low catalytic efficiency for hydrolysis of CPT-11 (7-ethyl-10-[4-(1-piperidino)-1-piperidino]- carbonyloxycamptothecin), a prodrug for camptothecin used in cancer therapeutics. DEMI4VE KD 33208: Metazoa DEMI4VE PL 7711: Chordata DEMI4VE CL 40674: Mammalia DEMI4VE OD 9443: Primates DEMI4VE FM 9604: Hominidae DEMI4VE GE 9605: Homo DEMI4VE SP 9606: Homo sapiens DE4HCYL ID DE4HCYL DE4HCYL DN Thymidine phosphorylase (TYMP) DE4HCYL GN TYMP DE4HCYL SN Platelet-derived endothelial cell growth factor; Gliostatin; TdRPase; PD-ECGF; ECGF1; TP; TYMP DE4HCYL UC TYPH_HUMAN DE4HCYL RD Floxuridine DE4HCYL GI 1890 DE4HCYL E1 2: Transferase DE4HCYL E2 2.4: Glycosyltransferases DE4HCYL E3 2.4.2: Pentosyltransferase DE4HCYL EC 2.4.2.4 DE4HCYL RC Pyrimidine catabolism:R-HSA-73621; Pyrimidine salvage:R-HSA-73614 DE4HCYL KG Bladder cancer:hsa05219; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DE4HCYL PD 1UOU; 2J0F; 2WK5; 2WK6 DE4HCYL SQ MAALMTPGTGAPPAPGDFSGEGSQGLPDPSPEPKQLPELIRMKRDGGRLSEADIRGFVAAVVNGSAQGAQIGAMLMAIRLRGMDLEETSVLTQALAQSGQQLEWPEAWRQQLVDKHSTGGVGDKVSLVLAPALAACGCKVPMISGRGLGHTGGTLDKLESIPGFNVIQSPEQMQVLLDQAGCCIVGQSEQLVPADGILYAARDVTATVDSLPLITASILSKKLVEGLSALVVDVKFGGAAVFPNQEQARELAKTLVGVGASLGLRVAAALTAMDKPLGRCVGHALEVEEALLCMDGAGPPDLRDLVTTLGGALLWLSGHAGTQAQGAARVAAALDDGSALGRFERMLAAQGVDPGLARALCSGSPAERRQLLPRAREQEELLAPADGTVELVRALPLALVLHELGAGRSRAGEPLRLGVGAELLVDVGQRLRRGTPWLRVHRDGPALSGPQSRALQEALVLSDRAPFAAPSPFAELVLPPQQ DE4HCYL TD Primarily distributed in lymphoid. DE4HCYL FC This enzyme catalyzes the reversible phosphorolysis of thymidine. DE4HCYL KD 33208: Metazoa DE4HCYL PL 7711: Chordata DE4HCYL CL 40674: Mammalia DE4HCYL OD 9443: Primates DE4HCYL FM 9604: Hominidae DE4HCYL GE 9605: Homo DE4HCYL SP 9606: Homo sapiens DEO1IE3 ID DEO1IE3 DEO1IE3 DN Cytochrome P450 3A43 (CYP3A43) DEO1IE3 GN CYP3A43 DEO1IE3 SN Cytochrome P450 family 3 subfamily A member 43; CYP3A43; OMIM: 606534; HomoloGene: 136124; GeneCards: CYP3A43 DEO1IE3 UC CP343_HUMAN DEO1IE3 RD Oxazepam DEO1IE3 GI 64816 DEO1IE3 E1 1: Oxidoreductase DEO1IE3 E2 1.14: Oxygen paired donor oxidoreductase DEO1IE3 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEO1IE3 EC 1.14.14.1 DEO1IE3 RC Miscellaneous substrates:R-HSA-211958; Xenobiotics:R-HSA-211981 DEO1IE3 KG Chemical carcinogenesis:hsa05204 DEO1IE3 SQ MDLIPNFAMETWVLVATSLVLLYIYGTHSHKLFKKLGIPGPTPLPFLGTILFYLRGLWNFDRECNEKYGEMWGLYEGQQPMLVIMDPDMIKTVLVKECYSVFTNQMPLGPMGFLKSALSFAEDEEWKRIRTLLSPAFTSVKFKEMVPIISQCGDMLVRSLRQEAENSKSINLKDFFGAYTMDVITGTLFGVNLDSLNNPQDPFLKNMKKLLKLDFLDPFLLLISLFPFLTPVFEALNIGLFPKDVTHFLKNSIERMKESRLKDKQKHRVDFFQQMIDSQNSKETKSHKALSDLELVAQSIIIIFAAYDTTSTTLPFIMYELATHPDVQQKLQEEIDAVLPNKAPVTYDALVQMEYLDMVVNETLRLFPVVSRVTRVCKKDIEINGVFIPKGLAVMVPIYALHHDPKYWTEPEKFCPERFSKKNKDSIDLYRYIPFGAGPRNCIGMRFALTNIKLAVIRALQNFSFKPCKETQIPLKLDNLPILQPEKPIVLKVHLRDGITSGP DEO1IE3 TD Primarily distributed in prostate, liver, kidney, pancreas, fetal liver and fetal skeletalmuscle. DEO1IE3 FC This enzyme exhibits low testosterone 6-beta-hydroxylase activity. DEO1IE3 KD 33208: Metazoa DEO1IE3 PL 7711: Chordata DEO1IE3 CL 40674: Mammalia DEO1IE3 OD 9443: Primates DEO1IE3 FM 9604: Hominidae DEO1IE3 GE 9605: Homo DEO1IE3 SP 9606: Homo sapiens DEKP5HX ID DEKP5HX DEKP5HX DN Cholesterol 24-hydroxylase (CYP46A1) DEKP5HX GN CYP46A1 DEKP5HX SN Cholesterol 24-monooxygenase; Cholesterol 24S-hydroxylase; Cytochrome P450 46A1; CH24H; CYP46; CYP46A1 DEKP5HX UC CP46A_HUMAN DEKP5HX RD Diclofenac sodium DEKP5HX GI 10858 DEKP5HX E1 1: Oxidoreductase DEKP5HX E2 1.14: Oxygen paired donor oxidoreductase DEKP5HX E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEKP5HX EC 1.14.14.25 DEKP5HX RC Endogenous sterols:R-HSA-211976; Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775 DEKP5HX KG Primary bile acid biosynthesis:hsa00120 DEKP5HX PD 2Q9F; 2Q9G; 3MDM; 3MDR; 3MDT; 3MDV; 4ENH; 4FIA; 4J14 DEKP5HX SQ MSPGLLLLGSAVLLAFGLCCTFVHRARSRYEHIPGPPRPSFLLGHLPCFWKKDEVGGRVLQDVFLDWAKKYGPVVRVNVFHKTSVIVTSPESVKKFLMSTKYNKDSKMYRALQTVFGERLFGQGLVSECNYERWHKQRRVIDLAFSRSSLVSLMETFNEKAEQLVEILEAKADGQTPVSMQDMLTYTAMDILAKAAFGMETSMLLGAQKPLSQAVKLMLEGITASRNTLAKFLPGKRKQLREVRESIRFLRQVGRDWVQRRREALKRGEEVPADILTQILKAEEGAQDDEGLLDNFVTFFIAGHETSANHLAFTVMELSRQPEIVARLQAEVDEVIGSKRYLDFEDLGRLQYLSQVLKESLRLYPPAWGTFRLLEEETLIDGVRVPGNTPLLFSTYVMGRMDTYFEDPLTFNPDRFGPGAPKPRFTYFPFSLGHRSCIGQQFAQMEVKVVMAKLLQRLEFRLVPGQRFGLQEQATLKPLDPVLCTLRPRGWQPAPPPPPC DEKP5HX TD Primarily distributed in brain. DEKP5HX FC This enzyme catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation. It further hydroxylates cholesterol derivatives and hormone steroids on both the ring and side chain of these molecules, converting them into active oxysterols involved in lipid signaling and biosynthesis. It acts as an epoxidase converting cholesta-5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, Besides, it may also catalyze the oxidative metabolism of xenobiotics, such as clotrimazole. DEKP5HX KD 33208: Metazoa DEKP5HX PL 7711: Chordata DEKP5HX CL 40674: Mammalia DEKP5HX OD 9443: Primates DEKP5HX FM 9604: Hominidae DEKP5HX GE 9605: Homo DEKP5HX SP 9606: Homo sapiens DE5ME8A ID DE5ME8A DE5ME8A DN Metallothionein-1A (MT1A) DE5ME8A GN MT1A DE5ME8A SN Metallothionein-IA; MT-1A; MT-IA; MT1A; MT1S; OMIM: 156350; GeneCards: MT1A DE5ME8A UC MT1A_HUMAN DE5ME8A RD Carboplatin DE5ME8A GI 4489 DE5ME8A E1 1: Oxidoreductase DE5ME8A E2 1.8: Sulfur donor oxidoreductase DE5ME8A E3 1.8.5: Quinone acceptor oxidoreductase DE5ME8A EC 1.8.5.1 DE5ME8A RC Metallothioneins bind metals:R-HSA-5661231 DE5ME8A KG Mineral absorption:hsa04978 DE5ME8A SQ MDPNCSCATGGSCTCTGSCKCKECKCTSCKKSCCSCCPMSCAKCAQGCICKGASEKCSCCA DE5ME8A TD Primarily distributed in adipose tissue, liver and skeletal muscle. DE5ME8A FC This enzyme acts as anti-oxidants, protect against hydroxyl free radicals, are important in homeostatic control of metal in the cell, and play a role in detoxification of heavy metals. DE5ME8A KD 33208: Metazoa DE5ME8A PL 7711: Chordata DE5ME8A CL 40674: Mammalia DE5ME8A OD 9443: Primates DE5ME8A FM 9604: Hominidae DE5ME8A GE 9605: Homo DE5ME8A SP 9606: Homo sapiens DETE84Z ID DETE84Z DETE84Z DN Eosinophil peroxidase (EPX) DETE84Z GN EPX DETE84Z SN Eosinophil peroxidase heavy chain; Eosinophil peroxidase light chain; EPER; EPO; EPP; EPX DETE84Z UC PERE_HUMAN DETE84Z RD Riboflavin DETE84Z GI 8288 DETE84Z E1 1: Oxidoreductase DETE84Z E2 1.11: Peroxidase DETE84Z E3 1.11.1: Peroxidase DETE84Z EC 1.11.1.7 DETE84Z RC Neutrophil degranulation:R-HSA-6798695 DETE84Z KG Asthma:hsa05310 DETE84Z SQ MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQRLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTEPQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLSLPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPESPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRNQINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARKIMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPFMFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDELRDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLARKFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTKRQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT DETE84Z TD Primarily distributed in bone marrow and lymphoid tissue. DETE84Z FC This enzyme mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils and shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis. DETE84Z KD 33208: Metazoa DETE84Z PL 7711: Chordata DETE84Z CL 40674: Mammalia DETE84Z OD 9443: Primates DETE84Z FM 9604: Hominidae DETE84Z GE 9605: Homo DETE84Z SP 9606: Homo sapiens DEPTKBQ ID DEPTKBQ DEPTKBQ DN Tryptophanyl-tRNA synthetase mitochondrial (WARS2) DEPTKBQ GN WARS2 DEPTKBQ SN Mitochondrial tryptophan--tRNA ligase; Mitochondrial tryptophan-tRNA ligase; (Mt)TrpRS; WARS2 DEPTKBQ UC SYWM_HUMAN DEPTKBQ RD TRP-01 DEPTKBQ GI 10352 DEPTKBQ E1 6: Ligase DEPTKBQ E2 6.1: Carbon-oxygen ligase DEPTKBQ E3 6.1.1: Aminoacyl tRNA synthetase DEPTKBQ EC 6.1.1.2 DEPTKBQ RC Mitochondrial tRNA aminoacylation:R-HSA-379726 DEPTKBQ KG Aminoacyl-tRNA biosynthesis:hsa00970 DEPTKBQ PD 5EKD DEPTKBQ SQ MALHSMRKARERWSFIRALHKGSAAAPALQKDSKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKLVGFL DEPTKBQ TD Low tissue/organ specificity. DEPTKBQ FC This enzyme activates and transfers the amino acids to their corresponding tRNAs during the translation of mitochondrial genes and protein synthesis. DEPTKBQ KD 33208: Metazoa DEPTKBQ PL 7711: Chordata DEPTKBQ CL 40674: Mammalia DEPTKBQ OD 9443: Primates DEPTKBQ FM 9604: Hominidae DEPTKBQ GE 9605: Homo DEPTKBQ SP 9606: Homo sapiens DEP5BDK ID DEP5BDK DEP5BDK DN Tryptophan 5-hydroxylase 1 (TPH1) DEP5BDK GN TPH1 DEP5BDK SN Tryptophan 5-monooxygenase 1; Normal tryptophan hydroxylase; TPH; TPH1; TPRH; TRPH DEP5BDK UC TPH1_HUMAN DEP5BDK RD TRP-01 DEP5BDK GI 7166 DEP5BDK E1 1: Oxidoreductase DEP5BDK E2 1.14: Oxygen paired donor oxidoreductase DEP5BDK E3 1.14.16: Pteridine donor oxidoreductase DEP5BDK EC 1.14.16.4 DEP5BDK RC Serotonin and melatonin biosynthesis:R-HSA-209931 DEP5BDK KG Folate biosynthesis:hsa00790; Metabolic pathways:hsa01100; Serotonergic synapse:hsa04726; Tryptophan metabolism:hsa00380 DEP5BDK PD 1IN9; 1MLW; 3HF6; 3HF8; 3HFB; 5J6D; 5L01; 5TPG DEP5BDK SQ MIEDNKENKDHSLERGRASLIFSLKNEVGGLIKALKIFQEKHVNLLHIESRKSKRRNSEFEIFVDCDINREQLNDIFHLLKSHTNVLSVNLPDNFTLKEDGMETVPWFPKKISDLDHCANRVLMYGSELDADHPGFKDNVYRKRRKYFADLAMNYKHGDPIPKVEFTEEEIKTWGTVFQELNKLYPTHACREYLKNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPFYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEEAVQKLATCYFFTVEFGLCKQDGQLRVFGAGLLSSISELKHALSGHAKVKPFDPKITCKQECLITTFQDVYFVSESFEDAKEKMREFTKTIKRPFGVKYNPYTRSIQILKDTKSITSAMNELQHDLDVVSDALAKVSRKPSI DEP5BDK TD Primarily distributed in brain, intestine, pituitary gland and stomach. DEP5BDK FC This enzyme catalyzes the formation of 5-hydroxytryptophan, a precursor to the neurotransmitter serotonin. DEP5BDK KD 33208: Metazoa DEP5BDK PL 7711: Chordata DEP5BDK CL 40674: Mammalia DEP5BDK OD 9443: Primates DEP5BDK FM 9604: Hominidae DEP5BDK GE 9605: Homo DEP5BDK SP 9606: Homo sapiens DERUZL7 ID DERUZL7 DERUZL7 DN Sulfotransferase 1A2 (SULT1A2) DERUZL7 GN SULT1A2 DERUZL7 SN Sulfotransferase family cytosolic 1A member 2; Aryl sulfotransferase 1A2; Aryl sulfotransferase 2; Phenol sulfotransferase 2; Phenol-sulfating phenol sulfotransferase 2; P-PST 2; ST1A2; STP2; SULT1A2 DERUZL7 UC ST1A2_HUMAN DERUZL7 RD Rotigotine DERUZL7 GI 6799 DERUZL7 E1 2: Transferase DERUZL7 E2 2.8: Sulfotransferase DERUZL7 E3 2.8.2: Sulfotransferase DERUZL7 EC 2.8.2.1 DERUZL7 RC Cytosolic sulfonation of small molecules:R-HSA-156584 DERUZL7 KG Chemical carcinogenesis:hsa05204 DERUZL7 PD 1Z29 DERUZL7 SQ MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAKKMAGCSLSFRSEL DERUZL7 TD Primarily distributed in intestine, liver and seminal vesicle. DERUZL7 FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. It is also responsible for the sulfonation and activation of minoxidil. And it mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products. DERUZL7 KD 33208: Metazoa DERUZL7 PL 7711: Chordata DERUZL7 CL 40674: Mammalia DERUZL7 OD 9443: Primates DERUZL7 FM 9604: Hominidae DERUZL7 GE 9605: Homo DERUZL7 SP 9606: Homo sapiens DESITDW ID DESITDW DESITDW DN Tartrate-resistant acid ATPase (ACP5) DESITDW GN ACP5 DESITDW SN Tartrate-resistant acid phosphatase type 5; Type 5 acid phosphatase; TrATPase; ACP5; TR-AP DESITDW UC PPA5_HUMAN DESITDW RD Riboflavin DESITDW GI 54 DESITDW E1 3: Hydrolases DESITDW E2 3.1: Ester bond hydrolase DESITDW E3 3.1.3: Phosphoric monoester hydrolase DESITDW EC 3.1.3.2 DESITDW RC Vitamin B2 (riboflavin) metabolism:R-HSA-196843 DESITDW KG Lysosome:hsa04142; Metabolic pathways:hsa01100; Osteoclast differentiation:hsa04380; Rheumatoid arthritis:hsa05323; Riboflavin metabolism:hsa00740 DESITDW PD 1WAR; 2BQ8 DESITDW SQ MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQIAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASGKSLFKTRLPRRARP DESITDW TD Primarily distributed in adipose tissue and lung. DESITDW FC This enzyme is involved in osteopontin/bone sialoprotein dephosphorylation. DESITDW KD 33208: Metazoa DESITDW PL 7711: Chordata DESITDW CL 40674: Mammalia DESITDW OD 9443: Primates DESITDW FM 9604: Hominidae DESITDW GE 9605: Homo DESITDW SP 9606: Homo sapiens DE7P2FB ID DE7P2FB DE7P2FB DN Aldo-keto reductase 1C1 (AKR1C1) DE7P2FB GN AKR1C1 DE7P2FB SN Aldo-keto reductase family 1 member C1; Chlordecone reductase homolog HAKRC; DD1/DD2; DDH; DDH1; Dihydrodiol dehydrogenase 1/2; HBAB; High-affinity hepatic bile acid-binding protein; Indanol dehydrogenase; Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; 20-alpha-hydroxysteroid dehydrogenase; AKR1C1 DE7P2FB UC AK1C1_HUMAN DE7P2FB RD Progesterone DE7P2FB GI 1645 DE7P2FB E1 1: Oxidoreductase DE7P2FB E2 1.1: CH-OH donor oxidoreductase DE7P2FB E3 1.1.1: NAD/NADP oxidoreductase DE7P2FB EC 1.1.1.149 DE7P2FB RC Retinoid metabolism and transport:R-HSA-975634; Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DE7P2FB KG Metabolism of xenobiotics by cytochrome P450:hsa00980; Steroid hormone biosynthesis:hsa00140 DE7P2FB PD 1MRQ; 3C3U; 3GUG; 3NTY; 4YVP; 6A7A; 6IJX DE7P2FB SQ MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY DE7P2FB TD Primarily distributed in liver, mammary gland and brain. DE7P2FB FC This enzyme converts progesterone to its inactive form, 20-alpha- dihydroxyprogesterone (20-alpha-OHP). DE7P2FB KD 33208: Metazoa DE7P2FB PL 7711: Chordata DE7P2FB CL 40674: Mammalia DE7P2FB OD 9443: Primates DE7P2FB FM 9604: Hominidae DE7P2FB GE 9605: Homo DE7P2FB SP 9606: Homo sapiens DE3Z9HM ID DE3Z9HM DE3Z9HM DN Ecto-5'-nucleotidase (NT5E) DE3Z9HM GN NT5E DE3Z9HM SN Ecto-nucleotidase; 5'-NT; 5'-nucleotidase; Ectonucleotidase; CD73; NT5; NT5E; NTE DE3Z9HM UC 5NTD_HUMAN DE3Z9HM RD Cytarabine DE3Z9HM GI 4907 DE3Z9HM E1 3: Hydrolases DE3Z9HM E2 3.1: Ester bond hydrolase DE3Z9HM E3 3.1.3: Phosphoric monoester hydrolase DE3Z9HM EC 3.1.3.5 DE3Z9HM RC Nicotinate metabolism:R-HSA-196807; Purine catabolism:R-HSA-74259; Pyrimidine catabolism:R-HSA-73621 DE3Z9HM KG Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760; Purine metabolism:hsa00230; Pyrimidine metabolism:hsa00240 DE3Z9HM PD 4H1S; 4H1Y; 4H2B; 4H2F; 4H2G; 4H2I; 6HXW DE3Z9HM SQ MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGGVARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYKGAEVAHFMNALRYDAMALGNHEFDNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKETPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVVGGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNVISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNMGNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGTFDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCRVPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYPAVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ DE3Z9HM TD Low tissue/organ specificity. DE3Z9HM FC This enzyme hydrolyzes extracellular nucleotides into membrane permeable nucleosides and exhibits AMP-, NAD-, and NMN-nucleosidase activities. DE3Z9HM KD 33208: Metazoa DE3Z9HM PL 7711: Chordata DE3Z9HM CL 40674: Mammalia DE3Z9HM OD 9443: Primates DE3Z9HM FM 9604: Hominidae DE3Z9HM GE 9605: Homo DE3Z9HM SP 9606: Homo sapiens DEA3U9Y ID DEA3U9Y DEA3U9Y DN Myeloperoxidase (MPO) DEA3U9Y GN MPO DEA3U9Y SN Myeloperoxidase heavy chain; Myeloperoxidase light chain; 84 kDa myeloperoxidase; 89 kDa myeloperoxidase; MPO DEA3U9Y UC PERM_HUMAN DEA3U9Y RD Carboplatin DEA3U9Y GI 4353 DEA3U9Y E1 1: Oxidoreductase DEA3U9Y E2 1.11: Peroxidase DEA3U9Y E3 1.11.2: Peroxygenase DEA3U9Y EC 1.11.2.2 DEA3U9Y RC Events associated with phagocytolytic activity of PMN cells:R-HSA-8941413; Neutrophil degranulation:R-HSA-6798695 DEA3U9Y KG Acute myeloid leukemia:hsa05221; Drug metabolism - other enzymes:hsa00983; Phagosome:hsa04145; Transcriptional misregulation in cancer:hsa05202 DEA3U9Y PD 1D5L; 1D7W; 1DNU; 1DNW; 1MHL; 1MYP; 3F9P; 3ZS0; 3ZS1 DEA3U9Y SQ MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTSLVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLHVALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREAS DEA3U9Y TD Primarily distributed in bone. DEA3U9Y FC This enzyme oxidizes tyrosine to tyrosyl radical using hydrogen peroxide as an oxidizing agent. DEA3U9Y KD 33208: Metazoa DEA3U9Y PL 7711: Chordata DEA3U9Y CL 40674: Mammalia DEA3U9Y OD 9443: Primates DEA3U9Y FM 9604: Hominidae DEA3U9Y GE 9605: Homo DEA3U9Y SP 9606: Homo sapiens DEFKGT7 ID DEFKGT7 DEFKGT7 DN Metallothionein-2A (MT2A) DEFKGT7 GN MT2A DEFKGT7 SN Metallothionein-II; Metallothionein-2; MT-2; MT-II; MT2; MT2A DEFKGT7 UC MT2_HUMAN DEFKGT7 RD Cisplatin DEFKGT7 GI 4502 DEFKGT7 E1 1: Oxidoreductase DEFKGT7 E2 1.8: Sulfur donor oxidoreductase DEFKGT7 E3 1.8.5: Quinone acceptor oxidoreductase DEFKGT7 EC 1.8.5.1 DEFKGT7 RC Interferon gamma signaling:R-HSA-877300; Metallothioneins bind metals:R-HSA-5661231 DEFKGT7 KG Mineral absorption:hsa04978 DEFKGT7 PD 1MHU; 2MHU DEFKGT7 SQ MDPNCSCAAGDSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA DEFKGT7 TD Primarily distributed in liver. DEFKGT7 FC This enzyme acts as anti-oxidants, protect against hydroxyl free radicals, are important in homeostatic control of metal in the cell, and play a role in detoxification of heavy metals. DEFKGT7 KD 33208: Metazoa DEFKGT7 PL 7711: Chordata DEFKGT7 CL 40674: Mammalia DEFKGT7 OD 9443: Primates DEFKGT7 FM 9604: Hominidae DEFKGT7 GE 9605: Homo DEFKGT7 SP 9606: Homo sapiens DE1ZNSC ID DE1ZNSC DE1ZNSC DN Heparanase (HPSE) DE1ZNSC GN HPSE DE1ZNSC SN Endo-glucoronidase; Heparanase 50 kDa subunit; Heparanase 8 kDa subunit; Heparanase-1; HEP; HPA; HPA1; Hpa1; HPR1; HPSE; HPSE1; HSE1 DE1ZNSC UC HPSE_HUMAN DE1ZNSC RD Heparin DE1ZNSC GI 10855 DE1ZNSC E1 3: Hydrolases DE1ZNSC E2 3.2: Glycosylase DE1ZNSC E3 3.2.1: O/S-glycosyl compound glycosidase DE1ZNSC EC 3.2.1.166 DE1ZNSC RC HS-GAG degradation:R-HSA-2024096; Neutrophil degranulation:R-HSA-6798695 DE1ZNSC KG Glycosaminoglycan degradation:hsa00531; Metabolic pathways:hsa01100; Proteoglycans in cancer:hsa05205 DE1ZNSC PD 5E8M; 5E97; 5E98; 5E9B; 5E9C; 5L9Y; 5L9Z; 5LA4; 5LA7 DE1ZNSC SQ MLLRSKPALPPPLMLLLLGPLGPLSPGALPRPAQAQDVVDLDFFTQEPLHLVSPSFLSVTIDANLATDPRFLILLGSPKLRTLARGLSPAYLRFGGTKTDFLIFDPKKESTFEERSYWQSQVNQDICKYGSIPPDVEEKLRLEWPYQEQLLLREHYQKKFKNSTYSRSSVDVLYTFANCSGLDLIFGLNALLRTADLQWNSSNAQLLLDYCSSKGYNISWELGNEPNSFLKKADIFINGSQLGEDFIQLHKLLRKSTFKNAKLYGPDVGQPRRKTAKMLKSFLKAGGEVIDSVTWHHYYLNGRTATKEDFLNPDVLDIFISSVQKVFQVVESTRPGKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLGLSARMGIEVVMRQVFFGAGNYHLVDENFDPLPDYWLSLLFKKLVGTKVLMASVQGSKRRKLRVYLHCTNTDNPRYKEGDLTLYAINLHNVTKYLRLPYPFSNKQVDKYLLRPLGPHGLLSKSVQLNGLTLKMVDDQTLPPLMEKPLRPGSSLGLPAFSYSFFVIRNAKVAACI DE1ZNSC TD Primarily distributed in placenta and spleen. Also expressed in lymph node, thymus, peripheral blood leukocytes, bonemarrow, endothelial cells and fetal liver. DE1ZNSC FC This enzyme cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. It selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. It can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. DE1ZNSC KD 33208: Metazoa DE1ZNSC PL 7711: Chordata DE1ZNSC CL 40674: Mammalia DE1ZNSC OD 9443: Primates DE1ZNSC FM 9604: Hominidae DE1ZNSC GE 9605: Homo DE1ZNSC SP 9606: Homo sapiens DET2NXO ID DET2NXO DET2NXO DN Monoamine oxidase type B (MAO-B) DET2NXO GN MAOB DET2NXO SN Amine oxidase [flavin-containing] B; Monoamine oxidase B; MAO-B; MAOB DET2NXO UC AOFB_HUMAN DET2NXO RD Dopamine hydrochloride DET2NXO GI 4129 DET2NXO E1 1: Oxidoreductase DET2NXO E2 1.4: CH-NH2 donor oxidoreductase DET2NXO E3 1.4.3: Oxygen acceptor oxidoreductase DET2NXO EC 1.4.3.4 DET2NXO RC Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB:R-HSA-141333 DET2NXO KG Alcoholism:hsa05034; Amphetamine addiction:hsa05031; Arginine and proline metabolism:hsa00330; Cocaine addiction:hsa05030; Dopaminergic synapse:hsa04728; Drug metabolism - cytochrome P450:hsa00982; Glycine, serine and threonine metabolism:hsa00260; Histidine metabolism:hsa00340; Metabolic pathways:hsa01100; Phenylalanine metabolism:hsa00360; Serotonergic synapse:hsa04726; Tryptophan metabolism:hsa00380; Tyrosine metabolism:hsa00350 DET2NXO PD 1OJ9; 1OJA; 1OJC; 1OJD; 1S2Q; 1S2Y; 1S3B; 1S3E; 2BK3 DET2NXO SQ MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV DET2NXO TD Primarily distributed in liver. DET2NXO FC This enzyme catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine. DET2NXO KD 33208: Metazoa DET2NXO PL 7711: Chordata DET2NXO CL 40674: Mammalia DET2NXO OD 9443: Primates DET2NXO FM 9604: Hominidae DET2NXO GE 9605: Homo DET2NXO SP 9606: Homo sapiens DE87OZS ID DE87OZS DE87OZS DN Arachidonate 5-lipoxygenase (ALOX5) DE87OZS GN ALOX5 DE87OZS SN Enzyme 5-lipoxygenase; 5-lipoxygenase; ALOX5; LOG5; Alox5; 5-LOX; 5LO; 5LX; AI850497; F730011J02; 5LPG; 5-LO DE87OZS UC LOX5_HUMAN DE87OZS RD Omega-3 Fatty acids DE87OZS GI 240 DE87OZS E1 1: Oxidoreductase DE87OZS E2 1.13: Oxygen single donor oxidoreductase DE87OZS E3 1.13.11: Oxygen single donor oxidoreductase DE87OZS EC 1.13.11.34 DE87OZS RC Biosynthesis of D-series resolvins:R-HSA-9018676; Biosynthesis of DPAn-3-derived 13-series resolvins:R-HSA-9026403; Biosynthesis of DPAn-3-derived maresins:R-HSA-9026290; Biosynthesis of DPAn-3-derived protectins and resolvins:R-HSA-9026286; Biosynthesis of E-series 18(R)-resolvins:R-HSA-9023661; Biosynthesis of E-series 18(S)-resolvins:R-HSA-9018896; Biosynthesis of aspirin-triggered D-series resolvins:R-HSA-9020265; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives:R-HSA-9027604; Biosynthesis of maresins:R-HSA-9018682; Interleukin-18 signaling:R-HSA-9012546; Interleukin-4 and Interleukin-13 signaling:R-HSA-6785807; Neutrophil degranulation:R-HSA-6798695; Synthesis of 5-eicosatetraenoic acids:R-HSA-2142688; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691; Synthesis of Lipoxins (LX):R-HSA-2142700 DE87OZS KG Arachidonic acid metabolism:hsa00590; Fc epsilon RI signaling pathway:hsa04664; Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Serotonergic synapse:hsa04726; Toxoplasmosis:hsa05145 DE87OZS PD 2ABV; 3O8Y; 3V92; 3V98; 3V99 DE87OZS SQ MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNGCNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDPCTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDFHVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECGLFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWEAIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYLTVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCWHLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPYYYLSPDRIPNSVAI DE87OZS TD Primarily distributed in blood, bone marrow and lymphoid tissue. DE87OZS FC This enzyme catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes. DE87OZS KD 33208: Metazoa DE87OZS PL 7711: Chordata DE87OZS CL 40674: Mammalia DE87OZS OD 9443: Primates DE87OZS FM 9604: Hominidae DE87OZS GE 9605: Homo DE87OZS SP 9606: Homo sapiens DE2GB8N ID DE2GB8N DE2GB8N DN UDP-glucuronosyltransferase 1A8 (UGT1A8) DE2GB8N GN UGT1A8 DE2GB8N SN UDP-glucuronosyltransferase family 1 member A8; UDP-glucuronosyltransferase 1-H; UDP-glucuronosyltransferase 1-8; UDPGT 1-8; UGT-1H; UGT1*8; UGT1-08; UGT1.8; UGT1A8; UGT1H DE2GB8N UC UD18_HUMAN DE2GB8N RD Vorinostat DE2GB8N GI 54576 DE2GB8N E1 2: Transferase DE2GB8N E2 2.4: Glycosyltransferases DE2GB8N E3 2.4.1: Hexosyltransferase DE2GB8N EC 2.4.1.17 DE2GB8N RC Glucuronidation:R-HSA-156588 DE2GB8N KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DE2GB8N SQ MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLFFSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEGAQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVTAYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH DE2GB8N TD Primarily distributed in colon, liver, kidney and small intestine. DE2GB8N FC This enzyme is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. DE2GB8N KD 33208: Metazoa DE2GB8N PL 7711: Chordata DE2GB8N CL 40674: Mammalia DE2GB8N OD 9443: Primates DE2GB8N FM 9604: Hominidae DE2GB8N GE 9605: Homo DE2GB8N SP 9606: Homo sapiens DE0JMZ5 ID DE0JMZ5 DE0JMZ5 DN Steroid 21-hydroxylase (CYP21A2) DE0JMZ5 GN CYP21A2 DE0JMZ5 SN Cytochrome P-450c21; Cytochrome P450 21; Cytochrome P450 XXI; Cytochrome P450-C21; Cytochrome P450-C21B; 21-OHase; CYP21; CYP21B DE0JMZ5 UC CP21A_HUMAN DE0JMZ5 RD Hydroxyprogesterone caproate DE0JMZ5 GI 1589 DE0JMZ5 E1 1: Oxidoreductase DE0JMZ5 E2 1.14: Oxygen paired donor oxidoreductase DE0JMZ5 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE0JMZ5 EC 1.14.14.16 DE0JMZ5 RC Defective CYP21A2 causes Adrenal hyperplasia 3 (AH3):R-HSA-5579021; Endogenous sterols:R-HSA-211976; Glucocorticoid biosynthesis:R-HSA-194002; Mineralocorticoid biosynthesis:R-HSA-193993 DE0JMZ5 KG Aldosterone synthesis and secretion:hsa04925; Cortisol synthesis and secretion:hsa04927; Cushing syndrome:hsa04934; Metabolic pathways:hsa01100; Steroid hormone biosynthesis:hsa00140 DE0JMZ5 PD 2GEG; 4Y8W DE0JMZ5 SQ MLLLGLLLLPLLAGARLLWNWWKLRSLHLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIYRLHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSKNYPDLSLGDYSLLWKAHKKLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGDKIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEMQLRQHKESLVAGQWRDMMDYMLQGVAQPSMEEGSGQLLEGHVHMAAVDLLIGGTETTANTLSWAVVFLLHHPEIQQRLQEELDHELGPGASSSRVPYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRPSSISGYDIPEGTVIIPNLQGAHLDETVWERPHEFWPDRFLEPGKNSRALAFGCGARVCLGEPLARLELFVVLTRLLQAFTLLPSGDALPSLQPLPHCSVILKMQPFQVRLQPRGMGAHSPGQNQ DE0JMZ5 TD Primarily distributed in adrenal. DE0JMZ5 FC This enzyme specifically catalyzes the 21-hydroxylation of steroids. DE0JMZ5 KD 33208: Metazoa DE0JMZ5 PL 7711: Chordata DE0JMZ5 CL 40674: Mammalia DE0JMZ5 OD 9443: Primates DE0JMZ5 FM 9604: Hominidae DE0JMZ5 GE 9605: Homo DE0JMZ5 SP 9606: Homo sapiens DERSX5P ID DERSX5P DERSX5P DN Cytochrome P450 2J2 (CYP2J2) DERSX5P GN CYP2J2 DERSX5P SN Cytochrome P450 family 2 subfamily J member 2; Hydroperoxy icosatetraenoate isomerase; Arachidonic acid epoxygenase; Albendazole monooxygenase (hydroxylating); CYP2J2; CYPIIJ2 DERSX5P UC CP2J2_HUMAN DERSX5P RD Riociguat DERSX5P GI 1573 DERSX5P E1 1: Oxidoreductase DERSX5P E2 1.14: Oxygen paired donor oxidoreductase DERSX5P E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DERSX5P EC 1.14.14.24 DERSX5P RC Fatty acids:R-HSA-211935; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET):R-HSA-2142670; Xenobiotics:R-HSA-211981 DERSX5P KG Arachidonic acid metabolism:hsa00590; Inflammatory mediator regulation of TRP channels:hsa04750; Linoleic acid metabolism:hsa00591; Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Serotonergic synapse:hsa04726 DERSX5P SQ MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVDFEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHIFKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDPHFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFLPGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMPYTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDTFNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLSLKFRMGITISPVSHRLCAVPQV DERSX5P TD Primarily distributed in heart muscle, intestine and liver. DERSX5P FC This enzyme is involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system. It catalyzes the epoxidation of double bonds of PUFA and converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE). In endothelial cells, it participates in eicosanoids metabolism by converting hydroperoxide species into hydroxy epoxy metabolites. In combination with 15- lipoxygenase , it metabolizes arachidonic acid and converts hydroperoxyicosatetraenoates (HpETEs) into hydroxy epoxy eicosatrienoates (HEETs). It can also catalyzes the monooxygenation of a various xenobiotics, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone; catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole; and catalyzes the sulfoxidation of fenbedazol. DERSX5P KD 33208: Metazoa DERSX5P PL 7711: Chordata DERSX5P CL 40674: Mammalia DERSX5P OD 9443: Primates DERSX5P FM 9604: Hominidae DERSX5P GE 9605: Homo DERSX5P SP 9606: Homo sapiens DEEH5Y9 ID DEEH5Y9 DEEH5Y9 DN Methionine-tRNA ligase mitochondrial (MARS2) DEEH5Y9 GN MARS2 DEEH5Y9 SN Methionyl-tRNA synthetase 2; Mitochondrial methionyl-tRNA synthetase; Methionine--tRNA ligase mitochondrial; MtMetRS; MARS2 DEEH5Y9 UC SYMM_HUMAN DEEH5Y9 RD Methionine DEEH5Y9 GI 92935 DEEH5Y9 E1 6: Ligase DEEH5Y9 E2 6.1: Carbon-oxygen ligase DEEH5Y9 E3 6.1.1: Aminoacyl tRNA synthetase DEEH5Y9 EC 6.1.1.10 DEEH5Y9 RC Mitochondrial tRNA aminoacylation:R-HSA-379726 DEEH5Y9 KG Aminoacyl-tRNA biosynthesis:hsa00970; Metabolic pathways:hsa01100; Selenocompound metabolism:hsa00450 DEEH5Y9 SQ MLRTSVLRLLGRTGASRLSLLEDFGPRYYSSGSLSAGDDACDVRAYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLFQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVTQQPGPSGDSFPVSLESGHPVSWTKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHHVVLQWLDEELPDLSVSRRSSHLHWGIPVPGDDSQTIYVWLDALVNYLTVIGYPNAEFKSWWPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRCTAKRINPSETYPAFCTTCFPSEPGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRHAPWKLNWESPVDAPWLGTVLHVALECLRVFGTLLQPVTPSLADKLLSRLGVSASERSLGELYFLPRFYGHPCPFEGRRLGPETGLLFPRLDQSRTWLVKAHRT DEEH5Y9 TD Low tissue/organ specificity. DEEH5Y9 FC This enzyme participates in 3 metabolic pathways: methionine metabolism, selenoamino acid metabolism, and aminoacyl-trna biosynthesis. DEEH5Y9 KD 33208: Metazoa DEEH5Y9 PL 7711: Chordata DEEH5Y9 CL 40674: Mammalia DEEH5Y9 OD 9443: Primates DEEH5Y9 FM 9604: Hominidae DEEH5Y9 GE 9605: Homo DEEH5Y9 SP 9606: Homo sapiens DEU2ZBY ID DEU2ZBY DEU2ZBY DN Peptide methionine sulfoxide reductase (MSRA) DEU2ZBY GN MSRA DEU2ZBY SN Peptide-methionine (S)-S-oxide reductase; Protein-methionine-S-oxide reductase; Mitochondrial peptide methionine sulfoxide reductase; Peptide Met(O) reductase; MSRA; PMSR DEU2ZBY UC MSRA_HUMAN DEU2ZBY RD Methionine DEU2ZBY GI 4482 DEU2ZBY E1 1: Oxidoreductase DEU2ZBY E2 1.8: Sulfur donor oxidoreductase DEU2ZBY E3 1.8.4: Disulfide acceptor oxidoreductase DEU2ZBY EC 1.8.4.11 DEU2ZBY RC Protein repair:R-HSA-5676934 DEU2ZBY SQ MLSATRRACQLLLLHSLFPVPRMGNSASNIVSPQEALPGRKEQTPVAAKHHVNGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGYTSNPTYKEVCSEKTGHAEVVRVVYQPEHMSFEELLKVFWENHDPTQGMRQGNDHGTQYRSAIYPTSAKQMEAALSSKENYQKVLSEHGFGPITTDIREGQTFYYAEDYHQQYLSKNPNGYCGLGGTGVSCPVGIKK DEU2ZBY TD Primarily distributed in kidney, cerebellum, liver, heart ventricles, bone marrow and hippocampus. DEU2ZBY FC This enzyme catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. DEU2ZBY KD 33208: Metazoa DEU2ZBY PL 7711: Chordata DEU2ZBY CL 40674: Mammalia DEU2ZBY OD 9443: Primates DEU2ZBY FM 9604: Hominidae DEU2ZBY GE 9605: Homo DEU2ZBY SP 9606: Homo sapiens DEYZEJA ID DEYZEJA DEYZEJA DN Glutathione S-transferase mu-1 (GSTM1) DEYZEJA GN GSTM1 DEYZEJA SN Glutathione S-transferase Mu 1; GST HB subunit 4; GST class-mu 1; GST1; GSTM1; GSTM1-1; GSTM1a-1a; GSTM1b-1b; GTH4 DEYZEJA UC GSTM1_HUMAN DEYZEJA RD Azathioprine DEYZEJA GI 2944 DEYZEJA E1 2: Transferase DEYZEJA E2 2.5: Alkyl/aryl transferase DEYZEJA E3 2.5.1: Alkyl/aryl transferase DEYZEJA EC 2.5.1.18 DEYZEJA RC Glutathione conjugation:R-HSA-156590 DEYZEJA KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DEYZEJA PD 1GTU; 1XW6; 1XWK; 1YJ6; 2F3M DEYZEJA SQ MPMILGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQTMDNHMQLGMICYNPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGNKITFVDFLVYDVLDLHRIFEPKCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPRPVFSKMAVWGNK DEYZEJA TD Primarily distributed in liver and seminal vesicle. DEYZEJA FC This enzyme conjugates reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. DEYZEJA KD 33208: Metazoa DEYZEJA PL 7711: Chordata DEYZEJA CL 40674: Mammalia DEYZEJA OD 9443: Primates DEYZEJA FM 9604: Hominidae DEYZEJA GE 9605: Homo DEYZEJA SP 9606: Homo sapiens DE76G8C ID DE76G8C DE76G8C DN S-adenosylmethionine synthase 2 (MAT2A) DE76G8C GN MAT2A DE76G8C SN Methionine adenosyltransferase 2; AdoMet synthase 2; Methionine adenosyltransferase II; S-adenosylmethionine synthase isoform type-2; AMS2; MAT 2; MAT-II; MAT2A; MATA2 DE76G8C UC METK2_HUMAN DE76G8C RD Methionine DE76G8C GI 4144 DE76G8C E1 2: Transferase DE76G8C E2 2.5: Alkyl/aryl transferase DE76G8C E3 2.5.1: Alkyl/aryl transferase DE76G8C EC 2.5.1.6 DE76G8C RC Methylation:R-HSA-156581 DE76G8C KG Biosynthesis of amino acids:hsa01230; Cysteine and methionine metabolism:hsa00270; Metabolic pathways:hsa01100 DE76G8C PD 4KTV; 4NDN; 5A19; 5A1G; 5A1I; 5UGH; 6FAJ; 6FBN; 6FBO DE76G8C SQ MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY DE76G8C TD Primarily distributed in pancreas and kidney. DE76G8C FC This enzyme catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. DE76G8C KD 33208: Metazoa DE76G8C PL 7711: Chordata DE76G8C CL 40674: Mammalia DE76G8C OD 9443: Primates DE76G8C FM 9604: Hominidae DE76G8C GE 9605: Homo DE76G8C SP 9606: Homo sapiens DEE5M8O ID DEE5M8O DEE5M8O DN Alcohol dehydrogenase class-I alpha (ADH1A) DEE5M8O GN ADH1A DEE5M8O SN Alcohol dehydrogenase 1A; Alcohol dehydrogenase subunit alpha; ADH1; ADH1A DEE5M8O UC ADH1A_HUMAN DEE5M8O RD Silodosin DEE5M8O GI 124 DEE5M8O E1 1: Oxidoreductase DEE5M8O E2 1.1: CH-OH donor oxidoreductase DEE5M8O E3 1.1.1: NAD/NADP oxidoreductase DEE5M8O EC 1.1.1.1 DEE5M8O RC Abacavir metabolism:R-HSA-2161541; Ethanol oxidation:R-HSA-71384; RA biosynthesis pathway:R-HSA-5365859 DEE5M8O KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Fatty acid degradation:hsa00071; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Tyrosine metabolism:hsa00350 DEE5M8O PD 1HSO; 1U3T DEE5M8O SQ MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTILMF DEE5M8O TD Primarily distributed in liver. DEE5M8O FC This enzyme metabolizes a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. DEE5M8O KD 33208: Metazoa DEE5M8O PL 7711: Chordata DEE5M8O CL 40674: Mammalia DEE5M8O OD 9443: Primates DEE5M8O FM 9604: Hominidae DEE5M8O GE 9605: Homo DEE5M8O SP 9606: Homo sapiens DEIASEZ ID DEIASEZ DEIASEZ DN Dimethylaniline oxidase 2 (FMO2) DEIASEZ GN FMO2 DEIASEZ SN Dimethylaniline monooxygenase [N-oxide-forming] 2; FMO 1B1; FMO 2; Pulmonary flavin-containing monooxygenase 2 DEIASEZ UC FMO2_HUMAN DEIASEZ RD Trifluoperazine DEIASEZ GI 2327 DEIASEZ E1 1: Oxidoreductase DEIASEZ E2 1.14: Oxygen paired donor oxidoreductase DEIASEZ E3 1.14.13: NADH/NADPH donor oxidoreductase DEIASEZ EC 1.14.13.8 DEIASEZ RC FMO oxidises nucleophiles:R-HSA-217271 DEIASEZ KG Drug metabolism - cytochrome P450:hsa00982 DEIASEZ SQ MAKKVAVIGAGVSGLISLKCCVDEGLEPTCFERTEDIGGVWRFKENVEDGRASIYQSVVTNTSKEMSCFSDFPMPEDFPNFLHNSKLLEYFRIFAKKFDLLKYIQFQTTVLSVRKCPDFSSSGQWKVVTQSNGKEQSAVFDAVMVCSGHHILPHIPLKSFPGMERFKGQYFHSRQYKHPDGFEGKRILVIGMGNSGSDIAVELSKNAAQVFISTRHGTWVMSRISEDGYPWDSVFHTRFRSMLRNVLPRTAVKWMIEQQMNRWFNHENYGLEPQNKYIMKEPVLNDDVPSRLLCGAIKVKSTVKELTETSAIFEDGTVEENIDVIIFATGYSFSFPFLEDSLVKVENNMVSLYKYIFPAHLDKSTLACIGLIQPLGSIFPTAELQARWVTRVFKGLCSLPSERTMMMDIIKRNEKRIDLFGESQSQTLQTNYVDYLDELALEIGAKPDFCSLLFKDPKLAVRLYFGPCNSYQYRLVGPGQWEGARNAIFTQKQRILKPLKTRALKDSSNFSVSFLLKILGLLAVVVAFFCQLQWS DEIASEZ TD Primarily distributed in adipose tissue, esophagus and lung. DEIASEZ FC This enzyme catalyzes the N-oxidation of certain primary alkylamines to their oximes via an N-hydroxylamine intermediate. And it can catalyze the S-oxidation of methimazole. DEIASEZ KD 33208: Metazoa DEIASEZ PL 7711: Chordata DEIASEZ CL 40674: Mammalia DEIASEZ OD 9443: Primates DEIASEZ FM 9604: Hominidae DEIASEZ GE 9605: Homo DEIASEZ SP 9606: Homo sapiens DE017IC ID DE017IC DE017IC DN Alcohol dehydrogenase class-V (ADH6) DE017IC GN ADH6 DE017IC SN Alcohol dehydrogenase 6; ADH6; ADH-5; Alcohol dehydrogenase 6 (class V) DE017IC UC ADH6_HUMAN DE017IC RD Abacavir DE017IC GI 130 DE017IC E1 1: Oxidoreductase DE017IC E2 1.1: CH-OH donor oxidoreductase DE017IC E3 1.1.1: NAD/NADP oxidoreductase DE017IC EC 1.1.1.1 DE017IC RC Ethanol oxidation:R-HSA-71384 DE017IC KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Fatty acid degradation:hsa00071; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Tyrosine metabolism:hsa00350 DE017IC SQ MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSKTQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKW DE017IC TD Primarily distributed in liver and stomach. DE017IC FC This enzyme metabolizes a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. DE017IC KD 33208: Metazoa DE017IC PL 7711: Chordata DE017IC CL 40674: Mammalia DE017IC OD 9443: Primates DE017IC FM 9604: Hominidae DE017IC GE 9605: Homo DE017IC SP 9606: Homo sapiens DEZO4N3 ID DEZO4N3 DEZO4N3 DN UDP-glucuronosyltransferase 1A7 (UGT1A7) DEZO4N3 GN UGT1A7 DEZO4N3 SN UDP-glucuronosyltransferase family 1 member A7; UDP-glucuronosyltransferase 1-G; UDP-glucuronosyltransferase 1-7; UDPGT 1-7; UGT-1G; UGT1*7; UGT1-07; UGT1.7; UGT1A7; UGT1G DEZO4N3 UC UD17_HUMAN DEZO4N3 RD Vorinostat DEZO4N3 GI 54577 DEZO4N3 E1 2: Transferase DEZO4N3 E2 2.4: Glycosyltransferases DEZO4N3 E3 2.4.1: Hexosyltransferase DEZO4N3 EC 2.4.1.17 DEZO4N3 RC Glucuronidation:R-HSA-156588 DEZO4N3 KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEZO4N3 SQ MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMPEVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLFFSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEGAQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVTAYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH DEZO4N3 TD Primarily distributed in liver, gastric tissue, esophagus, lymphoid tissue and tongue. DEZO4N3 FC This enzyme is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. DEZO4N3 KD 33208: Metazoa DEZO4N3 PL 7711: Chordata DEZO4N3 CL 40674: Mammalia DEZO4N3 OD 9443: Primates DEZO4N3 FM 9604: Hominidae DEZO4N3 GE 9605: Homo DEZO4N3 SP 9606: Homo sapiens DEHMPZR ID DEHMPZR DEHMPZR DN Glutathione S-transferase omega-2 (GSTO2) DEHMPZR GN GSTO2 DEHMPZR SN Glutathione S-transferase omega 2-2; GSTO 2-2; GSTO-2; GSTO2 DEHMPZR UC GSTO2_HUMAN DEHMPZR RD ANW-43980 DEHMPZR GI 119391 DEHMPZR E1 2: Transferase DEHMPZR E2 2.5: Alkyl/aryl transferase DEHMPZR E3 2.5.1: Alkyl/aryl transferase DEHMPZR EC 2.5.1.18 DEHMPZR RC Glutathione conjugation:R-HSA-156590; Vitamin C (ascorbate) metabolism:R-HSA-196836 DEHMPZR KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DEHMPZR PD 3Q18; 3Q19; 3QAG DEHMPZR SQ MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELFCKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDFGLC DEHMPZR TD Primarily distributed in testis. Also expressed in liver, kidney, skeletal muscle and prostate. DEHMPZR FC This enzyme exhibits glutathione-dependent thiol transferase activity. It has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. It participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). DEHMPZR KD 33208: Metazoa DEHMPZR PL 7711: Chordata DEHMPZR CL 40674: Mammalia DEHMPZR OD 9443: Primates DEHMPZR FM 9604: Hominidae DEHMPZR GE 9605: Homo DEHMPZR SP 9606: Homo sapiens DEMEPVJ ID DEMEPVJ DEMEPVJ DN Acyl-CoA thioesterase 2 (ACOT2) DEMEPVJ GN ACOT2 DEMEPVJ SN Acyl-coenzyme A thioester hydrolase 2a; Acyl-coenzyme A thioesterase 2, mitochondrial; CTE-Ia; Long-chain acyl-CoA thioesterase 2; ACOT2; PTE2; PTE2A; ZAP128 DEMEPVJ UC ACOT2_HUMAN DEMEPVJ RD Ibuprofen DEMEPVJ GI 10965 DEMEPVJ E1 3: Hydrolases DEMEPVJ E2 3.1: Ester bond hydrolase DEMEPVJ E3 3.1.2: Thioester hydrolase DEMEPVJ EC 3.1.2.2 DEMEPVJ RC Mitochondrial Fatty Acid Beta-Oxidation:R-HSA-77289; Peroxisomal protein import:R-HSA-9033241 DEMEPVJ KG Biosynthesis of unsaturated fatty acids:hsa01040; Fatty acid elongation:hsa00062; Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913 DEMEPVJ PD 3HLK DEMEPVJ SQ MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVPARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSKV DEMEPVJ TD Primarily distributed in heart, liver, muscle andkidney. DEMEPVJ FC This enzyme catalyzes the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. It displays higher activity toward long chain acyl CoAs (C14-C20). And it is involved in enhancing the hepatic fatty acid oxidation in mitochondria. DEMEPVJ KD 33208: Metazoa DEMEPVJ PL 7711: Chordata DEMEPVJ CL 40674: Mammalia DEMEPVJ OD 9443: Primates DEMEPVJ FM 9604: Hominidae DEMEPVJ GE 9605: Homo DEMEPVJ SP 9606: Homo sapiens DEKF1OH ID DEKF1OH DEKF1OH DN Methionine adenosyltransferase II beta (MAT2B) DEKF1OH GN MAT2B DEKF1OH SN Methionine adenosyltransferase 2 subunit beta; Putative dTDP-4-keto-6-deoxy-D-glucose 4-reductase; MAT II beta; MAT2B; MSTP045; Nbla02999; TGR; UNQ2435/PRO4995 DEKF1OH UC MAT2B_HUMAN DEKF1OH RD Methionine DEKF1OH GI 27430 DEKF1OH E1 2: Transferase DEKF1OH E2 2.5: Alkyl/aryl transferase DEKF1OH E3 2.5.1: Alkyl/aryl transferase DEKF1OH EC 2.5.1.6 DEKF1OH RC Methylation:R-HSA-156581; Ub-specific processing proteases:R-HSA-5689880 DEKF1OH KG Biosynthesis of amino acids:hsa01230; Cysteine and methionine metabolism:hsa00270; Metabolic pathways:hsa01100 DEKF1OH PD 2YDX; 2YDY; 4KTT; 4KTV; 4NDN DEKF1OH SQ MVGREKELSIHFVPGSCRLVEEEVNIPNRRVLVTGATGLLGRAVHKEFQQNNWHAVGCGFRRARPKFEQVNLLDSNAVHHIIHDFQPHVIVHCAAERRPDVVENQPDAASQLNVDASGNLAKEAAAVGAFLIYISSDYVFDGTNPPYREEDIPAPLNLYGKTKLDGEKAVLENNLGAAVLRIPILYGEVEKLEESAVTVMFDKVQFSNKSANMDHWQQRFPTHVKDVATVCRQLAEKRMLDPSIKGTFHWSGNEQMTKYEMACAIADAFNLPSSHLRPITDSPVLGAQRPRNAQLDCSKLETLGIGQRTPFRIGIKESLWPFLIDKRWRQTVFH DEKF1OH TD Low tissue/organ specificity. DEKF1OH FC This enzyme is a regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. DEKF1OH KD 33208: Metazoa DEKF1OH PL 7711: Chordata DEKF1OH CL 40674: Mammalia DEKF1OH OD 9443: Primates DEKF1OH FM 9604: Hominidae DEKF1OH GE 9605: Homo DEKF1OH SP 9606: Homo sapiens DEQ6NC9 ID DEQ6NC9 DEQ6NC9 DN S-adenosylmethionine synthase 1 (MAT1A) DEQ6NC9 GN MAT1A DEQ6NC9 SN Methionine adenosyltransferase 1; AdoMet synthase 1; Methionine adenosyltransferase I/III; S-adenosylmethionine synthase isoform type-1; AMS1; MAT 1; MAT-I/III; MAT1A; MATA1 DEQ6NC9 UC METK1_HUMAN DEQ6NC9 RD Methionine DEQ6NC9 GI 4143 DEQ6NC9 E1 2: Transferase DEQ6NC9 E2 2.5: Alkyl/aryl transferase DEQ6NC9 E3 2.5.1: Alkyl/aryl transferase DEQ6NC9 EC 2.5.1.6 DEQ6NC9 RC Defective MAT1A causes Methionine adenosyltransferase deficiency (MATD):R-HSA-5579024; Metabolism of ingested SeMet, Sec, MeSec into H2Se:R-HSA-2408508; Methylation:R-HSA-156581; Sulfur amino acid metabolism:R-HSA-1614635 DEQ6NC9 KG Biosynthesis of amino acids:hsa01230; Cysteine and methionine metabolism:hsa00270; Metabolic pathways:hsa01100 DEQ6NC9 PD 2OBV DEQ6NC9 SQ MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDSKTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDTVYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVIVRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF DEQ6NC9 TD Primarily distributed in liver. DEQ6NC9 FC This enzyme catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. DEQ6NC9 KD 33208: Metazoa DEQ6NC9 PL 7711: Chordata DEQ6NC9 CL 40674: Mammalia DEQ6NC9 OD 9443: Primates DEQ6NC9 FM 9604: Hominidae DEQ6NC9 GE 9605: Homo DEQ6NC9 SP 9606: Homo sapiens DEZMAHX ID DEZMAHX DEZMAHX DN Gastric alcohol dehydrogenase (ADH7) DEZMAHX GN ADH7 DEZMAHX SN Omega-hydroxydecanoate dehydrogenase ADH7; Retinol dehydrogenase; Alcohol dehydrogenase class 4 mu/sigma chain; Alcohol dehydrogenase class IV mu/sigma chain; All-trans-retinol dehydrogenase [NAD(+)] ADH7; ADH7 DEZMAHX UC ADH7_HUMAN DEZMAHX RD Ethanol DEZMAHX GI 131 DEZMAHX E1 1: Oxidoreductase DEZMAHX E2 1.1: CH-OH donor oxidoreductase DEZMAHX E3 1.1.1: NAD/NADP oxidoreductase DEZMAHX EC 1.1.1.105 DEZMAHX RC Ethanol oxidation:R-HSA-71384 DEZMAHX KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Fatty acid degradation:hsa00071; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Tyrosine metabolism:hsa00350 DEZMAHX PD 1AGN; 1D1S; 1D1T DEZMAHX SQ MFAEIQIQDKDRMGTAGKVIKCKAAVLWEQKQPFSIEEIEVAPPKTKEVRIKILATGICRTDDHVIKGTMVSKFPVIVGHEATGIVESIGEGVTTVKPGDKVIPLFLPQCRECNACRNPDGNLCIRSDITGRGVLADGTTRFTCKGKPVHHFMNTSTFTEYTVVDESSVAKIDDAAPPEKVCLIGCGFSTGYGAAVKTGKVKPGSTCVVFGLGGVGLSVIMGCKSAGASRIIGIDLNKDKFEKAMAVGATECISPKDSTKPISEVLSEMTGNNVGYTFEVIGHLETMIDALASCHMNYGTSVVVGVPPSAKMLTYDPMLLFTGRTWKGCVFGGLKSRDDVPKLVTEFLAKKFDLDQLITHVLPFKKISEGFELLNSGQSIRTVLTF DEZMAHX TD Primarily distributed in stomach, esophagus, lymphoid tissue and tongue. DEZMAHX FC This enzyme catalyzes the NAD-dependent oxidation of all-trans-retinol, alcohol, and omega-hydroxy fatty acids and their derivatives. It oxidizes preferentially all trans-retinol, all-trans-4-hydroxyretinol, 9-cis- retinol, 2-hexenol, and long chain omega-hydroxy fatty acids such as juniperic acid. In vitro it can also catalyzes the NADH-dependent reduction of all-trans- retinal and aldehydes and their derivatives. It reduces preferentially all trans- retinal, all-trans-4-oxoretinal and hexanal. DEZMAHX KD 33208: Metazoa DEZMAHX PL 7711: Chordata DEZMAHX CL 40674: Mammalia DEZMAHX OD 9443: Primates DEZMAHX FM 9604: Hominidae DEZMAHX GE 9605: Homo DEZMAHX SP 9606: Homo sapiens DECWT2V ID DECWT2V DECWT2V DN Folylpolyglutamate synthase (FPGS) DECWT2V GN FPGS DECWT2V SN Folylpoly-gamma-glutamate synthetase; Tetrahydrofolate synthase; Tetrahydrofolylpolyglutamate synthase; Mitochondrial Folylpolyglutamate synthase; FPGS DECWT2V UC FOLC_HUMAN DECWT2V RD Pralatrexate DECWT2V GI 2356 DECWT2V E1 6: Ligase DECWT2V E2 6.3: Carbon-nitrogen ligase DECWT2V E3 6.3.2: Peptide synthase DECWT2V EC 6.3.2.17 DECWT2V RC Metabolism of folate and pterines:R-HSA-196757 DECWT2V KG Antifolate resistance:hsa01523; Folate biosynthesis:hsa00790; Metabolic pathways:hsa01100 DECWT2V SQ MSRARSHLRAALFLAAASARGITTQVAARRGLSAWPVPQEPSMEYQDAVRMLNTLQTNAGYLEQVKRQRGDPQTQLEAMELYLARSGLQVEDLDRLNIIHVTGTKGKGSTCAFTECILRSYGLKTGFFSSPHLVQVRERIRINGQPISPELFTKYFWRLYHRLEETKDGSCVSMPPYFRFLTLMAFHVFLQEKVDLAVVEVGIGGAYDCTNIIRKPVVCGVSSLGIDHTSLLGDTVEKIAWQKGGIFKQGVPAFTVLQPEGPLAVLRDRAQQISCPLYLCPMLEALEEGGPPLTLGLEGEHQRSNAALALQLAHCWLQRQDRHGAGEPKASRPGLLWQLPLAPVFQPTSHMRLGLRNTEWPGRTQVLRRGPLTWYLDGAHTASSAQACVRWFRQALQGRERPSGGPEVRVLLFNATGDRDPAALLKLLQPCQFDYAVFCPNLTEVSSTGNADQQNFTVTLDQVLLRCLEHQQHWNHLDEEQASPDLWSAPSPEPGGSASLLLAPHPPHTCSASSLVFSCISHALQWISQGRDPIFQPPSPPKGLLTHPVAHSGASILREAAAIHVLVTGSLHLVGGVLKLLEPALSQ DECWT2V TD Low tissue/organ specificity. DECWT2V FC This enzyme catalyzes conversion of folates to polyglutamate derivatives and it can metabolizes methotrexate (MTX) to polyglutamates. DECWT2V KD 33208: Metazoa DECWT2V PL 7711: Chordata DECWT2V CL 40674: Mammalia DECWT2V OD 9443: Primates DECWT2V FM 9604: Hominidae DECWT2V GE 9605: Homo DECWT2V SP 9606: Homo sapiens DEAMVR3 ID DEAMVR3 DEAMVR3 DN Dehydropeptidase-I (DPEP1) DEAMVR3 GN DPEP1 DEAMVR3 SN Microsomal dipeptidase; RDP; Renal dipeptidase; Dipeptidase 1; MDP; hRDP; DPEP1 DEAMVR3 UC DPEP1_HUMAN DEAMVR3 RD Doripenem DEAMVR3 GI 1800 DEAMVR3 E1 3: Hydrolases DEAMVR3 E2 3.4: Peptidase DEAMVR3 E3 3.4.13: Dipeptidase DEAMVR3 EC 3.4.13.19 DEAMVR3 RC Aflatoxin activation and detoxification:R-HSA-5423646; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DEAMVR3 PD 1ITQ; 1ITU DEAMVR3 SQ MWSGWWLWPLVAVCTADFFRDEAERIMRDSPVIDGHNDLPWQLLDMFNNRLQDERANLTTLAGTHTNIPKLRAGFVGGQFWSVYTPCDTQNKDAVRRTLEQMDVVHRMCRMYPETFLYVTSSAGIRQAFREGKVASLIGVEGGHSIDSSLGVLRALYQLGMRYLTLTHSCNTPWADNWLVDTGDSEPQSQGLSPFGQRVVKELNRLGVLIDLAHVSVATMKATLQLSRAPVIFSHSSAYSVCASRRNVPDDVLRLVKQTDSLVMVNFYNNYISCTNKANLSQVADHLDHIKEVAGARAVGFGGDFDGVPRVPEGLEDVSKYPDLIAELLRRNWTEAEVKGALADNLLRVFEAVEQASNLTQAPEEEPIPLDQLGGSCRTHYGYSSGASSLHRHWGLLLASLAPLVLCLSLL DEAMVR3 TD Primarily distributed in intestine, kidney and pancreas. DEAMVR3 FC This enzyme hydrolyzes a wide range of dipeptides. It implicated in the renal metabolism of glutathione and its conjugates. DEAMVR3 KD 33208: Metazoa DEAMVR3 PL 7711: Chordata DEAMVR3 CL 40674: Mammalia DEAMVR3 OD 9443: Primates DEAMVR3 FM 9604: Hominidae DEAMVR3 GE 9605: Homo DEAMVR3 SP 9606: Homo sapiens DEX2KIA ID DEX2KIA DEX2KIA DN Steroid 17-alpha-monooxygenase (CYP17A1) DEX2KIA GN CYP17A1 DEX2KIA SN Steroid 17-alpha-hydroxylase/17,20 lyase; Cytochrome P450 17A1; 17-alpha-hydroxyprogesterone aldolase; Cytochrome P450-C17; Cytochrome P450c17; CYP17; CYP17A1; CYPXVII; S17AH DEX2KIA UC CP17A_HUMAN DEX2KIA RD Androstanolone DEX2KIA GI 1586 DEX2KIA E1 1: Oxidoreductase DEX2KIA E2 1.14: Oxygen paired donor oxidoreductase DEX2KIA E3 1.14.99: Oxygen paired donor oxidoreductase DEX2KIA EC 1.14.99.9 DEX2KIA RC Androgen biosynthesis:R-HSA-193048; Defective CYP17A1 causes Adrenal hyperplasia 5 (AH5):R-HSA-5579028; Glucocorticoid biosynthesis:R-HSA-194002 DEX2KIA KG Cortisol synthesis and secretion:hsa04927; Cushing syndrome:hsa04934; Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Prolactin signaling pathway:hsa04917; Steroid hormone biosynthesis:hsa00140 DEX2KIA PD 3SWZ; 4NKV; 4NKW; 4NKX; 4NKY; 4NKZ; 5IRQ; 5IRV; 5UYS DEX2KIA SQ MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVISLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVVFLIDSFKVKIKVRQAWREAQAEGST DEX2KIA TD Primarily distributed in adrenal. DEX2KIA FC This enzyme is involved in corticoid and androgen biosynthesis. It catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol. Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione. It has 16-alpha hydroxylase activity. It catalyzes 16-alpha hydroxylation of 17-alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA and also 16-alpha hydroxylates androgens, relevant for estriol synthesis. DEX2KIA KD 33208: Metazoa DEX2KIA PL 7711: Chordata DEX2KIA CL 40674: Mammalia DEX2KIA OD 9443: Primates DEX2KIA FM 9604: Hominidae DEX2KIA GE 9605: Homo DEX2KIA SP 9606: Homo sapiens DESZ5G9 ID DESZ5G9 DESZ5G9 DN Cellular glutathione peroxidase (GPX1) DESZ5G9 GN GPX1 DESZ5G9 SN Glutathione peroxidase 1; GPX1; GPx-1; GSHPx-1; GPXD; GSHPX1 DESZ5G9 UC GPX1_HUMAN DESZ5G9 RD Hydrogen peroxide DESZ5G9 GI 2876 DESZ5G9 E1 1: Oxidoreductase DESZ5G9 E2 1.11: Peroxidase DESZ5G9 E3 1.11.1: Peroxidase DESZ5G9 EC 1.11.1.9 DESZ5G9 RC Detoxification of Reactive Oxygen Species:R-HSA-3299685; Purine catabolism:R-HSA-74259; Synthesis of 12-eicosatetraenoic acid derivatives:R-HSA-2142712; Synthesis of 15-eicosatetraenoic acid derivatives:R-HSA-2142770; Synthesis of 5-eicosatetraenoic acids:R-HSA-2142688 DESZ5G9 KG Amyotrophic lateral sclerosis (ALS):hsa05014; Arachidonic acid metabolism:hsa00590; Glutathione metabolism:hsa00480; Huntington's disease:hsa05016; Metabolic pathways:hsa01100; Thyroid hormone synthesis:hsa04918 DESZ5G9 PD 2F8A DESZ5G9 SQ MCAARLAAAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA DESZ5G9 TD Primarily distributed in adipose, bone and testicle. DESZ5G9 FC This enzyme protects the hemoglobin in erythrocytes from oxidative breakdown. DESZ5G9 KD 33208: Metazoa DESZ5G9 PL 7711: Chordata DESZ5G9 CL 40674: Mammalia DESZ5G9 OD 9443: Primates DESZ5G9 FM 9604: Hominidae DESZ5G9 GE 9605: Homo DESZ5G9 SP 9606: Homo sapiens DEPE0RD ID DEPE0RD DEPE0RD DN Steroid 11-beta-hydroxylase (CYP11B1) DEPE0RD GN CYP11B1 DEPE0RD SN Steroid 11-beta-hydroxylase CYP11B1; Cytochrome P-450c11; Mitochondrial cytochrome P450 11B1; Cytochrome P450C11; CYP11B1; CYPXIB1; S11BH DEPE0RD UC C11B1_HUMAN DEPE0RD RD Hydrocortisone DEPE0RD GI 1584 DEPE0RD E1 1: Oxidoreductase DEPE0RD E2 1.14: Oxygen paired donor oxidoreductase DEPE0RD E3 1.14.15: Iron-sulfur protein donor oxidoreductase DEPE0RD EC 1.14.15.4 DEPE0RD RC Defective CYP11B1 causes Adrenal hyperplasia 4 (AH4):R-HSA-5579017; Endogenous sterols:R-HSA-211976; Glucocorticoid biosynthesis:R-HSA-194002 DEPE0RD KG Cortisol synthesis and secretion:hsa04927; Cushing syndrome:hsa04934; Metabolic pathways:hsa01100; Steroid hormone biosynthesis:hsa00140 DEPE0RD PD 6M7X DEPE0RD SQ MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQGYEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELSPDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVASSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRPERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQEDIKMVYSFILRPSMFPLLTFRAIN DEPE0RD TD Primarily distributed in adrenal. DEPE0RD FC This enzyme is involved in the biosynthesis of adrenal corticoids. It catalyzes the hydroxylation of carbon hydrogen bond at 11-beta position of 11-deoxycortisol and 11- deoxycorticosterone/21-hydroxyprogesterone yielding cortisol or corticosterone, respectively. DEPE0RD KD 33208: Metazoa DEPE0RD PL 7711: Chordata DEPE0RD CL 40674: Mammalia DEPE0RD OD 9443: Primates DEPE0RD FM 9604: Hominidae DEPE0RD GE 9605: Homo DEPE0RD SP 9606: Homo sapiens DEMWO83 ID DEMWO83 DEMWO83 DN Putrescine acetyltransferase (SSAT1) DEMWO83 GN SAT1 DEMWO83 SN Diamine acetyltransferase 1; Polyamine N-acetyltransferase 1; Spermidine/spermine N(1)-acetyltransferase 1; SAT1; SSAT; SSAT-1; SSAT1 DEMWO83 UC SAT1_HUMAN DEMWO83 RD CCG-205124 DEMWO83 GI 6303 DEMWO83 E1 2: Transferase DEMWO83 E2 2.3: Acyltransferase DEMWO83 E3 2.3.1: Acyltransferase DEMWO83 EC 2.3.1.57 DEMWO83 RC Interconversion of polyamines:R-HSA-351200 DEMWO83 KG Arginine and proline metabolism:hsa00330; Ferroptosis:hsa04216; Metabolic pathways:hsa01100 DEMWO83 PD 2B3U; 2B3V; 2B4B; 2B4D; 2B5G; 2F5I; 2FXF; 2G3T; 2JEV DEMWO83 SQ MAKFVIRPATAADCSDILRLIKELAKYEYMEEQVILTEKDLLEDGFGEHPFYHCLVAEVPKEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMRCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMATEE DEMWO83 TD Low tissue/organ specificity. DEMWO83 FC This enzyme catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)- acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. DEMWO83 KD 33208: Metazoa DEMWO83 PL 7711: Chordata DEMWO83 CL 40674: Mammalia DEMWO83 OD 9443: Primates DEMWO83 FM 9604: Hominidae DEMWO83 GE 9605: Homo DEMWO83 SP 9606: Homo sapiens DEFK2EH ID DEFK2EH DEFK2EH DN HMG-CoA reductase (HMGCR) DEFK2EH GN HMGCR DEFK2EH SN Hydroxy-methylglutaryl coenzyme A reductase; 3-hydroxy-3-methylglutaryl-coenzyme A reductase; HMGCR DEFK2EH UC HMDH_HUMAN DEFK2EH RD CoQ-10 DEFK2EH GI 3156 DEFK2EH E1 1: Oxidoreductase DEFK2EH E2 1.1: CH-OH donor oxidoreductase DEFK2EH E3 1.1.1: NAD/NADP oxidoreductase DEFK2EH EC 1.1.1.34 DEFK2EH RC Activation of gene expression by SREBF (SREBP) [P04035-1]:R-HSA-2426168; Cholesterol biosynthesis:R-HSA-191273; PPARA activates gene expression [P04035-1]:R-HSA-1989781 DEFK2EH KG AMPK signaling pathway:hsa04152; Bile secretion:hsa04976; Metabolic pathways:hsa01100; Terpenoid backbone biosynthesis:hsa00900 DEFK2EH PD 1DQA; 1HW8; 1HW9; 1HWI; 1HWJ; 1HWK; 1HWL; 2Q1L; 2Q6B DEFK2EH SQ MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVTQKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNSSLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA DEFK2EH TD Low tissue/organ specificity. DEFK2EH FC This enzyme is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins. DEFK2EH KD 33208: Metazoa DEFK2EH PL 7711: Chordata DEFK2EH CL 40674: Mammalia DEFK2EH OD 9443: Primates DEFK2EH FM 9604: Hominidae DEFK2EH GE 9605: Homo DEFK2EH SP 9606: Homo sapiens DEVXTP5 ID DEVXTP5 DEVXTP5 DN Hypoxanthine phosphoribosyltransferase (HPRT1) DEVXTP5 GN HPRT1 DEVXTP5 SN Hypoxanthine-guanine phosphoribosyltransferase; HGPRT; HGPRTase; HPRT; HPRT1 DEVXTP5 UC HPRT_HUMAN DEVXTP5 RD BW-5071 DEVXTP5 GI 3251 DEVXTP5 E1 2: Transferase DEVXTP5 E2 2.4: Glycosyltransferases DEVXTP5 E3 2.4.2: Pentosyltransferase DEVXTP5 EC 2.4.2.8 DEVXTP5 RC Purine salvage:R-HSA-74217 DEVXTP5 KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Purine metabolism:hsa00230 DEVXTP5 PD 1HMP; 1Z7G; 2VFA; 3GEP; 3GGC; 3GGJ; 4IJQ; 4KN6; 4RAB DEVXTP5 SQ MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA DEVXTP5 TD Low tissue/organ specificity. DEVXTP5 FC This enzyme converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. It transfers the 5-phosphoribosyl group from 5- phosphoribosylpyrophosphate onto the purine. DEVXTP5 KD 33208: Metazoa DEVXTP5 PL 7711: Chordata DEVXTP5 CL 40674: Mammalia DEVXTP5 OD 9443: Primates DEVXTP5 FM 9604: Hominidae DEVXTP5 GE 9605: Homo DEVXTP5 SP 9606: Homo sapiens DEFI12S ID DEFI12S DEFI12S DN Vitamin D(3) 24-hydroxylase (CYP24A1) DEFI12S GN CYP24A1 DEFI12S SN Cytochrome P450 24A1; Mitochondrial 1,25-dihydroxyvitamin D(3) 24-hydroxylase; Cytochrome P450-CC24; 24-OHase; CYP24; CYP24A1 DEFI12S UC CP24A_HUMAN DEFI12S RD Calcifediol DEFI12S GI 1591 DEFI12S E1 1: Oxidoreductase DEFI12S E2 1.14: Oxygen paired donor oxidoreductase DEFI12S E3 1.14.15: Iron-sulfur protein donor oxidoreductase DEFI12S EC 1.14.15.16 DEFI12S RC Defective CYP24A1 causes Hypercalcemia, infantile (HCAI):R-HSA-5579010; Vitamin D (calciferol) metabolism:R-HSA-196791; Vitamins:R-HSA-211916 DEFI12S KG Metabolic pathways:hsa01100; MicroRNAs in cancer:hsa05206; Parathyroid hormone synthesis, secretion and action:hsa04928; Steroid biosynthesis:hsa00100 DEFI12S SQ MSSPISKSRSLAAFLQQLRSPRQPPRLVTSTAYTSPQPREVPVCPLTAGGETQNAAALPGPTSWPLLGSLLQILWKGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGTVLMLNTQVLGSSEDNFEDSSQFRPERWLQEKEKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIVRKYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR DEFI12S TD Primarily distributed in kidney, lymphoid tissue and urinary bladder. DEFI12S FC This enzyme plays a key role in vitamin D catabolism and calcium homeostasis. Via C24- and C23-oxidation pathways, it catalyzes the inactivation of both the vitamin D precursor calcidiol (25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D(3)). With initial hydroxylation at C-24 (via C24-oxidation pathway), it performs a sequential 6-step oxidation of calcitriol leading to the formation of the biliary metabolite calcitroic acid. With initial hydroxylation at C-23 (via C23-oxidation pathway), it catalyzes sequential oxidation of calcidiol leading to the formation of 25(OH)D3-26,23-lactone as end product. It preferentially hydroxylates at C-25 other vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S- hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol. DEFI12S KD 33208: Metazoa DEFI12S PL 7711: Chordata DEFI12S CL 40674: Mammalia DEFI12S OD 9443: Primates DEFI12S FM 9604: Hominidae DEFI12S GE 9605: Homo DEFI12S SP 9606: Homo sapiens DEOY5ZM ID DEOY5ZM DEOY5ZM DN Aldo-keto reductase 1C2 (AKR1C2) DEOY5ZM GN AKR1C2 DEOY5ZM SN Aldo-keto reductase family 1 member C2; Chlordecone reductase homolog HAKRD; DD-2; DD/BABP; DD2; DDH2; Dihydrodiol dehydrogenase 2; Dihydrodiol dehydrogenase/bile acid-binding protein; Type III 3-alpha-hydroxysteroid dehydrogenase; 3-alpha-HSD3; AKR1C2 DEOY5ZM UC AK1C2_HUMAN DEOY5ZM RD Fenofibric acid DEOY5ZM GI 1646 DEOY5ZM E1 1: Oxidoreductase DEOY5ZM E2 1.1: CH-OH donor oxidoreductase DEOY5ZM E3 1.1.1: NAD/NADP oxidoreductase DEOY5ZM EC 1.1.1.357 DEOY5ZM RC Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DEOY5ZM KG Chemical carcinogenesis:hsa05204; Steroid hormone biosynthesis:hsa00140 DEOY5ZM PD 1XJB; 2HDJ; 2IPJ; 4JQ1; 4JQ2; 4JQ3; 4JQ4; 4JQA; 4JTQ DEOY5ZM SQ MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY DEOY5ZM TD Primarily distributed in breast, liver and tongue. DEOY5ZM FC This enzyme works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids, and it catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha- androstane-3-alpha,17-beta-diol (3-alpha-diol). DEOY5ZM KD 33208: Metazoa DEOY5ZM PL 7711: Chordata DEOY5ZM CL 40674: Mammalia DEOY5ZM OD 9443: Primates DEOY5ZM FM 9604: Hominidae DEOY5ZM GE 9605: Homo DEOY5ZM SP 9606: Homo sapiens DE2JP1Y ID DE2JP1Y DE2JP1Y DN Aldehyde dehydrogenase 1 (ALDH1) DE2JP1Y GN ALDH1A1 DE2JP1Y SN Aldehyde dehydrogenase 1 family member A1; Cytosolic aldehyde dehydrogenase; ALDC; ALDH-E1; ALDH1; ALDH1A1; ALHDII; PUMB1; RALDH 1; RalDH1; Retinal dehydrogenase 1 DE2JP1Y UC AL1A1_HUMAN DE2JP1Y RD Decanal DE2JP1Y GI 216 DE2JP1Y E1 1: Oxidoreductase DE2JP1Y E2 1.2: Aldehyde/oxo donor oxidoreductase DE2JP1Y E3 1.2.1: NAD/NADP acceptor oxidoreductase DE2JP1Y EC 1.2.1.36 DE2JP1Y RC Ethanol oxidation:R-HSA-71384; Fructose catabolism:R-HSA-70350; RA biosynthesis pathway:R-HSA-5365859 DE2JP1Y KG Metabolic pathways:hsa01100; Retinol metabolism:hsa00830 DE2JP1Y PD 4WP7; 4WPN; 4X4L; 5AC2; 5L2M; 5L2N; 5L2O; 5TEI; 6DUM DE2JP1Y SQ MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYLNDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKIGPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQGQCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIESGKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGEYGFHEYTEVKTVTVKISQKNS DE2JP1Y TD Primarily distributed in liver. DE2JP1Y FC This enzyme can convert/oxidize retinaldehyde to retinoic acid and it may have a broader specificity and oxidize other aldehydes in vivo. DE2JP1Y KD 33208: Metazoa DE2JP1Y PL 7711: Chordata DE2JP1Y CL 40674: Mammalia DE2JP1Y OD 9443: Primates DE2JP1Y FM 9604: Hominidae DE2JP1Y GE 9605: Homo DE2JP1Y SP 9606: Homo sapiens DEB2ZMT ID DEB2ZMT DEB2ZMT DN Choline phosphatase 1 (PLD1) DEB2ZMT GN PLD1 DEB2ZMT SN Phosphatidylcholine-hydrolyzing phospholipase D1; Phospholipase D1; hPLD1; PLD 1; PLD1 DEB2ZMT UC PLD1_HUMAN DEB2ZMT RD Miltefosine DEB2ZMT GI 5337 DEB2ZMT E1 3: Hydrolases DEB2ZMT E2 3.1: Ester bond hydrolase DEB2ZMT E3 3.1.4: Phosphoric diester hydrolase DEB2ZMT EC 3.1.4.4 DEB2ZMT RC Neutrophil degranulation:R-HSA-6798695; Role of phospholipids in phagocytosis:R-HSA-2029485; Synthesis of PA:R-HSA-1483166; Synthesis of PG:R-HSA-1483148 DEB2ZMT KG Choline metabolism in cancer:hsa05231; Endocytosis:hsa04144; Ether lipid metabolism:hsa00565; Fc gamma R-mediated phagocytosis:hsa04666; Glutamatergic synapse:hsa04724; Glycerophospholipid metabolism:hsa00564; GnRH signaling pathway:hsa04912; Metabolic pathways:hsa01100; Pancreatic cancer:hsa05212; Parathyroid hormone synthesis, secretion and action:hsa04928; Pathways in cancer:hsa05200; Phospholipase D signaling pathway:hsa04072; Ras signaling pathway:hsa04014; Sphingolipid signaling pathway:hsa04071; cAMP signaling pathway:hsa04024 DEB2ZMT SQ MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT DEB2ZMT TD Primarily distributed in gallbladder, pancreas and heart. Also expressed in brain, placenta, spleen, uterus and small intestine. DEB2ZMT FC This enzyme catalyzes the hydrolysis of phosphatidylcholine in order to yield phosphatidic acid and choline. DEB2ZMT KD 33208: Metazoa DEB2ZMT PL 7711: Chordata DEB2ZMT CL 40674: Mammalia DEB2ZMT OD 9443: Primates DEB2ZMT FM 9604: Hominidae DEB2ZMT GE 9605: Homo DEB2ZMT SP 9606: Homo sapiens DEP6GT1 ID DEP6GT1 DEP6GT1 DN Small intestine reductase (AKR1B10) DEP6GT1 GN AKR1B10 DEP6GT1 SN Aldo-keto reductase family 1 member B10; SI reductase; Aldose reductase-related protein; Aldose reductase-like; AKR1B10; AKR1B11; ARL-1; ARP; hARP DEP6GT1 UC AK1BA_HUMAN DEP6GT1 RD Phenanthrenequinone DEP6GT1 GI 57016 DEP6GT1 E1 1: Oxidoreductase DEP6GT1 E2 1.1: CH-OH donor oxidoreductase DEP6GT1 E3 1.1.1: NAD/NADP oxidoreductase DEP6GT1 EC 1.1.1.21 DEP6GT1 RC Retinoid metabolism and transport:R-HSA-975634 DEP6GT1 KG Folate biosynthesis:hsa00790; Fructose and mannose metabolism:hsa00051; Galactose metabolism:hsa00052; Glycerolipid metabolism:hsa00561; Metabolic pathways:hsa01100; Pentose and glucuronate interconversions:hsa00040 DEP6GT1 PD 4GAB; 4GQ0; 4GQG; 4I5X; 4ICC; 4JIH; 4JII; 4WEV; 4XZL DEP6GT1 SQ MATFVELSTKAKMPIVGLGTWKSPLGKVKEAVKVAIDAGYRHIDCAYVYQNEHEVGEAIQEKIQEKAVKREDLFIVSKLWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKSGDDLFPKDDKGNAIGGKATFLDAWEAMEELVDEGLVKALGVSNFSHFQIEKLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTAAQVLIRFHIQRNVIVIPKSVTPARIVENIQVFDFKLSDEEMATILSFNRNWRACNVLQSSHLEDYPFNAEY DEP6GT1 TD Primarily distributed in small intestine, colon, adrenal gland, esophagus and stomach. DEP6GT1 FC This enzyme catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. It displays strong enzymatic activity toward all-trans- retinal, 9-cis-retinal, and 13-cis-retinal. It plays a critical role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4- hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls). DEP6GT1 KD 33208: Metazoa DEP6GT1 PL 7711: Chordata DEP6GT1 CL 40674: Mammalia DEP6GT1 OD 9443: Primates DEP6GT1 FM 9604: Hominidae DEP6GT1 GE 9605: Homo DEP6GT1 SP 9606: Homo sapiens DEBMFZ8 ID DEBMFZ8 DEBMFZ8 DN Estradiol 17-beta-dehydrogenase 2 (HSD17B2) DEBMFZ8 GN HSD17B2 DEBMFZ8 SN Testosterone 17-beta-dehydrogenase; Microsomal 17-beta-hydroxysteroid dehydrogenase; Short chain dehydrogenase/reductase family 9C member 2; 17-beta-HSD 2; 17-beta-hydroxysteroid dehydrogenase type 2; E2DH; EDH17B2; HSD17B2; SDR9C2 DEBMFZ8 UC DHB2_HUMAN DEBMFZ8 RD Estrone DEBMFZ8 GI 3294 DEBMFZ8 E1 1: Oxidoreductase DEBMFZ8 E2 1.1: CH-OH donor oxidoreductase DEBMFZ8 E3 1.1.1: NAD/NADP oxidoreductase DEBMFZ8 EC 1.1.1.62 DEBMFZ8 RC Estrogen biosynthesis:R-HSA-193144 DEBMFZ8 KG Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Steroid hormone biosynthesis:hsa00140 DEBMFZ8 SQ MSTFFSDTAWICLAVPTVLCGTVFCKYKKSSGQLWSWMVCLAGLCAVCLLILSPFWGLILFSVSCFLMYTYLSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYILAQRNFLLLINSLASKDFSPVLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYFAKRHFGQDKPMPRALRMPNYKKKAT DEBMFZ8 TD Primarily distributed in intestine, liver and placenta. DEBMFZ8 FC This enzyme is capable of catalyzing the interconversion of testosterone and androstenedione, as well as estradiol and estrone. It also has 20-alpha- HSD activity. DEBMFZ8 KD 33208: Metazoa DEBMFZ8 PL 7711: Chordata DEBMFZ8 CL 40674: Mammalia DEBMFZ8 OD 9443: Primates DEBMFZ8 FM 9604: Hominidae DEBMFZ8 GE 9605: Homo DEBMFZ8 SP 9606: Homo sapiens DESDN74 ID DESDN74 DESDN74 DN Serum paraoxonase/arylesterase 1 (PON1) DESDN74 GN PON1 DESDN74 SN Aromatic esterase 1; Serum aryldialkylphosphatase 1; A-esterase 1; PON 1; PON1; PON; K-45 DESDN74 UC PON1_HUMAN DESDN74 RD Loteprednol etabonate DESDN74 GI 5444 DESDN74 E1 3: Hydrolases DESDN74 E2 3.1: Ester bond hydrolase DESDN74 E3 3.1.1: Carboxylic ester hydrolase DESDN74 EC 3.1.1.2 DESDN74 RC Synthesis of 5-eicosatetraenoic acids:R-HSA-2142688 DESDN74 PD 1V04; 1XHR DESDN74 SQ MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL DESDN74 TD Primarily distributed in liver. DESDN74 FC This enzyme hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. It is capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. DESDN74 KD 33208: Metazoa DESDN74 PL 7711: Chordata DESDN74 CL 40674: Mammalia DESDN74 OD 9443: Primates DESDN74 FM 9604: Hominidae DESDN74 GE 9605: Homo DESDN74 SP 9606: Homo sapiens DEOVJF2 ID DEOVJF2 DEOVJF2 DN Retinoic acid 4-hydroxylase 26A1 (CYP26A1) DEOVJF2 GN CYP26A1 DEOVJF2 SN Retinoic acid 4-hydroxylase; Cytochrome P450 26A1; Retinoic acid-metabolizing cytochrome; Cytochrome P450 retinoic acid-inactivating 1; Cytochrome P450RAI; CYP26; CYP26A1; P450RAI1; hP450RAI DEOVJF2 UC CP26A_HUMAN DEOVJF2 RD NSC-122758 DEOVJF2 GI 1592 DEOVJF2 E1 1: Oxidoreductase DEOVJF2 E2 1.14: Oxygen paired donor oxidoreductase DEOVJF2 E3 1.14.13: NADH/NADPH donor oxidoreductase DEOVJF2 EC 1.14.13.- DEOVJF2 RC RA biosynthesis pathway:R-HSA-5365859; Vitamins:R-HSA-211916 DEOVJF2 KG Metabolic pathways:hsa01100; Retinol metabolism:hsa00830 DEOVJF2 SQ MGLPALLASALCTFVLPLLLFLAAIKLWDLYCVSGRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGSGCLSNLHDSSHKQRKKVIMRAFSREALECYVPVITEEVGSSLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPQLAGDGDSEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGMKARNLIHARIEQNIRAKICGLRASEAGQGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREELKSKGLLCKSNQDNKLDMEILEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVAEIFTNKEEFNPDRFMLPHPEDASRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPARFTHFHGEI DEOVJF2 TD Primarily distributed in liver and retina. DEOVJF2 FC This enzyme is involved in the metabolism of all-trans retinoic acid (atRA). It catalyzes the hydroxylation of carbon hydrogen bonds of atRA primarily at C-4 and C-18. It has no activity toward 9-cis and 13-cis retinoic acid stereoisomers and may play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid. DEOVJF2 KD 33208: Metazoa DEOVJF2 PL 7711: Chordata DEOVJF2 CL 40674: Mammalia DEOVJF2 OD 9443: Primates DEOVJF2 FM 9604: Hominidae DEOVJF2 GE 9605: Homo DEOVJF2 SP 9606: Homo sapiens DE37ABY ID DE37ABY DE37ABY DN Phosphodiesterase 5A (PDE5A) DE37ABY GN PDE5A DE37ABY SN Phosphodiesterase class 5A; cGMP-binding cGMP-specific phosphodiesterase; cGMP-specific 3',5'-cyclic phosphodiesterase; CGB-PDE; PDE5; PDE5A DE37ABY UC PDE5A_HUMAN DE37ABY RD Molsidomine DE37ABY GI 8654 DE37ABY E1 3: Hydrolases DE37ABY E2 3.1: Ester bond hydrolase DE37ABY E3 3.1.4: Phosphoric diester hydrolase DE37ABY EC 3.1.4.35 DE37ABY RC cGMP effects:R-HSA-418457 DE37ABY KG Metabolic pathways:hsa01100; Purine metabolism:hsa00230; cGMP-PKG signaling pathway:hsa04022 DE37ABY PD 1T9S; 1TBF; 1UDT; 1UDU; 1UHO; 1XOZ; 1XP0; 2CHM; 2H40 DE37ABY SQ MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN DE37ABY TD Primarily distributed in aortic smooth muscle cells, heart, placenta, skeletal muscle and pancreas. Also expressed in brain, liver and lung. DE37ABY FC This enzyme catalyzes the specific hydrolysis of cGMP to 5'-GMP. DE37ABY KD 33208: Metazoa DE37ABY PL 7711: Chordata DE37ABY CL 40674: Mammalia DE37ABY OD 9443: Primates DE37ABY FM 9604: Hominidae DE37ABY GE 9605: Homo DE37ABY SP 9606: Homo sapiens DEWYTJB ID DEWYTJB DEWYTJB DN Aldehyde dehydrogenase 2 (ALDH2) DEWYTJB GN ALDH2 DEWYTJB SN Aldehyde dehydrogenase 2 family member; Mitochondrial aldehyde dehydrogenase; ALDH class 2; ALDH-E2; ALDH2; ALDHI; ALDM DEWYTJB UC ALDH2_HUMAN DEWYTJB RD Silodosin DEWYTJB GI 217 DEWYTJB E1 1: Oxidoreductase DEWYTJB E2 1.2: Aldehyde/oxo donor oxidoreductase DEWYTJB E3 1.2.1: NAD/NADP acceptor oxidoreductase DEWYTJB EC 1.2.1.3 DEWYTJB RC Ethanol oxidation:R-HSA-71384; Metabolism of serotonin:R-HSA-380612 DEWYTJB KG Arginine and proline metabolism:hsa00330; Ascorbate and aldarate metabolism:hsa00053; Fatty acid degradation:hsa00071; Glycerolipid metabolism:hsa00561; Glycolysis / Gluconeogenesis:hsa00010; Histidine metabolism:hsa00340; Lysine degradation:hsa00310; Metabolic pathways:hsa01100; Pyruvate metabolism:hsa00620; Tryptophan metabolism:hsa00380; Valine, leucine and isoleucine degradation:hsa00280; beta-Alanine metabolism:hsa00410 DEWYTJB PD 1NZX; 1NZZ; 1O00; 1O01; 1O02; 1O04; 1O05; 1ZUM; 2ONM DEWYTJB SQ MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS DEWYTJB TD Primarily distributed in liver. DEWYTJB FC This enzyme belongs to the aldehyde dehydrogenase family of enzymes that catalyze the chemical transformation from acetaldehyde to acetic acid. AND it is the second enzyme of the major oxidative pathway of alcohol metabolism. DEWYTJB KD 33208: Metazoa DEWYTJB PL 7711: Chordata DEWYTJB CL 40674: Mammalia DEWYTJB OD 9443: Primates DEWYTJB FM 9604: Hominidae DEWYTJB GE 9605: Homo DEWYTJB SP 9606: Homo sapiens DE1XPGH ID DE1XPGH DE1XPGH DN Catalase (CAT) DE1XPGH GN CAT DE1XPGH SN Caperase; Ab-catalase; CAT; OMIM: 115500; MGI: 88271; HomoloGene: 55514; GeneCards: CAT DE1XPGH UC CATA_HUMAN DE1XPGH RD Hydrogen peroxide DE1XPGH GI 847 DE1XPGH E1 1: Oxidoreductase DE1XPGH E2 1.11: Peroxidase DE1XPGH E3 1.11.1: Peroxidase DE1XPGH EC 1.11.1.6 DE1XPGH RC Detoxification of Reactive Oxygen Species:R-HSA-3299685; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes:R-HSA-9615017; Neutrophil degranulation:R-HSA-6798695; Peroxisomal protein import:R-HSA-9033241 DE1XPGH KG Amyotrophic lateral sclerosis (ALS):hsa05014; Carbon metabolism:hsa01200; FoxO signaling pathway:hsa04068; Glyoxylate and dicarboxylate metabolism:hsa00630; Longevity regulating pathway - multiple species:hsa04213; Longevity regulating pathway:hsa04211; Metabolic pathways:hsa01100; Peroxisome:hsa04146; Tryptophan metabolism:hsa00380 DE1XPGH PD 1DGB; 1DGF; 1DGG; 1DGH; 1F4J; 1QQW DE1XPGH SQ MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYNAEKPKNAIHTFVQSGSHLAAREKANL DE1XPGH TD Primarily distributed in blood and liver. DE1XPGH FC This enzyme catalyzes the decomposition of hydrogen peroxide to water and oxygen. DE1XPGH KD 33208: Metazoa DE1XPGH PL 7711: Chordata DE1XPGH CL 40674: Mammalia DE1XPGH OD 9443: Primates DE1XPGH FM 9604: Hominidae DE1XPGH GE 9605: Homo DE1XPGH SP 9606: Homo sapiens DE3FYEM ID DE3FYEM DE3FYEM DN Calcidiol 1-monooxygenase (CYP27B1) DE3FYEM GN CYP27B1 DE3FYEM SN Cytochrome P450 subfamily XXVIIB polypeptide 1; VD3 1A hydroxylase; Cytochrome P450C1 alpha; Cytochrome P450VD1-alpha; Cytochrome p450 27B1; 25-OHD-1 alpha-hydroxylase; 25-hydroxyvitamin D(3) 1-alpha-hydroxylase; Mitochondrial 25-hydroxyvitamin D-1 alpha hydroxylase; CYP1ALPHA; CYP27B; CYP27B1 DE3FYEM UC CP27B_HUMAN DE3FYEM RD Calcifediol DE3FYEM GI 1594 DE3FYEM E1 1: Oxidoreductase DE3FYEM E2 1.14: Oxygen paired donor oxidoreductase DE3FYEM E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE3FYEM EC 1.14.15.18 DE3FYEM RC Defective CYP27B1 causes Rickets vitamin D-dependent 1A (VDDR1A):R-HSA-5579014; Vitamin D (calciferol) metabolism:R-HSA-196791; Vitamins:R-HSA-211916 DE3FYEM KG Metabolic pathways:hsa01100; Parathyroid hormone synthesis, secretion and action:hsa04928; Steroid biosynthesis:hsa00100; Tuberculosis:hsa05152 DE3FYEM SQ MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSRLHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCRQRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPPALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPHWLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFREELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPSATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPAQFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQPEPGAAPVRPKTRTVLVPERSINLQFLDR DE3FYEM TD Primarily distributed in kidney. DE3FYEM FC This enzyme is involved in vitamin D metabolism. It catalyzes the rate-limiting step in the activation of vitamin D in the kidney, namely the hydroxylation of 25-hydroxyvitamin D3/calcidiol at the C1alpha- position to form the hormonally active form of vitamin D3, 1alpha,25- dihydroxyvitamin D3/calcitriol that acts via the vitamin D receptor (VDR). It has 1alpha-hydroxylase activity on vitamin D intermediates of the CYP24A1-mediated inactivation pathway and converts 24R,25-dihydroxyvitamin D3/secalciferol to 1-alpha,24,25-trihydroxyvitamin D3 and also active on 25-hydroxyvitamin D2. DE3FYEM KD 33208: Metazoa DE3FYEM PL 7711: Chordata DE3FYEM CL 40674: Mammalia DE3FYEM OD 9443: Primates DE3FYEM FM 9604: Hominidae DE3FYEM GE 9605: Homo DE3FYEM SP 9606: Homo sapiens DEQ2BAJ ID DEQ2BAJ DEQ2BAJ DN Acetylcholinesterase (ACHE) DEQ2BAJ GN ACHE DEQ2BAJ SN Acetylhydrolase; Primary cholinesterase; ACHE; AChE; Acetylcholinesterase (Yt blood group); ACEE; ARN-YT; Acetylcholinesterase (Cartwright blood group); True cholinesterase DEQ2BAJ UC ACES_HUMAN DEQ2BAJ RD Acetylcholine chloride DEQ2BAJ GI 43 DEQ2BAJ E1 3: Hydrolases DEQ2BAJ E2 3.1: Ester bond hydrolase DEQ2BAJ E3 3.1.1: Carboxylic ester hydrolase DEQ2BAJ EC 3.1.1.7 DEQ2BAJ RC Neurotransmitter clearance:R-HSA-112311; Synthesis of PC:R-HSA-1483191; Synthesis, secretion, and deacylation of Ghrelin:R-HSA-422085 DEQ2BAJ KG Cholinergic synapse:hsa04725; Glycerophospholipid metabolism:hsa00564 DEQ2BAJ PD 1PUV; 1PUW; 1VZJ; 2CLJ; 2X8B; 3LII; 4BDT; 4EY4; 4EY5 DEQ2BAJ SQ MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQACAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL DEQ2BAJ TD Primarily distributed in brain and skeletal muscle. DEQ2BAJ FC This enzyme hydrolyzes of the acetylcholine released into the synaptic cleft to terminate signal transduction at the neuromuscular junction. DEQ2BAJ KD 33208: Metazoa DEQ2BAJ PL 7711: Chordata DEQ2BAJ CL 40674: Mammalia DEQ2BAJ OD 9443: Primates DEQ2BAJ FM 9604: Hominidae DEQ2BAJ GE 9605: Homo DEQ2BAJ SP 9606: Homo sapiens DEULQ45 ID DEULQ45 DEULQ45 DN Sodium/potassium-transporting ATPase gamma (FXYD2) DEULQ45 GN FXYD2 DEULQ45 SN FXYD domain-containing ion transport regulator 2; Na(+)/K(+) ATPase gamma; Sodium pump gamma chain; Sodium/potassium-transporting ATPase gamma; ATP1C; ATP1G1; FXYD2 DEULQ45 UC ATNG_HUMAN DEULQ45 RD HSDB-3165 DEULQ45 GI 486 DEULQ45 E1 3: Hydrolases DEULQ45 E2 3.6: Acid anhydride hydrolase DEULQ45 E3 3.6.1: Acid anhydride hydrolase DEULQ45 EC 3.6.1.- DEULQ45 RC Ion homeostasis:R-HSA-5578775; Ion transport by P-type ATPases:R-HSA-936837 DEULQ45 KG Adrenergic signaling in cardiomyocytes:hsa04261; Aldosterone-regulated sodium reabsorption:hsa04960; Bile secretion:hsa04976; Carbohydrate digestion and absorption:hsa04973; Cardiac muscle contraction:hsa04260; Endocrine and other factor-regulated calcium reabsorption:hsa04961; Insulin secretion:hsa04911; Mineral absorption:hsa04978; Pancreatic secretion:hsa04972; Protein digestion and absorption:hsa04974; Proximal tubule bicarbonate reclamation:hsa04964; Salivary secretion:hsa04970; Thyroid hormone signaling pathway:hsa04919; Thyroid hormone synthesis:hsa04918; cAMP signaling pathway:hsa04024; cGMP-PKG signaling pathway:hsa04022 DEULQ45 PD 2MKV DEULQ45 SQ MTGLSMDGGGSPKGDVDPFYYDYETVRNGGLIFAGLAFIVGLLILLSRRFRCGGNKKRRQINEDEP DEULQ45 TD Primarily distributed in kidney, pancreas and salivary gland. DEULQ45 FC This enzyme is involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase. DEULQ45 KD 33208: Metazoa DEULQ45 PL 7711: Chordata DEULQ45 CL 40674: Mammalia DEULQ45 OD 9443: Primates DEULQ45 FM 9604: Hominidae DEULQ45 GE 9605: Homo DEULQ45 SP 9606: Homo sapiens DE9Z281 ID DE9Z281 DE9Z281 DN Glutamyl-tRNA(Gln) amidotransferase B (GATB) DE9Z281 GN GATB DE9Z281 SN Cytochrome c oxidase assembly factor PET112 homolog; GATB; Glu-AdT subunit B; Mitochondrial glutamyl-tRNA(Gln) amidotransferase subunit B; HSPC199; PET112; PET112L DE9Z281 UC GATB_HUMAN DE9Z281 RD L-glutamine DE9Z281 GI 5188 DE9Z281 E1 6: Ligase DE9Z281 E2 6.3: Carbon-nitrogen ligase DE9Z281 E3 6.3.5: Carbon-nitrogen ligase DE9Z281 EC 6.3.5.7 DE9Z281 KG Aminoacyl-tRNA biosynthesis:hsa00970; Metabolic pathways:hsa01100 DE9Z281 SQ MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGEHKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQINELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATSLPAGADPQQVINIDQIRETLPELPSVTREKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRAEPKKVTSWVLNTFLGYLKQQNLAVSESPVTPSALAELLDLLDSRTISSSAAKQVFEELWKREGKTPGQIVSEKQLELMQDQGALEQLCHSVMEAHPQVVMDVKNRNPRAINKLIGLVRKATQSRADPVMIKEILEKKLSL DE9Z281 TD Primarily distributed in muscle and heart. DE9Z281 FC This enzyme allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. DE9Z281 KD 33208: Metazoa DE9Z281 PL 7711: Chordata DE9Z281 CL 40674: Mammalia DE9Z281 OD 9443: Primates DE9Z281 FM 9604: Hominidae DE9Z281 GE 9605: Homo DE9Z281 SP 9606: Homo sapiens DE3E0VT ID DE3E0VT DE3E0VT DN L-glutamine amidohydrolase (GLS) DE3E0VT GN GLS DE3E0VT SN K-glutaminase; Mitochondrial glutaminase kidney isoform; Mitochondrial 65 kDa glutaminase kidney isoform; Mitochondrial 68 kDa glutaminase kidney isoform; GLS; GLS1; KIAA0838 DE3E0VT UC GLSK_HUMAN DE3E0VT RD L-glutamine DE3E0VT GI 2744 DE3E0VT E1 3: Hydrolases DE3E0VT E2 3.5: Carbon-nitrogen hydrolase DE3E0VT E3 3.5.1: Linear amide hydrolase DE3E0VT EC 3.5.1.2 DE3E0VT RC Glutamate Neurotransmitter Release Cycle:R-HSA-210500; Glutamate and glutamine metabolism:R-HSA-8964539; TP53 Regulates Metabolic Genes:R-HSA-5628897 DE3E0VT KG Alanine, aspartate and glutamate metabolism:hsa00250; Arginine biosynthesis:hsa00220; Central carbon metabolism in cancer:hsa05230; D-Glutamine and D-glutamate metabolism:hsa00471; GABAergic synapse:hsa04727; Glutamatergic synapse:hsa04724; Metabolic pathways:hsa01100; MicroRNAs in cancer:hsa05206; Proximal tubule bicarbonate reclamation:hsa04964 DE3E0VT PD 3UO9; 3VOY; 3VOZ; 3VP0; 3VP1; 3VP2; 3VP3; 3VP4; 4O7D DE3E0VT SQ MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGGGGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEGKELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL DE3E0VT TD Primarily distributed in kidney. DE3E0VT FC This enzyme catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. DE3E0VT KD 33208: Metazoa DE3E0VT PL 7711: Chordata DE3E0VT CL 40674: Mammalia DE3E0VT OD 9443: Primates DE3E0VT FM 9604: Hominidae DE3E0VT GE 9605: Homo DE3E0VT SP 9606: Homo sapiens DEAJN47 ID DEAJN47 DEAJN47 DN Aldo-keto reductase 1C4 (AKR1C4) DEAJN47 GN AKR1C4 DEAJN47 SN Aldo-keto reductase family 1 member C4; CDR; CHDR; Chlordecone reductase; DD-4; DD4; Dihydrodiol dehydrogenase 4; HAKRA; 3-alpha-HSD1; 3-alpha-hydroxysteroid dehydrogenase type I; AKR1C4 DEAJN47 UC AK1C4_HUMAN DEAJN47 RD Nabumetone DEAJN47 GI 1109 DEAJN47 E1 1: Oxidoreductase DEAJN47 E2 1.1: CH-OH donor oxidoreductase DEAJN47 E3 1.1.1: NAD/NADP oxidoreductase DEAJN47 EC 1.1.1.357 DEAJN47 RC Retinoid metabolism and transport:R-HSA-975634; Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DEAJN47 KG Metabolic pathways:hsa01100; Primary bile acid biosynthesis:hsa00120; Steroid hormone biosynthesis:hsa00140 DEAJN47 PD 2FVL DEAJN47 SQ MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVVMDFLMDHPDYPFSDEY DEAJN47 TD Primarily distributed in liver. DEAJN47 FC This enzyme catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan- 3-alpha,17-beta-diol (3-alpha-diol). It also has some 20-alpha- hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route. DEAJN47 KD 33208: Metazoa DEAJN47 PL 7711: Chordata DEAJN47 CL 40674: Mammalia DEAJN47 OD 9443: Primates DEAJN47 FM 9604: Hominidae DEAJN47 GE 9605: Homo DEAJN47 SP 9606: Homo sapiens DEZS5YK ID DEZS5YK DEZS5YK DN Estradiol 17-beta-dehydrogenase 1 (HSD17B1) DEZS5YK GN HSD17B1 DEZS5YK SN Placental 17-beta-hydroxysteroid dehydrogenase; Short chain dehydrogenase/reductase family 28C member 1; 17-beta-HSD 1; 17-beta-hydroxysteroid dehydrogenase type 1; 20 alpha-hydroxysteroid dehydrogenase; 20-alpha-HSD; E17KSR; EDH17B1; EDHB17; HSD17B1; SDR28C1 DEZS5YK UC DHB1_HUMAN DEZS5YK RD Dehydroepiandrosterone DEZS5YK GI 3292 DEZS5YK E1 1: Oxidoreductase DEZS5YK E2 1.1: CH-OH donor oxidoreductase DEZS5YK E3 1.1.1: NAD/NADP oxidoreductase DEZS5YK EC 1.1.1.62 DEZS5YK RC Estrogen biosynthesis:R-HSA-193144; The canonical retinoid cycle in rods (twilight vision):R-HSA-2453902 DEZS5YK KG Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Steroid hormone biosynthesis:hsa00140 DEZS5YK PD 1DHT; 1EQU; 1FDS; 1FDT; 1FDU; 1FDV; 1FDW; 1I5R; 1IOL DEZS5YK SQ MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ DEZS5YK TD Primarily distributed in placenta. DEZS5YK FC This enzyme favors the reduction of estrogens and androgens. It also has 20- alpha-HSD activity. DEZS5YK KD 33208: Metazoa DEZS5YK PL 7711: Chordata DEZS5YK CL 40674: Mammalia DEZS5YK OD 9443: Primates DEZS5YK FM 9604: Hominidae DEZS5YK GE 9605: Homo DEZS5YK SP 9606: Homo sapiens DEYLWI6 ID DEYLWI6 DEYLWI6 DN Serine sulfhydrase (CBS) DEYLWI6 GN CBS DEYLWI6 SN Cystathionine beta-synthase; Cytosolic serine acetyltransferase; Beta-thionase; CBS DEYLWI6 UC CBS_HUMAN DEYLWI6 RD Arsenic DEYLWI6 GI 875 DEYLWI6 E1 4: Lyases DEYLWI6 E2 4.2: Carbon-oxygen lyase DEYLWI6 E3 4.2.1: Hydro-lyase DEYLWI6 EC 4.2.1.22 DEYLWI6 RC Cysteine formation from homocysteine:R-HSA-1614603; Metabolism of ingested SeMet, Sec, MeSec into H2Se:R-HSA-2408508 DEYLWI6 KG Biosynthesis of amino acids:hsa01230; Cysteine and methionine metabolism:hsa00270; Glycine, serine and threonine metabolism:hsa00260; Metabolic pathways:hsa01100 DEYLWI6 PD 1JBQ; 1M54; 4COO; 4L0D; 4L28; 4L3V; 4PCU; 4UUU; 5MMS DEYLWI6 SQ MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLNFVAAQERDQK DEYLWI6 TD Primarily distributed in liver and pancreas. DEYLWI6 FC This enzyme catalyzes the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine. DEYLWI6 KD 33208: Metazoa DEYLWI6 PL 7711: Chordata DEYLWI6 CL 40674: Mammalia DEYLWI6 OD 9443: Primates DEYLWI6 FM 9604: Hominidae DEYLWI6 GE 9605: Homo DEYLWI6 SP 9606: Homo sapiens DE31KMQ ID DE31KMQ DE31KMQ DN Microsomal glutathione S-transferase 2 (MGST2) DE31KMQ GN MGST2 DE31KMQ SN Glutathione microsomal transferase 2; Microsomal GST-2; Microsomal GST-II; MGST2 DE31KMQ UC MGST2_HUMAN DE31KMQ RD Busulfan DE31KMQ GI 4258 DE31KMQ E1 2: Transferase DE31KMQ E2 2.5: Alkyl/aryl transferase DE31KMQ E3 2.5.1: Alkyl/aryl transferase DE31KMQ EC 2.5.1.18 DE31KMQ RC Aflatoxin activation and detoxification:R-HSA-5423646; Glutathione conjugation:R-HSA-156590 DE31KMQ KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DE31KMQ SQ MAGNSILLAAVSILSACQQSYFALQVGKARLKYKVTPPAVTGSPEFERVFRAQQNCVEFYPIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKRITGFRLSLGILALLTLLGALGIANSFLDEYLDLNIAKKLRRQF DE31KMQ TD Primarily distributed in liver, spleen, skeletal muscle, heart, adrenals, pancreas, prostate, testis, fetal liver and fetal spleen. DE31KMQ FC This enzyme can catalyze the production of LTC4 from LTA4 and reduced glutathione, and it can catalyze the conjugation of 1-chloro-2,4- dinitrobenzene with reduced glutathione. DE31KMQ KD 33208: Metazoa DE31KMQ PL 7711: Chordata DE31KMQ CL 40674: Mammalia DE31KMQ OD 9443: Primates DE31KMQ FM 9604: Hominidae DE31KMQ GE 9605: Homo DE31KMQ SP 9606: Homo sapiens DEF75S0 ID DEF75S0 DEF75S0 DN Transglutaminase H (TGM2) DEF75S0 GN TGM2 DEF75S0 SN Protein-glutamine gamma-glutamyltransferase H; Transglutaminase-2; Protein-glutamine gamma-glutamyltransferase 2; Tissue transglutaminase; Transglutaminase C; TG(C); TGC; TGM2; TGase C; TGase H; TGase-2 DEF75S0 UC TGM2_HUMAN DEF75S0 RD L-glutamine DEF75S0 GI 7052 DEF75S0 E1 2: Transferase DEF75S0 E2 2.3: Acyltransferase DEF75S0 E3 2.3.2: Aminoacyltransferase DEF75S0 EC 2.3.2.13 DEF75S0 KG Huntington's disease:hsa05016 DEF75S0 PD 1FAU; 1KV3; 2Q3Z; 3LY6; 3S3J; 3S3P; 3S3S; 4PYG; 6A8P DEF75S0 SQ MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYVLTQQGFIYQGSAKFIKNIPWNFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEKSVPLCILYEKYRDCLTESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPDPVEAGEEVKVRMDLLPLHMGLHKLVVNFESDKLKAVKGFRNVIIGPA DEF75S0 TD Primarily distributed in liver and placenta. DEF75S0 FC This enzyme catalyzes the cross-linking of proteins, such as WDR54, and the conjugation of polyamines to proteins. DEF75S0 KD 33208: Metazoa DEF75S0 PL 7711: Chordata DEF75S0 CL 40674: Mammalia DEF75S0 OD 9443: Primates DEF75S0 FM 9604: Hominidae DEF75S0 GE 9605: Homo DEF75S0 SP 9606: Homo sapiens DEVEFKM ID DEVEFKM DEVEFKM DN Alkaline phosphatase (ALPL) DEVEFKM GN ALPL DEVEFKM SN Alkaline phosphatase liver/bone/kidney isozyme; Alkaline phosphatase tissue-nonspecific isozyme; ALPL; AP-TNAP; TNSALP DEVEFKM UC PPBT_HUMAN DEVEFKM RD Amifostine DEVEFKM GI 249 DEVEFKM E1 3: Hydrolases DEVEFKM E2 3.1: Ester bond hydrolase DEVEFKM E3 3.1.3: Phosphoric monoester hydrolase DEVEFKM EC 3.1.3.1 DEVEFKM RC Post-translational modification-synthesis of GPI-anchored proteins:R-HSA-163125 DEVEFKM KG Folate biosynthesis:hsa00790; Metabolic pathways:hsa01100; Thiamine metabolism:hsa00730 DEVEFKM SQ MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF DEVEFKM TD Primarily distributed in blood, liver and lung. DEVEFKM FC This enzyme plays a key role in skeletal mineralization by regulating levels of diphosphate (PPi). DEVEFKM KD 33208: Metazoa DEVEFKM PL 7711: Chordata DEVEFKM CL 40674: Mammalia DEVEFKM OD 9443: Primates DEVEFKM FM 9604: Hominidae DEVEFKM GE 9605: Homo DEVEFKM SP 9606: Homo sapiens DEXPVUN ID DEXPVUN DEXPVUN DN Short-chain dehydrogenase/reductase retSDR1 (DHRS3) DEXPVUN GN DHRS3 DEXPVUN SN Short chain dehydrogenase/reductase family 16C member 1; Retinal short-chain dehydrogenase/reductase 1; Retinol dehydrogenase 17; Short-chain dehydrogenase/reductase 3; DD83.1; DHRS3; RDH17; SDR16C1; UNQ2424/PRO4983; retSDR1 DEXPVUN UC DHRS3_HUMAN DEXPVUN RD Acetohexamide DEXPVUN GI 9249 DEXPVUN E1 1: Oxidoreductase DEXPVUN E2 1.1: CH-OH donor oxidoreductase DEXPVUN E3 1.1.1: NAD/NADP oxidoreductase DEXPVUN EC 1.1.1.300 DEXPVUN RC RA biosynthesis pathway:R-HSA-5365859; The retinoid cycle in cones (daylight vision):R-HSA-2187335 DEXPVUN KG Metabolic pathways:hsa01100; Retinol metabolism:hsa00830 DEXPVUN SQ MVWKRLGALVMFPLQMIYLVVKAAVGLVLPAKLRDLSRENVLITGGGRGIGRQLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQTAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHINTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVEAVQLNQALLLLPWTMHALVILKSILPQAALEEIHKFSGTYTCMNTFKGRT DEXPVUN TD Primarily distributed in heart, placenta, lung, liver, kidney, pancreas, thyroid, testis, stomach, trachea and spinal cord. DEXPVUN FC This enzyme catalyzes the reduction of all-trans-retinal to all-trans- retinol in the presence of NADPH. DEXPVUN KD 33208: Metazoa DEXPVUN PL 7711: Chordata DEXPVUN CL 40674: Mammalia DEXPVUN OD 9443: Primates DEXPVUN FM 9604: Hominidae DEXPVUN GE 9605: Homo DEXPVUN SP 9606: Homo sapiens DELOY3P ID DELOY3P DELOY3P DN UDP-glucuronosyltransferase 1A4 (UGT1A4) DELOY3P GN UGT1A4 DELOY3P SN UDP-glucuronosyltransferase family 1 member A4; UDP-glucuronosyltransferase 1-D; UDP-glucuronosyltransferase 1-4; Bilirubin-specific UDPGT isozyme 2; UDPGT 1-4; UGT-1D; UGT1*4; UGT1-04; UGT1.4; UGT1A4; UGT1D; hUG-BR2 DELOY3P UC UD14_HUMAN DELOY3P RD Rilpivirine hydrochloride DELOY3P GI 54657 DELOY3P E1 2: Transferase DELOY3P E2 2.4: Glycosyltransferases DELOY3P E3 2.4.1: Hexosyltransferase DELOY3P EC 2.4.1.17 DELOY3P RC Defective UGT1A4 causes hyperbilirubinemia:R-HSA-5579016; Glucuronidation:R-HSA-156588; Heme degradation:R-HSA-189483 DELOY3P KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DELOY3P SQ MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVVLTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNVSLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDLDFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQREVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH DELOY3P TD Primarily distributed in liver. Also expressed in kidney, colon and small intestine. DELOY3P FC This enzyme glucuronidates bilirubin IX-alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. DELOY3P KD 33208: Metazoa DELOY3P PL 7711: Chordata DELOY3P CL 40674: Mammalia DELOY3P OD 9443: Primates DELOY3P FM 9604: Hominidae DELOY3P GE 9605: Homo DELOY3P SP 9606: Homo sapiens DEUTDON ID DEUTDON DEUTDON DN Superoxide dismutase 1 (SOD1) DEUTDON GN SOD1 DEUTDON SN Superoxide dismutase [Cu-Zn]; Superoxide dismutase [Copper-Zinc]; SOD1; hSod1 DEUTDON UC SODC_HUMAN DEUTDON RD Cisplatin DEUTDON GI 6647 DEUTDON E1 1: Oxidoreductase DEUTDON E2 1.15: Superoxide radical acceptor oxidoreductase DEUTDON E3 1.15.1: Superoxide radical acceptor oxidoreductase DEUTDON EC 1.15.1.1 DEUTDON RC Detoxification of Reactive Oxygen Species:R-HSA-3299685; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation:R-HSA-8950505; Platelet degranulation:R-HSA-114608 DEUTDON KG Amyotrophic lateral sclerosis (ALS):hsa05014; Huntington's disease:hsa05016; Longevity regulating pathway - multiple species:hsa04213; Peroxisome:hsa04146; Prion diseases:hsa05020 DEUTDON PD 2VR8; 2WKO; 3RE0; 3T5W; 4A7G; 5YTU; 5YUL; 6A9O; 6B79 DEUTDON SQ MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ DEUTDON TD Primarily distributed in liver. DEUTDON FC This enzyme destroys radicals which are normally produced within the cells and which are toxic to biological systems. DEUTDON KD 33208: Metazoa DEUTDON PL 7711: Chordata DEUTDON CL 40674: Mammalia DEUTDON OD 9443: Primates DEUTDON FM 9604: Hominidae DEUTDON GE 9605: Homo DEUTDON SP 9606: Homo sapiens DEAZDL8 ID DEAZDL8 DEAZDL8 DN UDP-glucuronosyltransferase 2B17 (UGT2B17) DEAZDL8 GN UGT2B17 DEAZDL8 SN UDP-glucuronosyltransferase family 2 member B17; C19-steroid-specific UDP-glucuronosyltransferase; C19-steroid-specific UDPGT; UDPGT 2B17; UGT2B17 DEAZDL8 UC UDB17_HUMAN DEAZDL8 RD Vorinostat DEAZDL8 GI 7367 DEAZDL8 E1 2: Transferase DEAZDL8 E2 2.4: Glycosyltransferases DEAZDL8 E3 2.4.1: Hexosyltransferase DEAZDL8 EC 2.4.1.17 DEAZDL8 RC Glucuronidation:R-HSA-156588 DEAZDL8 KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEAZDL8 SQ MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSASILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEYSDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYTVEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEVLGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRTMSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD DEAZDL8 TD Primarily distributed in intestine and liver. DEAZDL8 FC This enzyme has a major substrates eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) > androstane-3-alpha,17-beta-diol (3-alpha-diol) > testosterone > androsterone (ADT). DEAZDL8 KD 33208: Metazoa DEAZDL8 PL 7711: Chordata DEAZDL8 CL 40674: Mammalia DEAZDL8 OD 9443: Primates DEAZDL8 FM 9604: Hominidae DEAZDL8 GE 9605: Homo DEAZDL8 SP 9606: Homo sapiens DELF8BA ID DELF8BA DELF8BA DN Glutamine-dependent NAD(+) synthetase (NADSYN1) DELF8BA GN NADSYN1 DELF8BA SN NAD(+) synthase [glutamine-hydrolyzing]; NAD(+) synthetase; NADSYN1 DELF8BA UC NADE_HUMAN DELF8BA RD L-glutamine DELF8BA GI 55191 DELF8BA E1 6: Ligase DELF8BA E2 6.3: Carbon-nitrogen ligase DELF8BA E3 6.3.5: Carbon-nitrogen ligase DELF8BA EC 6.3.5.1 DELF8BA RC Nicotinate metabolism:R-HSA-196807 DELF8BA KG Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760 DELF8BA SQ MGRKVTVATCALNQWALDFEGNLQRILKSIEIAKNRGARYRLGPELEICGYGCWDHYYESDTLLHSFQVLAALVESPVTQDIICDVGMPVMHRNVRYNCRVIFLNRKILLIRPKMALANEGNYRELRWFTPWSRSRHTEEYFLPRMIQDLTKQETVPFGDAVLVTWDTCIGSEICEELWTPHSPHIDMGLDGVEIITNASGSHQVLRKANTRVDLVTMVTSKNGGIYLLANQKGCDGDRLYYDGCAMIAMNGSVFAQGSQFSLDDVEVLTATLDLEDVRSYRAEISSRNLAASRASPYPRVKVDFALSCHEDLLAPISEPIEWKYHSPEEEISLGPACWLWDFLRRSQQAGFLLPLSGGVDSAATACLIYSMCCQVCEAVRSGNEEVLADVRTIVNQISYTPQDPRDLCGRILTTCYMASKNSSQETCTRARELAQQIGSHHISLNIDPAVKAVMGIFSLVTGKSPLFAAHGGSSRENLALQNVQARIRMVLAYLFAQLSLWSRGVHGGLLVLGSANVDESLLGYLTKYDCSSADINPIGGISKTDLRAFVQFCIQRFQLPALQSILLAPATAELEPLADGQVSQTDEEDMGMTYAELSVYGKLRKVAKMGPYSMFCKLLGMWRHICTPRQVADKVKRFFSKYSMNRHKMTTLTPAYHAENYSPEDNRFDLRPFLYNTSWPWQFRCIENQVLQLERAEPQSLDGVD DELF8BA TD Low tissue/organ specificity. DELF8BA FC This enzyme catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. DELF8BA KD 33208: Metazoa DELF8BA PL 7711: Chordata DELF8BA CL 40674: Mammalia DELF8BA OD 9443: Primates DELF8BA FM 9604: Hominidae DELF8BA GE 9605: Homo DELF8BA SP 9606: Homo sapiens DEIHSMD ID DEIHSMD DEIHSMD DN Butyrylcholine esterase (BCHE) DEIHSMD GN BCHE DEIHSMD SN Acylcholine acylhydrolase; Choline esterase II; Cholinesterase; Pseudocholinesterase; BCHE; CHE1 DEIHSMD UC CHLE_HUMAN DEIHSMD RD Cocaine DEIHSMD GI 590 DEIHSMD E1 3: Hydrolases DEIHSMD E2 3.1: Ester bond hydrolase DEIHSMD E3 3.1.1: Carboxylic ester hydrolase DEIHSMD EC 3.1.1.8 DEIHSMD RC Neurotransmitter clearance:R-HSA-112311; Synthesis of PC:R-HSA-1483191; Synthesis, secretion, and deacylation of Ghrelin:R-HSA-422085 DEIHSMD PD 1KCJ; 1P0I; 1P0M; 1P0P; 1P0Q; 1XLU; 1XLV; 1XLW; 2J4C DEIHSMD SQ MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL DEIHSMD TD Primarily distributed in liver. DEIHSMD FC This enzyme has a broad substrate specificity. It contributes to the inactivation of the neurotransmitter acetylcholine and it can degrade neurotoxic organophosphate esters. DEIHSMD KD 33208: Metazoa DEIHSMD PL 7711: Chordata DEIHSMD CL 40674: Mammalia DEIHSMD OD 9443: Primates DEIHSMD FM 9604: Hominidae DEIHSMD GE 9605: Homo DEIHSMD SP 9606: Homo sapiens DE5LFD8 ID DE5LFD8 DE5LFD8 DN Phosphoribosylformylglycinamidine synthase (PFAS) DE5LFD8 GN PFAS DE5LFD8 SN Formylglycinamide ribonucleotide amidotransferase; Formylglycinamide ribotide amidotransferase; FGAM synthase; FGAR amidotransferase; FGAR-AT; FGAMS; KIAA0361; PFAS DE5LFD8 UC PUR4_HUMAN DE5LFD8 RD L-glutamine DE5LFD8 GI 5198 DE5LFD8 E1 6: Ligase DE5LFD8 E2 6.3: Carbon-nitrogen ligase DE5LFD8 E3 6.3.5: Carbon-nitrogen ligase DE5LFD8 EC 6.3.5.3 DE5LFD8 RC Purine ribonucleoside monophosphate biosynthesis:R-HSA-73817 DE5LFD8 KG Metabolic pathways:hsa01100; Purine metabolism:hsa00230 DE5LFD8 SQ MSPVLHFYVRPSGHEGAAPGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKLMWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVETTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEGRLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLHVDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQGLRHVVFTAETHNFPTGVCPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGYNLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREWIKPIMFSGGIGSMEADHISKEAPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPKGNPICSLHDQGAGGNGNVLKELSDPAGAIIYTSRFQLGDPTLNALEIWGAEYQESNALLLRSPNRDFLTHVSARERCPACFVGTITGDRRIVLVDDRECPVRRNGQGDAPPTPLPTPVDLELEWVLGKMPRKEFFLQRKPPMLQPLALPPGLSVHQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHEELIGAATALGEQPVKSLLDPKVAARLAVAEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAALADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVRAPGSLVISAYAVCPDITATVTPDLKHPEGRGHLLYVALSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFSITQGLLKDRLLCSGHDVSDGGLVTCLLEMAFAGNCGLQVDVPVPRVDVLSVLFAEEPGLVLEVQEPDLAQVLKRYRDAGLHCLELGHTGEAGPHAMVRVSVNGAVVLEEPVGELRALWEETSFQLDRLQAEPRCVAEEERGLRERMGPSYCLPPTFPKASVPREPGGPSPRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAIGLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFHPRAGAELRRFRKRPDTFSLGVCNGCQLLALLGWVGGDPNEDAAEMGPDSQPARPGLLLRHNLSGRYESRWASVRVGPGPALMLRGMEGAVLPVWSAHGEGYVAFSSPELQAQIEARGLAPLHWADDDGNPTEQYPLNPNGSPGGVAGICSCDGRHLAVMPHPERAVRPWQWAWRPPPFDTLTTSPWLQLFINARNWTLEGSC DE5LFD8 TD Low tissue/organ specificity. DE5LFD8 FC This enzyme catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. DE5LFD8 KD 33208: Metazoa DE5LFD8 PL 7711: Chordata DE5LFD8 CL 40674: Mammalia DE5LFD8 OD 9443: Primates DE5LFD8 FM 9604: Hominidae DE5LFD8 GE 9605: Homo DE5LFD8 SP 9606: Homo sapiens DES9MCU ID DES9MCU DES9MCU DN Kynurenine aminotransferase I (KYAT1) DES9MCU GN KYAT1 DES9MCU SN Glutamine transaminase K; Glutamine--phenylpyruvate transaminase; Cysteine-S-conjugate beta-lyase; Kynurenine aminotransferase 1; Kynurenine--oxoglutarate transaminase 1; Kynurenine--oxoglutarate transaminase I; CCBL1; GTK; KATI; KYAT1 DES9MCU UC KAT1_HUMAN DES9MCU RD L-glutamine DES9MCU GI 883 DES9MCU E1 2: Transferase DES9MCU E2 2.6: Transaminase DES9MCU E3 2.6.1: Transaminase DES9MCU EC 2.6.1.7 DES9MCU RC Glutamate and glutamine metabolism:R-HSA-8964539; Phenylalanine metabolism:R-HSA-8964208; Tryptophan catabolism:R-HSA-71240 DES9MCU KG Chemical carcinogenesis:hsa05204; Cysteine and methionine metabolism:hsa00270; Metabolic pathways:hsa01100; Selenocompound metabolism:hsa00450; Tryptophan metabolism:hsa00380 DES9MCU PD 1W7L; 1W7M; 1W7N; 3FVS; 3FVU; 3FVX; 4WLH; 4WLJ; 4WP0 DES9MCU SQ MAKQLQARRLDGIDYNPWVEFVKLASEHDVVNLGQGFPDFPPPDFAVEAFQHAVSGDFMLNQYTKTFGYPPLTKILASFFGELLGQEIDPLRNVLVTVGGYGALFTAFQALVDEGDEVIIIEPFFDCYEPMTMMAGGRPVFVSLKPGPIQNGELGSSSNWQLDPMELAGKFTSRTKALVLNTPNNPLGKVFSREELELVASLCQQHDVVCITDEVYQWMVYDGHQHISIASLPGMWERTLTIGSAGKTFSATGWKVGWVLGPDHIMKHLRTVHQNSVFHCPTQSQAAVAESFEREQLLFRQPSSYFVQFPQAMQRCRDHMIRSLQSVGLKPIIPQGSYFLITDISDFKRKMPDLPGAVDEPYDRRFVKWMIKNKGLVAIPVSIFYSVPHQKHFDHYIRFCFVKDEATLQAMDEKLRKWKVEL DES9MCU TD Low tissue/organ specificity. DES9MCU FC This enzyme catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). It metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. It also catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond. DES9MCU KD 33208: Metazoa DES9MCU PL 7711: Chordata DES9MCU CL 40674: Mammalia DES9MCU OD 9443: Primates DES9MCU FM 9604: Hominidae DES9MCU GE 9605: Homo DES9MCU SP 9606: Homo sapiens DE2MV1R ID DE2MV1R DE2MV1R DN Adenine phosphoribosyltransferase (APRT) DE2MV1R GN APRT DE2MV1R SN Adenine phosphoribosyltransferase enzyme; AMP; APRTD; APRTase; APRT DE2MV1R UC APT_HUMAN DE2MV1R RD Adenosine phosphate DE2MV1R GI 353 DE2MV1R E1 2: Transferase DE2MV1R E2 2.4: Glycosyltransferases DE2MV1R E3 2.4.2: Pentosyltransferase DE2MV1R EC 2.4.2.7 DE2MV1R RC Neutrophil degranulation:R-HSA-6798695; Purine salvage:R-HSA-74217 DE2MV1R KG Metabolic pathways:hsa01100; Purine metabolism:hsa00230 DE2MV1R PD 1ZN7; 1ZN8; 1ZN9; 4X44; 4X45; 6FCH; 6FCI; 6FCL; 6FD4 DE2MV1R SQ MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE DE2MV1R TD Low tissue/organ specificity. DE2MV1R FC This enzyme catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. DE2MV1R KD 33208: Metazoa DE2MV1R PL 7711: Chordata DE2MV1R CL 40674: Mammalia DE2MV1R OD 9443: Primates DE2MV1R FM 9604: Hominidae DE2MV1R GE 9605: Homo DE2MV1R SP 9606: Homo sapiens DEW8QEH ID DEW8QEH DEW8QEH DN Transglutaminase X (TGM5) DEW8QEH GN TGM5 DEW8QEH SN Protein-glutamine gamma-glutamyltransferase X; Transglutaminase-5; Protein-glutamine gamma-glutamyltransferase 5; TGase X; TGase-5; TG(X); TGM5; TGMX; TGX DEW8QEH UC TGM5_HUMAN DEW8QEH RD L-glutamine DEW8QEH GI 9333 DEW8QEH E1 2: Transferase DEW8QEH E2 2.3: Acyltransferase DEW8QEH E3 2.3.2: Aminoacyltransferase DEW8QEH EC 2.3.2.13 DEW8QEH RC Formation of the cornified envelope:R-HSA-6809371 DEW8QEH SQ MAQGLEVALTDLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFRNRSFQPGLDNIIFVVETGPLPDLALGTRAVFSLARHHSPSPWIAWLETNGATSTEVSLCAPPTAAVGRYLLKIHIDSFQGSVTAYQLGEFILLFNPWCPEDAVYLDSEPQRQEYVMNDYGFIYQGSKNWIRPCPWNYGQFEDKIIDICLKLLDKSLHFQTDPATDCALRGSPVYVSRVVCAMINSNDDNGVLNGNWSENYTDGANPAEWTGSVAILKQWNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIDEYYDNTGRILGNKKKDTIWNFHVWNECWMARKDLPPAYGGWQVLDATPQEMSNGVYCCGPASVRAIKEGEVDLNYDTPFVFSMVNADCMSWLVQGGKEQKLHQDTSSVGNFISTKSIQSDERDDITENYKYEEGSLQERQVFLKALQKLKARSFHGSQRGAELQPSRPTSLSQDSPRSLHTPSLRPSDVVQVSLKFKLLDPPNMGQDICFVLLALNMSSQFKDLKVNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYSQYLSTDKLIRISALGEEKSSPEKILVNKIITLSYPSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVLTVEGSGLFKKQQKVFLGVLKPQHQASIILETVPFKSGQRQIQANMRSNKFKDIKGYRNVYVDFAL DEW8QEH TD Primarily distributed in esophagus, lymphoid tissue, skin and tongue. DEW8QEH FC This enzyme catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. DEW8QEH KD 33208: Metazoa DEW8QEH PL 7711: Chordata DEW8QEH CL 40674: Mammalia DEW8QEH OD 9443: Primates DEW8QEH FM 9604: Hominidae DEW8QEH GE 9605: Homo DEW8QEH SP 9606: Homo sapiens DEWBT6H ID DEWBT6H DEWBT6H DN UDP-glucuronosyltransferase 2A3 (UGT2A3) DEWBT6H GN UGT2A3 DEWBT6H SN UDP-glucuronosyltransferase family 2 member A3; UDPGT 2A3; UGT2A3; UNQ2559/PRO6239 DEWBT6H UC UD2A3_HUMAN DEWBT6H RD Hyodeoxycholic acid DEWBT6H GI 79799 DEWBT6H E1 2: Transferase DEWBT6H E2 2.4: Glycosyltransferases DEWBT6H E3 2.4.1: Hexosyltransferase DEWBT6H EC 2.4.1.17 DEWBT6H RC Glucuronidation:R-HSA-156588 DEWBT6H KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEWBT6H SQ MRSDKSALVFLLLQLFCVGCGFCGKVLVWPCDMSHWLNVKVILEELIVRGHEVTVLTHSKPSLIDYRKPSALKFEVVHMPQDRTEENEIFVDLALNVLPGLSTWQSVIKLNDFFVEIRGTLKMMCESFIYNQTLMKKLQETNYDVMLIDPVIPCGDLMAELLAVPFVLTLRISVGGNMERSCGKLPAPLSYVPVPMTGLTDRMTFLERVKNSMLSVLFHFWIQDYDYHFWEEFYSKALGRPTTLCETVGKAEIWLIRTYWDFEFPQPYQPNFEFVGGLHCKPAKALPKEMENFVQSSGEDGIVVFSLGSLFQNVTEEKANIIASALAQIPQKVLWRYKGKKPSTLGANTRLYDWIPQNDLLGHPKTKAFITHGGMNGIYEAIYHGVPMVGVPIFGDQLDNIAHMKAKGAAVEINFKTMTSEDLLRALRTVITDSSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRSAAHDLTWFQHYSIDVIGFLLACVATAIFLFTKCFLFSCQKFNKTRKIEKRE DEWBT6H TD Primarily distributed in intestine and kidney. DEWBT6H FC This enzyme catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. DEWBT6H KD 33208: Metazoa DEWBT6H PL 7711: Chordata DEWBT6H CL 40674: Mammalia DEWBT6H OD 9443: Primates DEWBT6H FM 9604: Hominidae DEWBT6H GE 9605: Homo DEWBT6H SP 9606: Homo sapiens DEU7MWJ ID DEU7MWJ DEU7MWJ DN Gamma-Glu-X carboxypeptidase (GGH) DEU7MWJ GN GGH DEU7MWJ SN Gamma-glutamyl hydrolase; Carboxypeptidase AtGGH2; Folate conjugase AtGGH2; Folate hydrolase AtGGH2; Conjugase AtGGH2; GGH; GH DEU7MWJ UC GGH_HUMAN DEU7MWJ RD Methotrexate DEU7MWJ GI 8836 DEU7MWJ E1 3: Hydrolases DEU7MWJ E2 3.4: Peptidase DEU7MWJ E3 3.4.19: Omega peptidase DEU7MWJ EC 3.4.19.9 DEU7MWJ RC Neutrophil degranulation:R-HSA-6798695 DEU7MWJ KG Antifolate resistance:hsa01523; Folate biosynthesis:hsa00790 DEU7MWJ PD 1L9X DEU7MWJ SQ MASPGCLLCVLGLLLCGAASLELSRPHGDTAKKPIIGILMQKCRNKVMKNYGRYYIAASYVKYLESAGARVVPVRLDLTEKDYEILFKSINGILFPGGSVDLRRSDYAKVAKIFYNLSIQSFDDGDYFPVWGTCLGFEELSLLISGECLLTATDTVDVAMPLNFTGGQLHSRMFQNFPTELLLSLAVEPLTANFHKWSLSVKNFTMNEKLKKFFNVLTTNTDGKIEFISTMEGYKYPVYGVQWHPEKAPYEWKNLDGISHAPNAVKTAFYLAEFFVNEARKNNHHFKSESEEEKALIYQFSPIYTGNISSFQQCYIFD DEU7MWJ TD Primarily distributed in kidney and liver. DEU7MWJ FC This enzyme hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates and progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. It may play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates. DEU7MWJ KD 33208: Metazoa DEU7MWJ PL 7711: Chordata DEU7MWJ CL 40674: Mammalia DEU7MWJ OD 9443: Primates DEU7MWJ FM 9604: Hominidae DEU7MWJ GE 9605: Homo DEU7MWJ SP 9606: Homo sapiens DE9B45K ID DE9B45K DE9B45K DN Cytosolic branched aminotransferase (BCAT1) DE9B45K GN BCAT1 DE9B45K SN Cytosolic branched-chain-amino-acid aminotransferase; Protein ECA39; ECA39; BCAT(c); BCAT1; BCT1 DE9B45K UC BCAT1_HUMAN DE9B45K RD L-valine DE9B45K GI 586 DE9B45K E1 2: Transferase DE9B45K E2 2.6: Transaminase DE9B45K E3 2.6.1: Transaminase DE9B45K EC 2.6.1.42 DE9B45K RC Branched-chain amino acid catabolism:R-HSA-70895 DE9B45K KG 2-Oxocarboxylic acid metabolism:hsa01210; Biosynthesis of amino acids:hsa01230; Cysteine and methionine metabolism:hsa00270; Metabolic pathways:hsa01100; Pantothenate and CoA biosynthesis:hsa00770; Valine, leucine and isoleucine biosynthesis:hsa00290; Valine, leucine and isoleucine degradation:hsa00280 DE9B45K PD 2ABJ; 2COG; 2COI; 2COJ DE9B45K SQ MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS DE9B45K TD Primarily distributed in pancreas. DE9B45K FC This enzyme catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. DE9B45K KD 33208: Metazoa DE9B45K PL 7711: Chordata DE9B45K CL 40674: Mammalia DE9B45K OD 9443: Primates DE9B45K FM 9604: Hominidae DE9B45K GE 9605: Homo DE9B45K SP 9606: Homo sapiens DERA3OF ID DERA3OF DERA3OF DN Bile acid-CoA thioesterase (BAAT) DERA3OF GN BAAT DERA3OF SN Choloyl-CoA hydrolase; Glycine N-choloyltransferase; Bile acid-CoA:amino acid N-acyltransferase; Long-chain fatty-acyl-CoA hydrolase; BAAT; BACAT; BAT DERA3OF UC BAAT_HUMAN DERA3OF RD Obeticholic acid DERA3OF GI 570 DERA3OF E1 2: Transferase DERA3OF E2 2.3: Acyltransferase DERA3OF E3 2.3.1: Acyltransferase DERA3OF EC 2.3.1.65 DERA3OF RC Peroxisomal protein import:R-HSA-9033241; Recycling of bile acids and salts:R-HSA-159418; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DERA3OF KG Bile secretion:hsa04976; Biosynthesis of unsaturated fatty acids:hsa01040; Metabolic pathways:hsa01100; Peroxisome:hsa04146; Primary bile acid biosynthesis:hsa00120; Taurine and hypotaurine metabolism:hsa00430 DERA3OF SQ MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVASAPKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASLLASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFETTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGAGHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL DERA3OF TD Primarily distributed in liver, gallbladder mucosa and pancreas. DERA3OF FC This enzyme catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine. Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism. It may also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, it catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs. DERA3OF KD 33208: Metazoa DERA3OF PL 7711: Chordata DERA3OF CL 40674: Mammalia DERA3OF OD 9443: Primates DERA3OF FM 9604: Hominidae DERA3OF GE 9605: Homo DERA3OF SP 9606: Homo sapiens DEAXY04 ID DEAXY04 DEAXY04 DN Delta(24)-sterol reductase (DHCR24) DEAXY04 GN DHCR24 DEAXY04 SN Diminuto/dwarf1 homolog; 24-dehydrocholesterol reductase; 3-beta-hydroxysterol Delta-24-reductase; DHCR24; KIAA0018; Seladin-1 DEAXY04 UC DHC24_HUMAN DEAXY04 RD Desmosterol DEAXY04 GI 1718 DEAXY04 E1 1: Oxidoreductase DEAXY04 E2 1.3: CH-CH donor oxidoreductase DEAXY04 E3 1.3.1: NAD/NADP acceptor oxidoreductase DEAXY04 EC 1.3.1.72 DEAXY04 RC Cholesterol biosynthesis via desmosterol:R-HSA-6807047; Cholesterol biosynthesis via lathosterol:R-HSA-6807062 DEAXY04 KG Metabolic pathways:hsa01100; Steroid biosynthesis:hsa00100 DEAXY04 SQ MEPAVSLAVCALLFLLWVRLKGLEFVLIHQRWVFVCLFLLPLSLIFDIYYYVRAWVVFKLSSAPRLHEQRVRDIQKQVREWKEQGSKTFMCTGRPGWLTVSLRVGKYKKTHKNIMINLMDILEVDTKKQIVRVEPLVTMGQVTALLTSIGWTLPVLPELDDLTVGGLIMGTGIESSSHKYGLFQHICTAYELVLADGSFVRCTPSENSDLFYAVPWSCGTLGFLVAAEIRIIPAKKYVKLRFEPVRGLEAICAKFTHESQRQENHFVEGLLYSLDEAVIMTGVMTDEAEPSKLNSIGNYYKPWFFKHVENYLKTNREGLEYIPLRHYYHRHTRSIFWELQDIIPFGNNPIFRYLFGWMVPPKISLLKLTQGETLRKLYEQHHVVQDMLVPMKCLQQALHTFQNDIHVYPIWLCPFILPSQPGLVHPKGNEAELYIDIGAYGEPRVKHFEARSCMRQLEKFVRSVHGFQMLYADCYMNREEFWEMFDGSLYHKLREKLGCQDAFPEVYDKICKAARH DEAXY04 TD Primarily distributed in adrenal gland and liver. DEAXY04 FC This enzyme catalyzes the reduction of the delta-24 double bond of sterol intermediates during cholesterol biosynthesis. In addition to its cholesterol-synthesizing activity, it can protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress and protects against amyloid-beta peptide-induced apoptosis. DEAXY04 KD 33208: Metazoa DEAXY04 PL 7711: Chordata DEAXY04 CL 40674: Mammalia DEAXY04 OD 9443: Primates DEAXY04 FM 9604: Hominidae DEAXY04 GE 9605: Homo DEAXY04 SP 9606: Homo sapiens DEISPU8 ID DEISPU8 DEISPU8 DN Arachidonate 12-lipoxygenase (ALOX12B) DEISPU8 GN ALOX12B DEISPU8 SN Arachidonate 12-lipoxygenase 12R-type; Epidermis-type lipoxygenase 12; 12R-LOX; 12R-lipoxygenase; ALOX12B DEISPU8 UC LX12B_HUMAN DEISPU8 RD Arachidonic acid DEISPU8 GI 242 DEISPU8 E1 1: Oxidoreductase DEISPU8 E2 1.13: Oxygen single donor oxidoreductase DEISPU8 E3 1.13.11: Oxygen single donor oxidoreductase DEISPU8 EC 1.13.11.31 DEISPU8 RC Synthesis of 12-eicosatetraenoic acid derivatives:R-HSA-2142712 DEISPU8 KG Arachidonic acid metabolism:hsa00590; Metabolic pathways:hsa01100; Serotonergic synapse:hsa04726 DEISPU8 SQ MATYKVRVATGTDLLSGTRDSISLTIVGTQGESHKQLLNHFGRDFATGAVGQYTVQCPQDLGELIIIRLHKERYAFFPKDPWYCNYVQICAPNGRIYHFPAYQWMDGYETLALREATGKTTADDSLPVLLEHRKEEIRAKQDFYHWRVFLPGLPSYVHIPSYRPPVRRHRNPNRPEWNGYIPGFPILINFKATKFLNLNLRYSFLKTASFFVRLGPMALAFKVRGLLDCKHSWKRLKDIRKIFPGKKSVVSEYVAEHWAEDTFFGYQYLNGVNPGLIRRCTRIPDKFPVTDDMVAPFLGEGTCLQAELEKGNIYLADYRIMEGIPTVELSGRKQHHCAPLCLLHFGPEGKMMPIAIQLSQTPGPDCPIFLPSDSEWDWLLAKTWVRYAEFYSHEAIAHLLETHLIAEAFCLALLRNLPMCHPLYKLLIPHTRYTVQINSIGRAVLLNEGGLSAKGMSLGVEGFAGVMVRALSELTYDSLYLPNDFVERGVQDLPGYYYRDDSLAVWNALEKYVTEIITYYYPSDAAVEGDPELQSWVQEIFKECLLGRESSGFPRCLRTVPELIRYVTIVIYTCSAKHAAVNTGQMEFTAWMPNFPASMRNPPIQTKGLTTLETFMDTLPDVKTTCITLLVLWTLSREPDDRRPLGHFPDIHFVEEAPRRSIEAFRQRLNQISHDIRQRNKCLPIPYYYLDPVLIENSISI DEISPU8 TD Primarily distributed in skin and tongue. DEISPU8 FC This enzyme catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species. DEISPU8 KD 33208: Metazoa DEISPU8 PL 7711: Chordata DEISPU8 CL 40674: Mammalia DEISPU8 OD 9443: Primates DEISPU8 FM 9604: Hominidae DEISPU8 GE 9605: Homo DEISPU8 SP 9606: Homo sapiens DEFZWAX ID DEFZWAX DEFZWAX DN Uridine phosphorylase 1 (UPP1) DEFZWAX GN UPP1 DEFZWAX SN Pyrimidine nucleoside phosphorylase 1; Uridinephosphorylase 1; UrdPase 1; UPase 1; UPP1 DEFZWAX UC UPP1_HUMAN DEFZWAX RD Fluorouracilo DEFZWAX GI 7378 DEFZWAX E1 2: Transferase DEFZWAX E2 2.4: Glycosyltransferases DEFZWAX E3 2.4.2: Pentosyltransferase DEFZWAX EC 2.4.2.3 DEFZWAX RC Pyrimidine catabolism:R-HSA-73621; Pyrimidine salvage:R-HSA-73614 DEFZWAX KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DEFZWAX PD 3EUE; 3EUF; 3NBQ DEFZWAX SQ MAATGANAEKAESHNDCPVRLLNPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCPGRDYPNICAGTDRYAMYKVGPVLSVSHGMGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKKKLSKA DEFZWAX TD Low tissue/organ specificity. DEFZWAX FC This enzyme catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. DEFZWAX KD 33208: Metazoa DEFZWAX PL 7711: Chordata DEFZWAX CL 40674: Mammalia DEFZWAX OD 9443: Primates DEFZWAX FM 9604: Hominidae DEFZWAX GE 9605: Homo DEFZWAX SP 9606: Homo sapiens DECG04O ID DECG04O DECG04O DN Xanthine dehydrogenase/oxidase (XDH) DECG04O GN XDH DECG04O SN Xanthine dehydrogenase; Xanthine oxidase; Xanthine oxidoreductase; XD; XDH; XDHA; XO; XOR DECG04O UC XDH_HUMAN DECG04O RD Doxorubicin DECG04O GI 7498 DECG04O E1 1: Oxidoreductase DECG04O E2 1.17: CH/CH2 oxidoreductase DECG04O E3 1.17.1: NAD/NADP acceptor oxidoreductase DECG04O EC 1.17.1.4 DECG04O RC Butyrophilin (BTN) family interactions:R-HSA-8851680; Purine catabolism:R-HSA-74259 DECG04O KG Caffeine metabolism:hsa00232; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Peroxisome:hsa04146; Purine metabolism:hsa00230 DECG04O PD 2CKJ; 2E1Q DECG04O SQ MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDRLQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCCMNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQASTLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFGAACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISDLNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSAFKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKEELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLDPTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRYENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDKVTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDLKKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKMLGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGRHPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGRLCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKLEGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAASVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLGYSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAVGEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVTGVPENCKPWSVRV DECG04O TD Primarily distributed in intestine and liver. DECG04O FC This enzyme is a key enzyme in purine degradation. It catalyzes the oxidation of hypoxanthine to xanthine and catalyzes the oxidation of xanthine to uric acid. DECG04O KD 33208: Metazoa DECG04O PL 7711: Chordata DECG04O CL 40674: Mammalia DECG04O OD 9443: Primates DECG04O FM 9604: Hominidae DECG04O GE 9605: Homo DECG04O SP 9606: Homo sapiens DEI8NGH ID DEI8NGH DEI8NGH DN UDP-glucuronosyltransferase 2B10 (UGT2B10) DEI8NGH GN UGT2B10 DEI8NGH SN UDP-glucuronosyltransferase family 2 member B10; UDPGT 2B10; UGT2B10; OMIM: 600070; MGI: 2140962; HomoloGene: 117389; GeneCards: UGT2B10 DEI8NGH UC UDB10_HUMAN DEI8NGH RD Desloratadine DEI8NGH GI 7365 DEI8NGH E1 2: Transferase DEI8NGH E2 2.4: Glycosyltransferases DEI8NGH E3 2.4.1: Hexosyltransferase DEI8NGH EC 2.4.1.17 DEI8NGH RC Glucuronidation:R-HSA-156588 DEI8NGH KG Ascorbate and aldarate metabolism:hsa00053; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DEI8NGH SQ MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSASILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAINDIIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFERHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLGRPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMSSTDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD DEI8NGH TD Primarily distributed in liver. DEI8NGH FC This enzyme is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. DEI8NGH KD 33208: Metazoa DEI8NGH PL 7711: Chordata DEI8NGH CL 40674: Mammalia DEI8NGH OD 9443: Primates DEI8NGH FM 9604: Hominidae DEI8NGH GE 9605: Homo DEI8NGH SP 9606: Homo sapiens DETXQZ1 ID DETXQZ1 DETXQZ1 DN Serum paraoxonase/lactonase 3 (PON3) DETXQZ1 GN PON3 DETXQZ1 SN Paraoxonase III; Paraoxonase 3; PON3; OMIM: 602720; MGI: 106686; HomoloGene: 37371; GeneCards: PON3 DETXQZ1 UC PON3_HUMAN DETXQZ1 RD Lovastatin DETXQZ1 GI 5446 DETXQZ1 E1 3: Hydrolases DETXQZ1 E2 3.1: Ester bond hydrolase DETXQZ1 E3 3.1.1: Carboxylic ester hydrolase DETXQZ1 EC 3.1.1.2 DETXQZ1 RC Synthesis of 5-eicosatetraenoic acids:R-HSA-2142688 DETXQZ1 SQ MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPSGLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFIDKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYATRDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVAAKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPGSEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL DETXQZ1 TD Primarily distributed in liver. DETXQZ1 FC This enzyme has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. It rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin) and hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents. DETXQZ1 KD 33208: Metazoa DETXQZ1 PL 7711: Chordata DETXQZ1 CL 40674: Mammalia DETXQZ1 OD 9443: Primates DETXQZ1 FM 9604: Hominidae DETXQZ1 GE 9605: Homo DETXQZ1 SP 9606: Homo sapiens DEZV4AP ID DEZV4AP DEZV4AP DN RNA cytidine acetyltransferase (hALP) DEZV4AP GN NAT10 DEZV4AP SN N-acetyltransferase 10; N-acetyltransferase-like protein; 18S rRNA cytosine acetyltransferase; KIAA1709; NAT10 DEZV4AP UC NAT10_HUMAN DEZV4AP RD Allopurinol DEZV4AP GI 55226 DEZV4AP E1 2: Transferase DEZV4AP E2 2.3: Acyltransferase DEZV4AP E3 2.3.1: Acyltransferase DEZV4AP EC 2.3.1.5 DEZV4AP RC rRNA modification in the nucleus and cytosol:R-HSA-6790901 DEZV4AP KG Ribosome biogenesis in eukaryotes:hsa03008 DEZV4AP SQ MHRKKVDNRIRILIENGVAERQRSLFVVVGDRGKDQVVILHHMLSKATVKARPSVLWCYKKELGFSSHRKKRMRQLQKKIKNGTLNIKQDDPFELFIAATNIRYCYYNETHKILGNTFGMCVLQDFEALTPNLLARTVETVEGGGLVVILLRTMNSLKQLYTVTMDVHSRYRTEAHQDVVGRFNERFILSLASCKKCLVIDDQLNILPISSHVATMEALPPQTPDESLGPSDLELRELKESLQDTQPVGVLVDCCKTLDQAKAVLKFIEGISEKTLRSTVALTAARGRGKSAALGLAIAGAVAFGYSNIFVTSPSPDNLHTLFEFVFKGFDALQYQEHLDYEIIQSLNPEFNKAVIRVNVFREHRQTIQYIHPADAVKLGQAELVVIDEAAAIPLPLVKSLLGPYLVFMASTINGYEGTGRSLSLKLIQQLRQQSAQSQVSTTAENKTTTTARLASARTLYEVSLQESIRYAPGDAVEKWLNDLLCLDCLNITRIVSGCPLPEACELYYVNRDTLFCYHKASEVFLQRLMALYVASHYKNSPNDLQMLSDAPAHHLFCLLPPVPPTQNALPEVLAVIQVCLEGEISRQSILNSLSRGKKASGDLIPWTVSEQFQDPDFGGLSGGRVVRIAVHPDYQGMGYGSRALQLLQMYYEGRFPCLEEKVLETPQEIHTVSSEAVSLLEEVITPRKDLPPLLLKLNERPAERLDYLGVSYGLTPRLLKFWKRAGFVPVYLRQTPNDLTGEHSCIMLKTLTDEDEADQGGWLAAFWKDFRRRFLALLSYQFSTFSPSLALNIIQNRNMGKPAQPALSREELEALFLPYDLKRLEMYSRNMVDYHLIMDMIPAISRIYFLNQLGDLALSAAQSALLLGIGLQHKSVDQLEKEIELPSGQLMGLFNRIIRKVVKLFNEVQEKAIEEQMVAAKDVVMEPTMKTLSDDLDEAAKEFQEKHKKEVGKLKSMDLSEYIIRGDDEEWNEVLNKAGPNASIISLKSDKKRKLEAKQEPKQSKKLKNRETKNKKDMKLKRKK DEZV4AP TD Low tissue/organ specificity. DEZV4AP FC This enzyme catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs. It catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation. In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro. DEZV4AP KD 33208: Metazoa DEZV4AP PL 7711: Chordata DEZV4AP CL 40674: Mammalia DEZV4AP OD 9443: Primates DEZV4AP FM 9604: Hominidae DEZV4AP GE 9605: Homo DEZV4AP SP 9606: Homo sapiens DEVON3M ID DEVON3M DEVON3M DN Aldo-keto reductase 1D1 (AKR1D1) DEVON3M GN AKR1D1 DEVON3M SN Aldo-keto reductase family 1 member D1; Delta(4)-3-ketosteroid 5-beta-reductase; Delta(4)-3-oxosteroid 5-beta-reductase; SRD5B1; 3-oxo-5-beta-steroid 4-dehydrogenase; AKR1D1 DEVON3M UC AK1D1_HUMAN DEVON3M RD Norethindrone acetate DEVON3M GI 6718 DEVON3M E1 1: Oxidoreductase DEVON3M E2 1.3: CH-CH donor oxidoreductase DEVON3M E3 1.3.1: NAD/NADP acceptor oxidoreductase DEVON3M EC 1.3.1.3 DEVON3M RC Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DEVON3M KG Metabolic pathways:hsa01100; Primary bile acid biosynthesis:hsa00120; Steroid hormone biosynthesis:hsa00140 DEVON3M PD 3BV7; 3CAQ; 3CAS; 3CAV; 3CMF; 3COT; 3DOP; 3G1R; 3UZW DEVON3M SQ MDLSAASHRIPLSDGNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLKDALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEYPFHDEY DEVON3M TD Primarily distributed in liver. Also expressed in testis and weakly in colon. DEVON3M FC This enzyme catalyzes the stereospecific NADPH-dependent reduction of the C4-C5 double bond of bile acid intermediates and steroid hormones carrying a delta(4)-3-one structure to yield an A/B cis-ring junction. This cis-configuration plays important roles in steroid metabolism. It is also capable of reducing a broad range of delta-(4)-3-ketosteroids from C18 (such as, 17beta- hydroxyestr-4-en-3-one) to C27 (such as, 7alpha-hydroxycholest-4-en-3-one). DEVON3M KD 33208: Metazoa DEVON3M PL 7711: Chordata DEVON3M CL 40674: Mammalia DEVON3M OD 9443: Primates DEVON3M FM 9604: Hominidae DEVON3M GE 9605: Homo DEVON3M SP 9606: Homo sapiens DEFQ8VO ID DEFQ8VO DEFQ8VO DN Thiopurine methyltransferase (TPMT) DEFQ8VO GN TPMT DEFQ8VO SN Thiopurine S-methyltransferase; Thiopurine-methyl transferase; Thiopurinemethyltransferase; TPMT DEFQ8VO UC TPMT_HUMAN DEFQ8VO RD Methotrexate DEFQ8VO GI 7172 DEFQ8VO E1 2: Transferase DEFQ8VO E2 2.1: Methylase DEFQ8VO E3 2.1.1: Methyltransferase DEFQ8VO EC 2.1.1.67 DEFQ8VO RC Defective TPMT causes Thiopurine S-methyltransferase deficiency (TPMT deficiency):R-HSA-5578995; Methylation:R-HSA-156581 DEFQ8VO KG Drug metabolism - other enzymes:hsa00983 DEFQ8VO PD 2BZG; 2H11 DEFQ8VO SQ MDGTRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGKSGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKVFKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQYLLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLYLLTEK DEFQ8VO TD Primarily distributed in thyroid. DEFQ8VO FC This enzyme catalyzes the S-methylation of thiopurine drugs such as 6- mercaptopurine (also called mercaptopurine, 6-MP or its brand name Purinethol) and 6-thioguanine (also called tioguanine or 6-TG) using S- adenosyl-L-methionine as the methyl donor. TPMT activity modulates the cytotoxic effects of thiopurine prodrugs. A natural substrate for this enzyme has yet to be identified. DEFQ8VO KD 33208: Metazoa DEFQ8VO PL 7711: Chordata DEFQ8VO CL 40674: Mammalia DEFQ8VO OD 9443: Primates DEFQ8VO FM 9604: Hominidae DEFQ8VO GE 9605: Homo DEFQ8VO SP 9606: Homo sapiens DE741FI ID DE741FI DE741FI DN NADH-ubiquinone oxidoreductase 30 kDa (NDUFS3) DE741FI GN NDUFS3 DE741FI SN NADH-ubiquinone oxidoreductase 30 kDa subunit; Mitochondrial NADH dehydrogenase [ubiquinone] iron-sulfur protein 3; Complex I-30kD; CI-30kD; NDUFS3 DE741FI UC NDUS3_HUMAN DE741FI RD Doxorubicin DE741FI GI 4722 DE741FI E1 7: Translocase DE741FI E2 7.1: Hydron translocase DE741FI E3 7.1.1: Hydron translocase DE741FI EC 7.1.1.2 DE741FI RC Complex I biogenesis:R-HSA-6799198; Respiratory electron transport:R-HSA-611105 DE741FI KG Alzheimer's disease:hsa05010; Huntington's disease:hsa05016; Metabolic pathways:hsa01100; Non-alcoholic fatty liver disease (NAFLD):hsa04932; Oxidative phosphorylation:hsa00190; Parkinson's disease:hsa05012; Retrograde endocannabinoid signaling:hsa04723; Thermogenesis:hsa04714 DE741FI PD 5XTB; 5XTD; 5XTH; 5XTI DE741FI SQ MAAAAVARLWWRGILGASALTRGTGRPSVLLLPVRRESAGADTRPTVRPRNDVAHKQLSAFGEYVAEILPKYVQQVQVSCFNELEVCIHPDGVIPVLTFLRDHTNAQFKSLVDLTAVDVPTRQNRFEIVYNLLSLRFNSRIRVKTYTDELTPIESAVSVFKAANWYEREIWDMFGVFFANHPDLRRILTDYGFEGHPFRKDFPLSGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWEAFPVYRQPPESLKLEAGDKKPDAK DE741FI TD Primarily distributed in skeletal. DE741FI FC This enzyme is the core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I).Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. DE741FI KD 33208: Metazoa DE741FI PL 7711: Chordata DE741FI CL 40674: Mammalia DE741FI OD 9443: Primates DE741FI FM 9604: Hominidae DE741FI GE 9605: Homo DE741FI SP 9606: Homo sapiens DESYL1F ID DESYL1F DESYL1F DN Glutamate-cysteine ligase catalytic (GCLC) DESYL1F GN GCLC DESYL1F SN Gamma-glutamylcysteine synthetase; Glutamate--cysteine ligase catalytic subunit; Gamma-ECS; GCLC; GCS heavy chain; GLCL; GLCLC DESYL1F UC GSH1_HUMAN DESYL1F RD L-glutamine DESYL1F GI 2729 DESYL1F E1 6: Ligase DESYL1F E2 6.3: Carbon-nitrogen ligase DESYL1F E3 6.3.2: Peptide synthase DESYL1F EC 6.3.2.2 DESYL1F RC Defective GCLC causes Hemolytic anemia due to gamma-glutamylcysteine synthetase deficiency (HAGGSD):R-HSA-5578999; Glutathione synthesis and recycling:R-HSA-174403 DESYL1F KG Cysteine and methionine metabolism:hsa00270; Ferroptosis:hsa04216; Glutathione metabolism:hsa00480; Metabolic pathways:hsa01100 DESYL1F SQ MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDHENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTVEANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAINKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDAMGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVISASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQEGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDIGWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVLQGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNSYLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYSLILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN DESYL1F TD Primarily distributed in liver. DESYL1F FC This enzyme is the first rate limiting enzyme of glutathione synthesis. The enzyme consists of two subunits, a heavy catalytic subunit and a light regulatory subunit. DESYL1F KD 33208: Metazoa DESYL1F PL 7711: Chordata DESYL1F CL 40674: Mammalia DESYL1F OD 9443: Primates DESYL1F FM 9604: Hominidae DESYL1F GE 9605: Homo DESYL1F SP 9606: Homo sapiens DESOEW1 ID DESOEW1 DESOEW1 DN Dihydrothymine dehydrogenase (DPYD) DESOEW1 GN DPYD DESOEW1 SN Dihydropyrimidine dehydrogenase [NADP(+)]; Dihydrouracil dehydrogenase; DHPDHase; DPD; DPYD DESOEW1 UC DPYD_HUMAN DESOEW1 RD Fluorouracilo DESOEW1 GI 1806 DESOEW1 E1 1: Oxidoreductase DESOEW1 E2 1.3: CH-CH donor oxidoreductase DESOEW1 E3 1.3.1: NAD/NADP acceptor oxidoreductase DESOEW1 EC 1.3.1.2 DESOEW1 RC Pyrimidine catabolism:R-HSA-73621 DESOEW1 KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Pantothenate and CoA biosynthesis:hsa00770; Pyrimidine metabolism:hsa00240; beta-Alanine metabolism:hsa00410 DESOEW1 SQ MAPVLSKDSADIESILALNPRTQTHATLCSTSAKKLDKKHWKRNPDKNCFNCEKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSIANKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQFATEVFKAMSIPQIRNPSLPPPEKMSEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNEMTLSTLKEKGYKAAFIGIGLPEPNKDAIFQGLTQDQGFYTSKDFLPLVAKGSKAGMCACHSPLPSIRGVVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEMELAKEEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWNEDEDQMVHLKADVVISAFGSVLSDPKVKEALSPIKFNRWGLPEVDPETMQTSEAWVFAGGDVVGLANTTVESVNDGKQASWYIHKYVQSQYGASVSAKPELPLFYTPIDLVDISVEMAGLKFINPFGLASATPATSTSMIRRAFEAGWGFALTKTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNKNDWTELAKKSEDSGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVQIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKSDGTPWPAVGIAKRTTYGGVSGTAIRPIALRAVTSIARALPGFPILATGGIDSAESGLQFLHSGASVLQVCSAIQNQDFTVIEDYCTGLKALLYLKSIEELQDWDGQSPATVSHQKGKPVPRIAELMDKKLPSFGPYLEQRKKIIAENKIRLKEQNVAFSPLKRNCFIPKRPIPTIKDVIGKALQYLGTFGELSNVEQVVAMIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTITDTCTGCTLCLSVCPIVDCIKMVSRTTPYEPKRGVPLSVNPVC DESOEW1 TD Primarily distributed in liver and peripheral blood mononuclear cells. DESOEW1 FC This enzyme is involved in pyrimidine base degradation. It catalyzes the reduction of uracil and thymine and also involved the degradation of the chemotherapeutic drug 5-fluorouracil. DESOEW1 KD 33208: Metazoa DESOEW1 PL 7711: Chordata DESOEW1 CL 40674: Mammalia DESOEW1 OD 9443: Primates DESOEW1 FM 9604: Hominidae DESOEW1 GE 9605: Homo DESOEW1 SP 9606: Homo sapiens DEWJYTE ID DEWJYTE DEWJYTE DN Uridine 5'-monophosphate synthase (UMPS) DEWJYTE GN UMPS DEWJYTE SN Orotate phosphoribosyltransferase; Orotidine 5'-phosphate decarboxylase; UMP synthase; OMPdecase; ODC; OK/SW-cl.21; OPRT; OPRTase; UMPS DEWJYTE UC UMPS_HUMAN DEWJYTE RD Fluorouracilo DEWJYTE GI 7372 DEWJYTE E1 4: Lyases DEWJYTE E2 4.1: Carbon-carbon lyase DEWJYTE E3 4.1.1: Carboxy-lyase DEWJYTE EC 4.1.1.23 DEWJYTE RC Pyrimidine biosynthesis:R-HSA-500753 DEWJYTE KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DEWJYTE PD 2QCD; 2QCE; 3BGG; 3L0N; 3MI2; 3MO7; 3MW7; 4HIB; 4HKP DEWJYTE SQ MAVARAALGPLVTGLYDVQAFKFGDFVLKSGLSSPIYIDLRGIVSRPRLLSQVADILFQTAQNAGISFDTVCGVPYTALPLATVICSTNQIPMLIRRKETKDYGTKRLVEGTINPGETCLIIEDVVTSGSSVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAHGIRLHSVCTLSKMLEILEQQKKVDAETVGRVKRFIQENVFVAANHNGSPLSIKEAPKELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSLARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLAKCHEFLIFEDRKFADIGNTVKKQYEGGIFKIASWADLVNAHVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGDYTRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQLEAGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEAAEMYRKAAWEAYLSRLGV DEWJYTE TD Low tissue/organ specificity. DEWJYTE FC This enzyme catalyzes the final two reactions of the de novo biosynthesis of UMP in mammalian cells by the sequential action of orotate phosphoribosyltransferase and orotidine 5'-monophosphate (OMP) decarboxylase. DEWJYTE KD 33208: Metazoa DEWJYTE PL 7711: Chordata DEWJYTE CL 40674: Mammalia DEWJYTE OD 9443: Primates DEWJYTE FM 9604: Hominidae DEWJYTE GE 9605: Homo DEWJYTE SP 9606: Homo sapiens DE20ETR ID DE20ETR DE20ETR DN Uracil phosphoribosyltransferase (UPRT) DE20ETR GN UPRT DE20ETR SN Uracil phospho-ribosyl-transferase; Uracil phosphoribosyltransferase homolog; UPRT DE20ETR UC UPP_HUMAN DE20ETR RD Fluorouracilo DE20ETR GI 139596 DE20ETR E1 2: Transferase DE20ETR E2 2.4: Glycosyltransferases DE20ETR E3 2.4.2: Pentosyltransferase DE20ETR EC 2.4.2.9 DE20ETR KG Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DE20ETR SQ MATELQCPDSMPCHNQQVNSASTPSPEQLRPGDLILDHAGGNRASRAKVILLTGYAHSSLPAELDSGACGGSSLNSEGNSGSGDSSSYDAPAGNSFLEDCELSRQIGAQLKLLPMNDQIRELQTIIRDKTASRGDFMFSADRLIRLVVEEGLNQLPYKECMVTTPTGYKYEGVKFEKGNCGVSIMRSGEAMEQGLRDCCRSIRIGKILIQSDEETQRAKVYYAKFPPDIYRRKVLLMYPILSTGNTVIEAVKVLIEHGVQPSVIILLSLFSTPHGAKSIIQEFPEITILTTEVHPVAPTHFGQKYFGTD DE20ETR TD Primarily distributed in leukocytes, liver and spleen andthymus. Also expressed in brain, lung and skeletal muscle. DE20ETR FC This enzyme is an enzyme which creates UMP from uracil and phosphoribosylpyrophosphate. DE20ETR KD 33208: Metazoa DE20ETR PL 7711: Chordata DE20ETR CL 40674: Mammalia DE20ETR OD 9443: Primates DE20ETR FM 9604: Hominidae DE20ETR GE 9605: Homo DE20ETR SP 9606: Homo sapiens DEH49YS ID DEH49YS DEH49YS DN Glutathione S-transferase alpha-2 (GSTA2) DEH49YS GN GSTA2 DEH49YS SN Glutathione S-transferase A2; GST class-alpha member 2; GST-gamma; GST HA subunit 2; GST2; GSTA2; GSTA2-2; GTH2 DEH49YS UC GSTA2_HUMAN DEH49YS RD Azathioprine DEH49YS GI 2939 DEH49YS E1 2: Transferase DEH49YS E2 2.5: Alkyl/aryl transferase DEH49YS E3 2.5.1: Alkyl/aryl transferase DEH49YS EC 2.5.1.18 DEH49YS RC Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation:R-HSA-8950505; Glutathione conjugation:R-HSA-156590 DEH49YS KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DEH49YS PD 1AGS; 2VCT; 2WJU; 4ACS DEH49YS SQ MAEKPKLHYSNIRGRMESIRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKEKALIDMYIEGIADLGEMILLLPFSQPEEQDAKLALIQEKTKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEESRKIFRF DEH49YS TD Primarily distributed in kidney, liver and pancreas. DEH49YS FC This enzyme conjugates reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. DEH49YS KD 33208: Metazoa DEH49YS PL 7711: Chordata DEH49YS CL 40674: Mammalia DEH49YS OD 9443: Primates DEH49YS FM 9604: Hominidae DEH49YS GE 9605: Homo DEH49YS SP 9606: Homo sapiens DESTKG6 ID DESTKG6 DESTKG6 DN Sulfotransferase 1E1 (SULT1E1) DESTKG6 GN SULT1E1 DESTKG6 SN Sulfotransferase family cytosolic 1E member 1; Estrogen sulfotransferase; Estrogen-preferring sulfotransferase; EST-1; ST1E1; STE; SULT1E1 DESTKG6 UC ST1E1_HUMAN DESTKG6 RD Rotigotine DESTKG6 GI 6783 DESTKG6 E1 2: Transferase DESTKG6 E2 2.8: Sulfotransferase DESTKG6 E3 2.8.2: Sulfotransferase DESTKG6 EC 2.8.2.4 DESTKG6 RC Cytosolic sulfonation of small molecules:R-HSA-156584 DESTKG6 KG Steroid hormone biosynthesis:hsa00140 DESTKG6 PD 1G3M; 1HY3; 4JVL; 4JVM; 4JVN DESTKG6 SQ MNSELDYYEKFEEVHGILMYKDFVKYWDNVEAFQARPDDLVIATYPKSGTTWVSEIVYMIYKEGDVEKCKEDVIFNRIPFLECRKENLMNGVKQLDEMNSPRIVKTHLPPELLPASFWEKDCKIIYLCRNAKDVAVSFYYFFLMVAGHPNPGSFPEFVEKFMQGQVPYGSWYKHVKSWWEKGKSPRVLFLFYEDLKEDIRKEVIKLIHFLERKPSEELVDRIIHHTSFQEMKNNPSTNYTTLPDEIMNQKLSPFMRKGITGDWKNHFTVALNEKFDKHYEQQMKESTLKFRTEI DESTKG6 TD Primarily distributed in intestine, liver and vagina. DESTKG6 FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. The sulfation of estrogens leads to their inactivation. It also sulfates dehydroepiandrosterone (DHEA), pregnenolone, (24S)-hydroxycholesterol and xenobiotic compounds like ethinylestradiol, equalenin, diethyl stilbesterol and 1-naphthol at significantly lower efficency. DESTKG6 KD 33208: Metazoa DESTKG6 PL 7711: Chordata DESTKG6 CL 40674: Mammalia DESTKG6 OD 9443: Primates DESTKG6 FM 9604: Hominidae DESTKG6 GE 9605: Homo DESTKG6 SP 9606: Homo sapiens DE870HF ID DE870HF DE870HF DN Aminomuconic semialdehyde dehydrogenase (ALDH12) DE870HF GN ALDH8A1 DE870HF SN Aldehyde dehydrogenase family 8 member A1; Aldehyde dehydrogenase 12; 2-aminomuconic semialdehyde dehydrogenase; ALDH12; ALDH8A1 DE870HF UC AL8A1_HUMAN DE870HF RD SC-47945 DE870HF GI 64577 DE870HF E1 1: Oxidoreductase DE870HF E2 1.2: Aldehyde/oxo donor oxidoreductase DE870HF E3 1.2.1: NAD/NADP acceptor oxidoreductase DE870HF EC 1.2.1.3 DE870HF RC RA biosynthesis pathway:R-HSA-5365859 DE870HF KG Metabolic pathways:hsa01100; Tryptophan metabolism:hsa00380 DE870HF SQ MAGTNALLMLENFIDGKFLPCSSYIDSYDPSTGEVYCRVPNSGKDEIEAAVKAAREAFPSWSSRSPQERSRVLNQVADLLEQSLEEFAQAESKDQGKTLALARTMDIPRSVQNFRFFASSSLHHTSECTQMDHLGCMHYTVRAPVGVAGLISPWNLPLYLLTWKIAPAMAAGNTVIAKPSELTSVTAWMLCKLLDKAGVPPGVVNIVFGTGPRVGEALVSHPEVPLISFTGSQPTAERITQLSAPHCKKLSLELGGKNPAIIFEDANLDECIPATVRSSFANQGEICLCTSRIFVQKSIYSEFLKRFVEATRKWKVGIPSDPLVSIGALISKAHLEKVRSYVKRALAEGAQIWCGEGVDKLSLPARNQAGYFMLPTVITDIKDESCCMTEEIFGPVTCVVPFDSEEEVIERANNVKYGLAATVWSSNVGRVHRVAKKLQSGLVWTNCWLIRELNLPFGGMKSSGIGREGAKDSYDFFTEIKTITVKH DE870HF TD Primarily distributed in kidney and liver. DE870HF FC This enzyme catalyzes the NAD-dependent oxidation of 2-aminomuconic semialdehyde of the kynurenine metabolic pathway in L-tryptophan degradation. DE870HF KD 33208: Metazoa DE870HF PL 7711: Chordata DE870HF CL 40674: Mammalia DE870HF OD 9443: Primates DE870HF FM 9604: Hominidae DE870HF GE 9605: Homo DE870HF SP 9606: Homo sapiens DENUPDX ID DENUPDX DENUPDX DN UDP-glucuronosyltransferase 2B4 (UGT2B4) DENUPDX GN UGT2B4 DENUPDX SN UDP-glucuronosyltransferase family 2 member B4; Hyodeoxycholic acid-specific UDPGT; UDPGT 2B4; UDPGTh-1; UGT2B4 DENUPDX UC UD2B4_HUMAN DENUPDX RD Labetalol DENUPDX GI 7363 DENUPDX E1 2: Transferase DENUPDX E2 2.4: Glycosyltransferases DENUPDX E3 2.4.1: Hexosyltransferase DENUPDX EC 2.4.1.17 DENUPDX RC Glucuronidation:R-HSA-156588 DENUPDX KG Ascorbate and aldarate metabolism:hsa00053; Bile secretion:hsa04976; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860; Retinol metabolism:hsa00830; Steroid hormone biosynthesis:hsa00140 DENUPDX SQ MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSASISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFNDILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAIEKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVLGRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTMSSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD DENUPDX TD Primarily distributed in liver. DENUPDX FC This enzyme is active on polyhydroxylated estrogens (such as estriol, 4-hydroxyestrone and 2-hydroxyestriol) and xenobiotics (such as 4-methylumbelliferone, 1-naphthol, 4-nitrophenol, 2-aminophenol, 4-hydroxybiphenyl and menthol). It is also capable of 6 alpha- hydroxyglucuronidation of hyodeoxycholic acid. DENUPDX KD 33208: Metazoa DENUPDX PL 7711: Chordata DENUPDX CL 40674: Mammalia DENUPDX OD 9443: Primates DENUPDX FM 9604: Hominidae DENUPDX GE 9605: Homo DENUPDX SP 9606: Homo sapiens DEUM1EX ID DEUM1EX DEUM1EX DN Oleamide hydrolase 1 (FAAH) DEUM1EX GN FAAH DEUM1EX SN Anandamide amidohydrolase 1; Fatty-acid amide hydrolase 1; FAAH; FAAH1 DEUM1EX UC FAAH1_HUMAN DEUM1EX RD Propofol DEUM1EX GI 2166 DEUM1EX E1 3: Hydrolases DEUM1EX E2 3.5: Carbon-nitrogen hydrolase DEUM1EX E3 3.5.1: Linear amide hydrolase DEUM1EX EC 3.5.1.99 DEUM1EX RC Arachidonic acid metabolism:R-HSA-2142753 DEUM1EX KG Retrograde endocannabinoid signaling:hsa04723 DEUM1EX SQ MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYTSSQPLRVGYYETDNYTMPSPAMRRAVLETKQSLEAAGHTLVPFLPSNIPHALETLSTGGLFSDGGHTFLQNFKGDFVDPCLGDLVSILKLPQWLKGLLAFLVKPLLPRLSAFLSNMKSRSAGKLWELQHEIEVYRKTVIAQWRALDLDVVLTPMLAPALDLNAPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDEAQMEHYRGYFGDIWDKMLQKGMKKSVGLPVAVQCVALPWQEELCLRFMREVERLMTPEKQSS DEUM1EX TD Primarily distributed in brain, small intestine, pancreas, skeletal muscle and testis. Also expressed in kidney, liver, lung, placenta and prostate. DEUM1EX FC This enzyme degrades bioactive fatty acid amides like oleamide, the endogenous cannabinoid, anandamide and myristic amide to their corresponding acids. It also hydrolyzes polyunsaturated substrate anandamide preferentially as compared to monounsaturated substrates. DEUM1EX KD 33208: Metazoa DEUM1EX PL 7711: Chordata DEUM1EX CL 40674: Mammalia DEUM1EX OD 9443: Primates DEUM1EX FM 9604: Hominidae DEUM1EX GE 9605: Homo DEUM1EX SP 9606: Homo sapiens DEKX5CD ID DEKX5CD DEKX5CD DN NADH-ubiquinone oxidoreductase 49 kDa (NDUFS2) DEKX5CD GN NDUFS2 DEKX5CD SN NADH-ubiquinone oxidoreductase 49 kDa subunit; Mitochondrial NADH dehydrogenase [ubiquinone] iron-sulfur protein 2; Complex I-49kD; CI-49kD; NDUFS2 DEKX5CD UC NDUS2_HUMAN DEKX5CD RD Doxorubicin DEKX5CD GI 4720 DEKX5CD E1 7: Translocase DEKX5CD E2 7.1: Hydron translocase DEKX5CD E3 7.1.1: Hydron translocase DEKX5CD EC 7.1.1.2 DEKX5CD RC Complex I biogenesis:R-HSA-6799198; Respiratory electron transport:R-HSA-611105 DEKX5CD KG Alzheimer's disease:hsa05010; Huntington's disease:hsa05016; Metabolic pathways:hsa01100; Non-alcoholic fatty liver disease (NAFLD):hsa04932; Oxidative phosphorylation:hsa00190; Parkinson's disease:hsa05012; Retrograde endocannabinoid signaling:hsa04723; Thermogenesis:hsa04714 DEKX5CD PD 5XTB; 5XTC; 5XTD; 5XTH; 5XTI DEKX5CD SQ MAALRALCGFRGVAAQVLRPGAGVRLPIQPSRGVRQWQPDVEWAQQFGGAVMYPSKETAHWKPPPWNDVDPPKDTIVKNITLNFGPQHPAAHGVLRLVMELSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQAYSLAVEKLLNIRPPPRAQWIRVLFGEITRLLNHIMAVTTHALDLGAMTPFFWLFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGLMDDIYQFSKNFSLRLDELEELLTNNRIWRNRTIDIGVVTAEEALNYGFSGVMLRGSGIQWDLRKTQPYDVYDQVEFDVPVGSRGDCYDRYLCRVEEMRQSLRIIAQCLNKMPPGEIKVDDAKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAIEAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSKGHMLADVVAIIGTQDIVFGEVDR DEKX5CD TD Primarily distributed in skeletal. DEKX5CD FC This enzyme is the core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I).Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. DEKX5CD KD 33208: Metazoa DEKX5CD PL 7711: Chordata DEKX5CD CL 40674: Mammalia DEKX5CD OD 9443: Primates DEKX5CD FM 9604: Hominidae DEKX5CD GE 9605: Homo DEKX5CD SP 9606: Homo sapiens DE6SOC5 ID DE6SOC5 DE6SOC5 DN Copper amine oxidase (AOC3) DE6SOC5 GN AOC3 DE6SOC5 SN Vascular adhesion protein 1; Membrane primary amine oxidase; AOC3; HPAO; VAP-1; VAP1 DE6SOC5 UC AOC3_HUMAN DE6SOC5 RD LF-08-0299 DE6SOC5 GI 8639 DE6SOC5 E1 1: Oxidoreductase DE6SOC5 E2 1.4: CH-NH2 donor oxidoreductase DE6SOC5 E3 1.4.3: Oxygen acceptor oxidoreductase DE6SOC5 EC 1.4.3.21 DE6SOC5 RC Phase I - Functionalization of compounds:R-HSA-211945 DE6SOC5 KG Glycine, serine and threonine metabolism:hsa00260; Metabolic pathways:hsa01100; Phenylalanine metabolism:hsa00360; Tyrosine metabolism:hsa00350; beta-Alanine metabolism:hsa00410 DE6SOC5 PD 1PU4; 1US1; 2C10; 2Y73; 2Y74; 3ALA; 4BTW; 4BTX; 4BTY DE6SOC5 SQ MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPPAREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDIDQMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFLHHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSWSLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLVYEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQAPKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFHPSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVWAEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHPRGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDFSDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSADSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN DE6SOC5 TD Primarily distributed in peripheral lymph node, hepatic endothelia, appendix, lung and small intestine. DE6SOC5 FC This enzyme has semicarbazide-sensitive (SSAO) monoamine oxidase activity. DE6SOC5 KD 33208: Metazoa DE6SOC5 PL 7711: Chordata DE6SOC5 CL 40674: Mammalia DE6SOC5 OD 9443: Primates DE6SOC5 FM 9604: Hominidae DE6SOC5 GE 9605: Homo DE6SOC5 SP 9606: Homo sapiens DEU3DHN ID DEU3DHN DEU3DHN DN Sulfotransferase 1C4 (SULT1C4) DEU3DHN GN SULT1C4 DEU3DHN SN Sulfotransferase family cytosolic 1C member 4; humSULTC4; ST1C4; SULT1C#2; SULT1C4 DEU3DHN UC ST1C4_HUMAN DEU3DHN RD Rotigotine DEU3DHN GI 27233 DEU3DHN E1 2: Transferase DEU3DHN E2 2.8: Sulfotransferase DEU3DHN E3 2.8.2: Sulfotransferase DEU3DHN EC 2.8.2.1 DEU3DHN RC Cytosolic sulfonation of small molecules:R-HSA-156584 DEU3DHN PD 2AD1; 2GWH DEU3DHN SQ MALHDMEDFTFDGTKRLSVNYVKGILQPTDTCDIWDKIWNFQAKPDDLLISTYPKAGTTWTQEIVELIQNEGDVEKSKRAPTHQRFPFLEMKIPSLGSGLEQAHAMPSPRILKTHLPFHLLPPSLLEKNCKIIYVARNPKDNMVSYYHFQRMNKALPAPGTWEEYFETFLAGKVCWGSWHEHVKGWWEAKDKHRILYLFYEDMKKNPKHEIQKLAEFIGKKLDDKVLDKIVHYTSFDVMKQNPMANYSSIPAEIMDHSISPFMRKGAVGDWKKHFTVAQNERFDEDYKKKMTDTRLTFHFQF DEU3DHN TD Primarily distributed in fetal lung and kidney. Also expressed in fetal heart, adult kidney, ovary and spinal chord. DEU3DHN FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. It is also involved in the activation of carcinogenic hydroxylamines. It has activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). DEU3DHN KD 33208: Metazoa DEU3DHN PL 7711: Chordata DEU3DHN CL 40674: Mammalia DEU3DHN OD 9443: Primates DEU3DHN FM 9604: Hominidae DEU3DHN GE 9605: Homo DEU3DHN SP 9606: Homo sapiens DE7PT32 ID DE7PT32 DE7PT32 DN Alanyl aminopeptidase (ANPEP) DE7PT32 GN ANPEP DE7PT32 SN Aminopeptidase M; Aminopeptidase N; CD13; Microsomal aminopeptidase; Myeloid plasma membrane glycoprotein CD13; ANPEP; AP-M; AP-N; APN; PEPN; gp150; hAPN DE7PT32 UC AMPN_HUMAN DE7PT32 RD Human calcitonin DE7PT32 GI 290 DE7PT32 E1 3: Hydrolases DE7PT32 E2 3.4: Peptidase DE7PT32 E3 3.4.11: Aminopeptidase DE7PT32 EC 3.4.11.2 DE7PT32 RC Metabolism of Angiotensinogen to Angiotensins:R-HSA-2022377; Neutrophil degranulation:R-HSA-6798695 DE7PT32 KG Glutathione metabolism:hsa00480; Hematopoietic cell lineage:hsa04640; Metabolic pathways:hsa01100; Renin-angiotensin system:hsa04614 DE7PT32 PD 4FYQ; 4FYR; 4FYS; 4FYT; 5LHD; 6ATK; 6U7E; 6U7F; 6U7G DE7PT32 SQ MAKGFYISKSLGILGILLGVAAVCTIIALSVVYSQEKNKNANSSPVASTTPSASATTNPASATTLDQSKAWNRYRLPNTLKPDSYRVTLRPYLTPNDRGLYVFKGSSTVRFTCKEATDVIIIHSKKLNYTLSQGHRVVLRGVGGSQPPDIDKTELVEPTEYLVVHLKGSLVKDSQYEMDSEFEGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKAEFNITLIHPKDLTALSNMLPKGPSTPLPEDPNWNVTEFHTTPKMSTYLLAFIVSEFDYVEKQASNGVLIRIWARPSAIAAGHGDYALNVTGPILNFFAGHYDTPYPLPKSDQIGLPDFNAGAMENWGLVTYRENSLLFDPLSSSSSNKERVVTVIAHELAHQWFGNLVTIEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLMVLNDVYRVMAVDALASSHPLSTPASEINTPAQISELFDAISYSKGASVLRMLSSFLSEDVFKQGLASYLHTFAYQNTIYLNLWDHLQEAVNNRSIQLPTTVRDIMNRWTLQMGFPVITVDTSTGTLSQEHFLLDPDSNVTRPSEFNYVWIVPITSIRDGRQQQDYWLIDVRAQNDLFSTSGNEWVLLNLNVTGYYRVNYDEENWRKIQTQLQRDHSAIPVINRAQIINDAFNLASAHKVPVTLALNNTLFLIEERQYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLKKQVTPLFIHFRNNTNNWREIPENLMDQYSEVNAISTACSNGVPECEEMVSGLFKQWMENPNNNPIHPNLRSTVYCNAIAQGGEEEWDFAWEQFRNATLVNEADKLRAALACSKELWILNRYLSYTLNPDLIRKQDATSTIISITNNVIGQGLVWDFVQSNWKKLFNDYGGGSFSFSNLIQAVTRRFSTEYELQQLEQFKKDNEETGFGSGTRALEQALEKTKANIKWVKENKEVVLQWFTENSK DE7PT32 TD Primarily distributed in intestine, kidney and pancreas. DE7PT32 FC This enzyme plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. DE7PT32 KD 33208: Metazoa DE7PT32 PL 7711: Chordata DE7PT32 CL 40674: Mammalia DE7PT32 OD 9443: Primates DE7PT32 FM 9604: Hominidae DE7PT32 GE 9605: Homo DE7PT32 SP 9606: Homo sapiens DE6AY40 ID DE6AY40 DE6AY40 DN N-acetyl-beta-glucosaminidase beta (HEXB) DE6AY40 GN HEXB DE6AY40 SN Beta-N-acetylhexosaminidase subunit beta; Beta-hexosaminidase subunit beta; Beta-hexosaminidase subunit beta chain A; Beta-hexosaminidase subunit beta chain B; Cervical cancer proto-oncogene 7 protein; Hexosaminidase subunit B; N-acetyl-beta-glucosaminidase subunit beta; HCC-7; HCC7; HEXB DE6AY40 UC HEXB_HUMAN DE6AY40 RD Chondroitin sulfate DE6AY40 GI 3074 DE6AY40 E1 3: Hydrolases DE6AY40 E2 3.2: Glycosylase DE6AY40 E3 3.2.1: O/S-glycosyl compound glycosidase DE6AY40 EC 3.2.1.52 DE6AY40 RC CS/DS degradation:R-HSA-2024101; Defective HEXB causes GM2G2:R-HSA-3656248; Glycosphingolipid metabolism:R-HSA-1660662; Hyaluronan uptake and degradation:R-HSA-2160916; Keratan sulfate degradation:R-HSA-2022857; Neutrophil degranulation:R-HSA-6798695 DE6AY40 KG Amino sugar and nucleotide sugar metabolism:hsa00520; Glycosaminoglycan degradation:hsa00531; Glycosphingolipid biosynthesis - ganglio series:hsa00604; Glycosphingolipid biosynthesis - globo series:hsa00603; Lysosome:hsa04142; Metabolic pathways:hsa01100; Other glycan degradation:hsa00511; Various types of N-glycan biosynthesis:hsa00513 DE6AY40 PD 1NOU; 1NOW; 1NP0; 1O7A; 1QBD; 2GJX; 2GK1; 3LMY; 5BRO DE6AY40 SQ MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLSVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFGPINPTLNTTYSFLTTFFKEISEVFPDQFIHLGGDEVEFKCWESNPKIQDFMRQKGFGTDFKKLESFYIQKVLDIIATINKGSIVWQEVFDDKAKLAPGTIVEVWKDSAYPEELSRVTASGFPVILSAPWYLDLISYGQDWRKYYKVEPLDFGGTQKQKQLFIGGEACLWGEYVDATNLTPRLWPRASAVGERLWSSKDVRDMDDAYDRLTRHRCRMVERGIAAQPLYAGYCNHENM DE6AY40 TD Primarily distributed in placenta. DE6AY40 FC This enzyme is responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues. DE6AY40 KD 33208: Metazoa DE6AY40 PL 7711: Chordata DE6AY40 CL 40674: Mammalia DE6AY40 OD 9443: Primates DE6AY40 FM 9604: Hominidae DE6AY40 GE 9605: Homo DE6AY40 SP 9606: Homo sapiens DE9A2LB ID DE9A2LB DE9A2LB DN Microsomal cytochrome MCB5 (CYB5A) DE9A2LB GN CYB5A DE9A2LB SN Microsomal cytochrome b5 type A; Cytochrome b5; MCB5; CYB5; CYB5A DE9A2LB UC CYB5_HUMAN DE9A2LB RD Halothane DE9A2LB GI 1528 DE9A2LB E1 1: Oxidoreductase DE9A2LB E2 1.14: Oxygen paired donor oxidoreductase DE9A2LB E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE9A2LB EC 1.14.14.1 DE9A2LB RC Insertion of tail-anchored proteins into the endoplasmic reticulum membrane [P00167-1]:R-HSA-9609523; Vitamin C (ascorbate) metabolism:R-HSA-196836 DE9A2LB PD 2I96 DE9A2LB SQ MAEQSDEAVKYYTLEEIQKHNHSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDAREMSKTFIIGELHPDDRPKLNKPPETLITTIDSSSSWWTNWVIPAISAVAVALMYRLYMAED DE9A2LB TD Primarily distributed in liver. DE9A2LB FC This enzyme functions as an electron carrier for several membrane-bound oxygenases. DE9A2LB KD 33208: Metazoa DE9A2LB PL 7711: Chordata DE9A2LB CL 40674: Mammalia DE9A2LB OD 9443: Primates DE9A2LB FM 9604: Hominidae DE9A2LB GE 9605: Homo DE9A2LB SP 9606: Homo sapiens DE3OP9S ID DE3OP9S DE3OP9S DN Galactose kinase (GALK1) DE3OP9S GN GALK1 DE3OP9S SN Galactokinase; ATP:D-galactose-1-phosphotransferase; BiGalK; GALK; GALK1; CLB.507001.110; CLB.510667.120 DE3OP9S UC GALK1_HUMAN DE3OP9S RD CERC-801 DE3OP9S GI 2584 DE3OP9S E1 2: Transferase DE3OP9S E2 2.7: Kinase DE3OP9S E3 2.7.1: Phosphotransferase DE3OP9S EC 2.7.1.6 DE3OP9S RC Defective GALK1 can cause Galactosemia II (GALCT2):R-HSA-5609976; Galactose catabolism:R-HSA-70370 DE3OP9S KG Amino sugar and nucleotide sugar metabolism:hsa00520; Galactose metabolism:hsa00052; Metabolic pathways:hsa01100 DE3OP9S PD 1WUU; 1YH7; 6GR2; 6Q3W; 6Q8Z; 6Q90; 6Q91; 6QJE DE3OP9S SQ MAALRQPQVAELLAEARRAFREEFGAEPELAVSAPGRVNLIGEHTDYNQGLVLPMALELMTVLVGSPRKDGLVSLLTTSEGADEPQRLQFPLPTAQRSLEPGTPRWANYVKGVIQYYPAAPLPGFSAVVVSSVPLGGGLSSSASLEVATYTFLQQLCPDSGTIAARAQVCQQAEHSFAGMPCGIMDQFISLMGQKGHALLIDCRSLETSLVPLSDPKLAVLITNSNVRHSLASSEYPVRRRQCEEVARALGKESLREVQLEELEAARDLVSKEGFRRARHVVGEIRRTAQAAAALRRGDYRAFGRLMVESHRSLRDDYEVSCPELDQLVEAALAVPGVYGSRMTGGGFGGCTVTLLEASAAPHAMRHIQEHYGGTATFYLSQAADGAKVLCL DE3OP9S TD Primarily distributed in blood. DE3OP9S FC This enzyme is important for galactose metabolism. DE3OP9S KD 33208: Metazoa DE3OP9S PL 7711: Chordata DE3OP9S CL 40674: Mammalia DE3OP9S OD 9443: Primates DE3OP9S FM 9604: Hominidae DE3OP9S GE 9605: Homo DE3OP9S SP 9606: Homo sapiens DERWDYE ID DERWDYE DERWDYE DN Transglutaminase Z (TGM7) DERWDYE GN TGM7 DERWDYE SN Protein-glutamine gamma-glutamyltransferase Z; Transglutaminase-7; Protein-glutamine gamma-glutamyltransferase 7; TGase Z; TGase-7; TG(Z); TGM7; TGZ DERWDYE UC TGM7_HUMAN DERWDYE RD L-glutamine DERWDYE GI 116179 DERWDYE E1 2: Transferase DERWDYE E2 2.3: Acyltransferase DERWDYE E3 2.3.2: Aminoacyltransferase DERWDYE EC 2.3.2.13 DERWDYE SQ MDQVATLRLESVDLQSSRNNKEHHTQEMGVKRLTVRRGQPFYLRLSFSRPFQSQNDHITFVAETGPKPSELLGTRATFFLTRVQPGNVWSASDFTIDSNSLQVSLFTPANAVIGHYTLKIEISQGQGHSVTYPLGTFILLFNPWSPEDDVYLPSEILLQEYIMRDYGFVYKGHERFITSWPWNYGQFEEDIIDICFEILNKSLYHLKNPAKDCSQRNDVVYVCRVVSAMINSNDDNGVLQGNWGEDYSKGVSPLEWKGSVAILQQWSARGGQPVKYGQCWVFASVMCTVMRCLGVPTRVVSNFRSAHNVDRNLTIDTYYDRNAEMLSTQKRDKIWNFHVWNECWMIRKDLPPGYNGWQVLDPTPQQTSSGLFCCGPASVKAIREGDVHLAYDTPFVYAEVNADEVIWLLGDGQAQEILAHNTSSIGKEISTKMVGSDQRQSITSSYKYPEGSPEERAVFMKASRKMLGPQRASLPFLDLLESGGLRDQPAQLQLHLARIPEWGQDLQLLLRIQRVPDSTHPRGPIGLVVRFCAQALLHGGGTQKPFWRHTVRMNLDFGKETQWPLLLPYSNYRNKLTDEKLIRVSGIAEVEETGRSMLVLKDICLEPPHLSIEVSERAEVGKALRVHVTLTNTLMVALSSCTMVLEGSGLINGQIAKDLGTLVAGHTLQIQLDLYPTKAGPRQLQVLISSNEVKEIKGYKDIFVTVAGAP DERWDYE TD Primarily distributed in lymphoid tissue and testis. DERWDYE FC This enzyme catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. DERWDYE KD 33208: Metazoa DERWDYE PL 7711: Chordata DERWDYE CL 40674: Mammalia DERWDYE OD 9443: Primates DERWDYE FM 9604: Hominidae DERWDYE GE 9605: Homo DERWDYE SP 9606: Homo sapiens DER7TA0 ID DER7TA0 DER7TA0 DN N-acetyltransferase 2 (NAT2) DER7TA0 GN NAT2 DER7TA0 SN Arylamine N-acetyltransferase 2; N-acetyltransferase type 2; Arylamide acetylase 2; Polymorphic arylamine N-acetyltransferase; AAC2; NAT-2; NAT2; PNAT DER7TA0 UC ARY2_HUMAN DER7TA0 RD Amifampridine DER7TA0 GI 10 DER7TA0 E1 2: Transferase DER7TA0 E2 2.3: Acyltransferase DER7TA0 E3 2.3.1: Acyltransferase DER7TA0 EC 2.3.1.5 DER7TA0 RC Acetylation:R-HSA-156582 DER7TA0 KG Caffeine metabolism:hsa00232; Chemical carcinogenesis:hsa05204; Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100 DER7TA0 PD 2PFR DER7TA0 SQ MDIEAYFERIGYKNSRNKLDLETLTDILEHQIRAVPFENLNMHCGQAMELGLEAIFDHIVRRNRGGWCLQVNQLLYWALTTIGFQTTMLGGYFYIPPVNKYSTGMVHLLLQVTIDGRNYIVDAGSGSSSQMWQPLELISGKDQPQVPCIFCLTEERGIWYLDQIRREQYITNKEFLNSHLLPKKKHQKIYLFTLEPRTIEDFESMNTYLQTSPTSSFITTSFCSLQTPEGVYCLVGFILTYRKFNYKDNTDLVEFKTLTEEEVEEVLKNIFKISLGRNLVPKPGDGSLTI DER7TA0 TD Primarily distributed in intestine and liver. DER7TA0 FC This enzyme participates in the detoxification of a plethora of hydrazine and arylamine drugs. It catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens. DER7TA0 KD 33208: Metazoa DER7TA0 PL 7711: Chordata DER7TA0 CL 40674: Mammalia DER7TA0 OD 9443: Primates DER7TA0 FM 9604: Hominidae DER7TA0 GE 9605: Homo DER7TA0 SP 9606: Homo sapiens DE6NIY9 ID DE6NIY9 DE6NIY9 DN Methionine synthase reductase (MTRR) DE6NIY9 GN MTRR DE6NIY9 SN Methionine synthase cob(II)alamin reductase (methylating); NADPH-dependent diflavin oxidoreductase; MSR; MTRR DE6NIY9 UC MTRR_HUMAN DE6NIY9 RD Menadione DE6NIY9 GI 4552 DE6NIY9 E1 1: Oxidoreductase DE6NIY9 E2 1.16: Metal ion oxidoreductase DE6NIY9 E3 1.16.1: NAD/NADP acceptor oxidoreductase DE6NIY9 EC 1.16.1.8 DE6NIY9 RC Cobalamin (Cbl, vitamin B12) transport and metabolism:R-HSA-196741; Defective MTR causes methylmalonic aciduria and homocystinuria type cblG:R-HSA-3359469; Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE:R-HSA-3359467; Methylation:R-HSA-156581; Sulfur amino acid metabolism:R-HSA-1614635 DE6NIY9 PD 2QTL; 2QTZ DE6NIY9 SQ MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKHFRSSRGQEEISGALPVASPASSRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVNSNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPVFQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSGKALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIWS DE6NIY9 TD Primarily distributed in skeletal muscle. DE6NIY9 FC This enzyme is involved in the reductive regeneration of cob(I)alamin (vitamin B12) cofactor required for the maintenance of methionine synthase in a functional state. It is necessary for utilization of methylgroups from the folate cycle, thereby affecting transgenerational epigenetic inheritance. Folate pathway donates methyl groups necessary for cellular methylation and affects different pathways such as DNA methylation, possibly explaining the transgenerational epigenetic inheritance effects. DE6NIY9 KD 33208: Metazoa DE6NIY9 PL 7711: Chordata DE6NIY9 CL 40674: Mammalia DE6NIY9 OD 9443: Primates DE6NIY9 FM 9604: Hominidae DE6NIY9 GE 9605: Homo DE6NIY9 SP 9606: Homo sapiens DER5U19 ID DER5U19 DER5U19 DN Bifunctional epoxide hydrolase 2 (EPHX2) DER5U19 GN EPHX2 DER5U19 SN Lipid-phosphate phosphatase; Soluble epoxide hydrolase; Cytosolic epoxide hydrolase 2; CEH2; EPHX2; SEH DER5U19 UC HYES_HUMAN DER5U19 RD Myrisglycerol-phosphate DER5U19 GI 2053 DER5U19 E1 3: Hydrolases DER5U19 E2 3.3: Ether hydrolase DER5U19 E3 3.3.2: Ether hydrolase DER5U19 EC 3.3.2.10 DER5U19 RC Biosynthesis of maresins:R-HSA-9018682; Peroxisomal protein import:R-HSA-9033241; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET):R-HSA-2142670 DER5U19 KG Arachidonic acid metabolism:hsa00590; Metabolic pathways:hsa01100; Peroxisome:hsa04146 DER5U19 PD 1ZD2; 1ZD3; 1ZD4; 1ZD5; 3ANS; 3ANT; 3I1Y; 3I28; 3KOO DER5U19 SQ MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM DER5U19 TD Primarily distributed in intestine and liver. DER5U19 FC This enzyme has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides and plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Besides, it also determines steady- state levels of physiological mediators Additionally, the N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid. DER5U19 KD 33208: Metazoa DER5U19 PL 7711: Chordata DER5U19 CL 40674: Mammalia DER5U19 OD 9443: Primates DER5U19 FM 9604: Hominidae DER5U19 GE 9605: Homo DER5U19 SP 9606: Homo sapiens DENZGO4 ID DENZGO4 DENZGO4 DN ADP-dependent glucokinase (ADPGK) DENZGO4 GN ADPGK DENZGO4 SN ADP-specific glucokinase; Glucokinase ADP dependent; ADP-GK; ADPGK; PSEC0260; RbBP-35; 2610017G09Rik DENZGO4 UC ADPGK_HUMAN DENZGO4 RD D-glucose DENZGO4 GI 83440 DENZGO4 E1 2: Transferase DENZGO4 E2 2.7: Kinase DENZGO4 E3 2.7.1: Phosphotransferase DENZGO4 EC 2.7.1.147 DENZGO4 RC Glycolysis:R-HSA-70171 DENZGO4 KG Carbon metabolism:hsa01200; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100 DENZGO4 SQ MALWRGSAYAGFLALAVGCVFLLEPELPGSALRSLWSSLCLGPAPAPPGPVSPEGRLAAAWDALIVRPVRRWRRVAVGVNACVDVVLSGVKLLQALGLSPGNGKDHSILHSRNDLEEAFIHFMGKGAAAERFFSDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGPVGPKLHELLDDNVFVPPESLQEVDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEFQPDLVVLSGLHMMEGQSKELQRKRLLEVVTSISDIPTGIPVHLELASMTNRELMSSIVHQQVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWNGVPDVGMVSDILFWILKEHGRSKSRASDLTRIHFHTLVYHILATVDGHWANQLAAVAAGARVAGTQACATETIDTSRVSLRAPQEFMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLGDAISAEGLFYSEVHPHY DENZGO4 TD Low tissue/organ specificity. DENZGO4 FC This enzyme catalyzes the phosphorylation of D-glucose to D-glucose 6- phosphate using ADP as the phosphate donor. DENZGO4 KD 33208: Metazoa DENZGO4 PL 7711: Chordata DENZGO4 CL 40674: Mammalia DENZGO4 OD 9443: Primates DENZGO4 FM 9604: Hominidae DENZGO4 GE 9605: Homo DENZGO4 SP 9606: Homo sapiens DEOTVYU ID DEOTVYU DEOTVYU DN Thymidylate kinase (DTYMK) DEOTVYU GN DTYMK DEOTVYU SN Deoxythymidine 5'-monophosphate kinase; Deoxythymidine monophosphate kinase TMPK; dTMP kinase; CDC8; DTYMK; TMPK; TYMK DEOTVYU UC KTHY_HUMAN DEOTVYU RD AZT-MP DEOTVYU GI 1841 DEOTVYU E1 2: Transferase DEOTVYU E2 2.7: Kinase DEOTVYU E3 2.7.4: Phosphotransferase DEOTVYU EC 2.7.4.9 DEOTVYU RC Interconversion of nucleotide di- and triphosphates:R-HSA-499943 DEOTVYU KG Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DEOTVYU PD 1E9E; 1E9F; 1NMX; 1NMY; 1NMZ; 1NN0; 1NN5; 2XX3 DEOTVYU SQ MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKKSDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQPDVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDASKSIEAVHEDIRVLSEDAIRTATEKPLGELWK DEOTVYU TD Low tissue/organ specificity. DEOTVYU FC This enzyme catalyzes the conversion of dTMP to dTDP. DEOTVYU KD 33208: Metazoa DEOTVYU PL 7711: Chordata DEOTVYU CL 40674: Mammalia DEOTVYU OD 9443: Primates DEOTVYU FM 9604: Hominidae DEOTVYU GE 9605: Homo DEOTVYU SP 9606: Homo sapiens DEVN830 ID DEVN830 DEVN830 DN Neprilysin (MME) DEVN830 GN MME DEVN830 SN Atriopeptidase; Common acute lymphocytic leukemia antigen; Enkephalinase; Neutral endopeptidase; Neutral endopeptidase 24.11; Skin fibroblast elastase; CALLA; CD10; EPN; MME; NEP; SFE DEVN830 UC NEP_HUMAN DEVN830 RD Liraglutide DEVN830 GI 4311 DEVN830 E1 3: Hydrolases DEVN830 E2 3.4: Peptidase DEVN830 E3 3.4.24: Metallopeptidase DEVN830 EC 3.4.24.11 DEVN830 RC Metabolism of Angiotensinogen to Angiotensins:R-HSA-2022377; Neutrophil degranulation:R-HSA-6798695 DEVN830 KG Alzheimer's disease:hsa05010; Hematopoietic cell lineage:hsa04640; Protein digestion and absorption:hsa04974; Renin-angiotensin system:hsa04614 DEVN830 PD 1QVD; 1R1H; 1R1I; 1R1J; 1Y8J; 2QPJ; 2YB9; 4CTH; 5JMY DEVN830 SQ MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW DEVN830 TD Primarily distributed in blood, intestine and kidney. DEVN830 FC This enzyme has thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. It is biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond and able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. It is also involved in the degradation of atrial natriuretic factor. DEVN830 KD 33208: Metazoa DEVN830 PL 7711: Chordata DEVN830 CL 40674: Mammalia DEVN830 OD 9443: Primates DEVN830 FM 9604: Hominidae DEVN830 GE 9605: Homo DEVN830 SP 9606: Homo sapiens DE05S8C ID DE05S8C DE05S8C DN Fatty acid desaturase 1 (FADS1) DE05S8C GN FADS1 DE05S8C SN Acyl-CoA (8-3)-desaturase; Delta(5) desaturase; Delta(5) fatty acid desaturase; Delta-5 desaturase; D5D; FADS1; FADSD5 DE05S8C UC FADS1_HUMAN DE05S8C RD Omega-6-FA DE05S8C GI 3992 DE05S8C E1 1: Oxidoreductase DE05S8C E2 1.14: Oxygen paired donor oxidoreductase DE05S8C E3 1.14.19: Oxygen paired donor oxidoreductase DE05S8C EC 1.14.19.44 DE05S8C RC Linoleic acid (LA) metabolism:R-HSA-2046105; PPARA activates gene expression:R-HSA-1989781; alpha-linolenic acid (ALA) metabolism:R-HSA-2046106 DE05S8C KG Biosynthesis of unsaturated fatty acids:hsa01040; Fatty acid metabolism:hsa01212; Metabolic pathways:hsa01100 DE05S8C SQ MAPDPVAAETAAQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYNISEFTRRHPGGSRVISHYAGQDATDPFVAFHINKGLVKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVERMGLMKANHVFFLLYLLHILLLDGAAWLTLWVFGTSFLPFLLCAVLLSAVQAQAGWLQHDFGHLSVFSTSKWNHLLHHFVIGHLKGAPASWWNHMHFQHHAKPNCFRKDPDINMHPFFFALGKILSVELGKQKKKYMPYNHQHKYFFLIGPPALLPLYFQWYIFYFVIQRKKWVDLAWMITFYVRFFLTYVPLLGLKAFLGLFFIVRFLESNWFVWVTQMNHIPMHIDHDRNMDWVSTQLQATCNVHKSAFNDWFSGHLNFQIEHHLFPTMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKESGQLWLDAYLHQ DE05S8C TD Primarily distributed in liver, brain, adrenal gland, heart, fetal liver and brain. DE05S8C FC This enzyme acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. It is involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Specifically, it desaturates dihomo-gamma-linoleoate (DGLA) (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3), respectively. As a rate limiting enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid biosynthesis, it controls the metabolism of inflammatory lipids like prostaglandin E2. DE05S8C KD 33208: Metazoa DE05S8C PL 7711: Chordata DE05S8C CL 40674: Mammalia DE05S8C OD 9443: Primates DE05S8C FM 9604: Hominidae DE05S8C GE 9605: Homo DE05S8C SP 9606: Homo sapiens DED5AT3 ID DED5AT3 DED5AT3 DN Cytochrome P450 2F1 (CYP2F1) DED5AT3 GN CYP2F1 DED5AT3 SN Cytochrome P450 family 2 subfamily F member 1; CYP2F1; CYPIIF1; C2F1; CYP2F; OMIM: 124070; MGI: 88608; HomoloGene: 73898; GeneCards: CYP2F1 DED5AT3 UC CP2F1_HUMAN DED5AT3 RD Enflurane DED5AT3 GI 1572 DED5AT3 E1 1: Oxidoreductase DED5AT3 E2 1.14: Oxygen paired donor oxidoreductase DED5AT3 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DED5AT3 EC 1.14.14.1 DED5AT3 RC CYP2E1 reactions:R-HSA-211999; Fatty acids:R-HSA-211935; Xenobiotics:R-HSA-211981 DED5AT3 KG Metabolism of xenobiotics by cytochrome P450:hsa00980 DED5AT3 SQ MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNLPRPFQLCLRPR DED5AT3 TD Primarily distributed in lung, lymphoid tissue, pituitary gland and testis. DED5AT3 FC This enzyme is involved in the metabolism of various pneumotoxicants including naphthalene. It is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. It bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine. DED5AT3 KD 33208: Metazoa DED5AT3 PL 7711: Chordata DED5AT3 CL 40674: Mammalia DED5AT3 OD 9443: Primates DED5AT3 FM 9604: Hominidae DED5AT3 GE 9605: Homo DED5AT3 SP 9606: Homo sapiens DEZDRQO ID DEZDRQO DEZDRQO DN Corticosteroid 11-beta-dehydrogenase 1 (HSD11B1) DEZDRQO GN HSD11B1 DEZDRQO SN Corticosteroid 11-beta-dehydrogenase isozyme 1; Short chain dehydrogenase/reductase family 26C member 1; 11-beta-hydroxysteroid dehydrogenase 1; 11-DH; 11-beta-HSD1; HSD11; HSD11B1; HSD11L; SDR26C1 DEZDRQO UC DHI1_HUMAN DEZDRQO RD Cortisone acetate DEZDRQO GI 3290 DEZDRQO E1 1: Oxidoreductase DEZDRQO E2 1.1: CH-OH donor oxidoreductase DEZDRQO E3 1.1.1: NAD/NADP oxidoreductase DEZDRQO EC 1.1.1.146 DEZDRQO RC Glucocorticoid biosynthesis:R-HSA-194002 DEZDRQO KG Chemical carcinogenesis:hsa05204; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Steroid hormone biosynthesis:hsa00140 DEZDRQO PD 2BEL; 2ILT; 2IRW; 2RBE; 3BYZ; 3BZU; 3CH6; 3CZR; 3D3E DEZDRQO SQ MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK DEZDRQO TD Primarily distributed in liver. DEZDRQO FC This enzyme catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone and the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. DEZDRQO KD 33208: Metazoa DEZDRQO PL 7711: Chordata DEZDRQO CL 40674: Mammalia DEZDRQO OD 9443: Primates DEZDRQO FM 9604: Hominidae DEZDRQO GE 9605: Homo DEZDRQO SP 9606: Homo sapiens DEP54UE ID DEP54UE DEP54UE DN Beta-glucuronidase (GUSB) DEP54UE GN GUSB DEP54UE SN Glucuronidase beta; Complex carbohydrate glycosidase; Beta-G1; GUSB DEP54UE UC BGLR_HUMAN DEP54UE RD Niraparib DEP54UE GI 2990 DEP54UE E1 3: Hydrolases DEP54UE E2 3.2: Glycosylase DEP54UE E3 3.2.1: O/S-glycosyl compound glycosidase DEP54UE EC 3.2.1.31 DEP54UE RC HS-GAG degradation:R-HSA-2024096; Hyaluronan uptake and degradation:R-HSA-2160916; MPS VII - Sly syndrome:R-HSA-2206292; Neutrophil degranulation:R-HSA-6798695 DEP54UE KG Drug metabolism - other enzymes:hsa00983; Glycosaminoglycan degradation:hsa00531; Lysosome:hsa04142; Metabolic pathways:hsa01100; Pentose and glucuronate interconversions:hsa00040; Porphyrin and chlorophyll metabolism:hsa00860 DEP54UE PD 1BHG; 3HN3 DEP54UE SQ MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFEEQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVVLRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTTLPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQDSGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYLYSLEVQLTAQTSLGPVSDFYTLPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKGFDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNNVSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVTFVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSEYGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTRVLGNKKGIFTRQRQPKSAAFLLRERYWKIANETRYPHSVAKSQCLENSLFT DEP54UE TD Low tissue/organ specificity. DEP54UE FC This enzyme Plays an important role in the degradation of dermatan and keratan sulfates. DEP54UE KD 33208: Metazoa DEP54UE PL 7711: Chordata DEP54UE CL 40674: Mammalia DEP54UE OD 9443: Primates DEP54UE FM 9604: Hominidae DEP54UE GE 9605: Homo DEP54UE SP 9606: Homo sapiens DE6TYUK ID DE6TYUK DE6TYUK DN Aldosterone synthase (CYP11B2) DE6TYUK GN CYP11B2 DE6TYUK SN Aldosterone-synthesizing enzyme; Corticosterone 18-monooxygenase CYP11B2; Cytochrome P-450Aldo; Cytochrome P-450C18; Mitochondrial cytochrome P450 11B2; Steroid 11-beta-hydroxylase CYP11B2; Steroid 18-hydroxylase; ALDOS; CYP11B2; CYPXIB2 DE6TYUK UC C11B2_HUMAN DE6TYUK RD Hydrocortisone DE6TYUK GI 1585 DE6TYUK E1 1: Oxidoreductase DE6TYUK E2 1.14: Oxygen paired donor oxidoreductase DE6TYUK E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE6TYUK EC 1.14.15.4 DE6TYUK RC Defective CYP11B2 causes Corticosterone methyloxidase 1 deficiency (CMO-1 deficiency):R-HSA-5579009; Endogenous sterols:R-HSA-211976; Glucocorticoid biosynthesis:R-HSA-194002; Mineralocorticoid biosynthesis:R-HSA-193993 DE6TYUK KG Aldosterone synthesis and secretion:hsa04925; Metabolic pathways:hsa01100; Steroid hormone biosynthesis:hsa00140 DE6TYUK PD 4DVQ; 4FDH; 4ZGX DE6TYUK SQ MALRAKAEVCVAAPWLSLQRARALGTRAARAPRTVLPFEAMPQHPGNRWLRLLQIWREQGYEHLHLEMHQTFQELGPIFRYNLGGPRMVCVMLPEDVEKLQQVDSLHPCRMILEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPDVLSPKAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWISPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFNRPQHYTGIVAELLLKAELSLEAIKANSMELTAGSVDTTAFPLLMTLFELARNPDVQQILRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVQVFLYSLGRNAALFPRPERYNPQRWLDIRGSGRNFHHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHFLVETLTQEDIKMVYSFILRPGTSPLLTFRAIN DE6TYUK TD Primarily distributed in adrenal. DE6TYUK FC This enzyme catalyzes the biosynthesis of adrenal mineralocorticoid aldosterone. And it catalyzes three sequential oxidative reactions of 11-deoxycorticosterone/21- hydroxyprogesterone, namely 11-beta hydroxylation followed with two successive oxidations at C18 to yield 18-hydroxy and then 18-aldehyde derivatives, resulting in the formation of aldosterone. DE6TYUK KD 33208: Metazoa DE6TYUK PL 7711: Chordata DE6TYUK CL 40674: Mammalia DE6TYUK OD 9443: Primates DE6TYUK FM 9604: Hominidae DE6TYUK GE 9605: Homo DE6TYUK SP 9606: Homo sapiens DEKZQY6 ID DEKZQY6 DEKZQY6 DN Dipeptidyl peptidase IV (DPP4) DEKZQY6 GN DPP4 DEKZQY6 SN Dipeptidyl peptidase 4; Adenosine deaminase complexing protein 2; Dipeptidyl peptidase 4 membrane form; Dipeptidyl peptidase 4 soluble form; Dipeptidyl peptidase IV membrane form; Dipeptidyl peptidase IV soluble form; T-cell activation antigen CD26; TP103; ADABP; ADCP-2; ADCP2; CD26; DPP IV; DPP4 DEKZQY6 UC DPP4_HUMAN DEKZQY6 RD Exenatide DEKZQY6 GI 1803 DEKZQY6 E1 3: Hydrolases DEKZQY6 E2 3.4: Peptidase DEKZQY6 E3 3.4.14: Di/tripeptidyl peptidase DEKZQY6 EC 3.4.14.5 DEKZQY6 RC Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1):R-HSA-381771; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP):R-HSA-400511 DEKZQY6 KG Protein digestion and absorption:hsa04974 DEKZQY6 PD 1NU6; 1NU8; 1PFQ; 1R9M; 1R9N; 1RWQ; 1TK3; 1TKR; 1U8E DEKZQY6 SQ MKTPWKVLLGLLGAAALVTIITVPVVLLNKGTDDATADSRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVFNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYNYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSPVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGITDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYSFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSVTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRIQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRPSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITKGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDYTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPLYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIILNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVFRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLGTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFIKQCFSLP DEKZQY6 TD Primarily distributed in intestine and parathyroid gland. DEKZQY6 FC This enzyme is involved in the pericellular proteolysis of the extracellular matrix (ECM) in association with FAP, the migration and invasion of endothelial cells into the ECM. It also acts as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. It removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. DEKZQY6 KD 33208: Metazoa DEKZQY6 PL 7711: Chordata DEKZQY6 CL 40674: Mammalia DEKZQY6 OD 9443: Primates DEKZQY6 FM 9604: Hominidae DEKZQY6 GE 9605: Homo DEKZQY6 SP 9606: Homo sapiens DERDQWN ID DERDQWN DERDQWN DN Dihydrotestosterone oxidoreductase (HSD3B1) DERDQWN GN HSD3B1 DERDQWN SN Delta-5-3-ketosteroid isomerase; Steroid Delta-isomerase; Trophoblast antigen FDO161G; 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1; 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type I; 3-beta-hydroxysteroid 3-dehydrogenase; 3-beta-HSD I; 3BH; HSD3B1; HSDB3A DERDQWN UC 3BHS1_HUMAN DERDQWN RD Tibolone DERDQWN GI 3283 DERDQWN E1 1: Oxidoreductase DERDQWN E2 1.1: CH-OH donor oxidoreductase DERDQWN E3 1.1.1: NAD/NADP oxidoreductase DERDQWN EC 1.1.1.145 DERDQWN RC Androgen biosynthesis:R-HSA-193048; Glucocorticoid biosynthesis:R-HSA-194002; Mineralocorticoid biosynthesis:R-HSA-193993 DERDQWN KG Aldosterone synthesis and secretion:hsa04925; Cortisol synthesis and secretion:hsa04927; Cushing syndrome:hsa04934; Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Steroid hormone biosynthesis:hsa00140 DERDQWN SQ MTGWSCLVTGAGGFLGQRIIRLLVKEKELKEIRVLDKAFGPELREEFSKLQNKTKLTVLEGDILDEPFLKRACQDVSVIIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPAPYPHSKKLAEKAVLAANGWNLKNGGTLYTCALRPMYIYGEGSRFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALQDPKKAPSIRGQFYYISDDTPHQSYDNLNYTLSKEFGLRLDSRWSFPLSLMYWIGFLLEIVSFLLRPIYTYRPPFNRHIVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLVDRHKETLKSKTQ DERDQWN TD Primarily distributed in placenta and skin. DERDQWN FC This enzyme is responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo- Delta(4)-steroids. It specifically catalyzes the conversion of pregnenolone to progesterone, 17alpha-hydroxypregnenolone to 17alpha-hydroxyprogesterone, dehydroepiandrosterone (DHEA) to 4-androstenedione, and androstenediol to testosterone. Additionally, it catalyzes the interconversion between 3beta-hydroxy and 3-oxo-5alpha-androstane steroids controlling the bioavalability of the active forms. And it specifically converts dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR and converts androstanedione, a precursor of testosterone and estrone, to epiandrosterone. DERDQWN KD 33208: Metazoa DERDQWN PL 7711: Chordata DERDQWN CL 40674: Mammalia DERDQWN OD 9443: Primates DERDQWN FM 9604: Hominidae DERDQWN GE 9605: Homo DERDQWN SP 9606: Homo sapiens DE08Z3W ID DE08Z3W DE08Z3W DN Cytosolic phospholipase A2 (PLA2G4A) DE08Z3W GN PLA2G4A DE08Z3W SN Phosphatidylcholine 2-acylhydrolase; Phospholipase A2; Phospholipase A2 group IVA; Lysophospholipase; PLA2G4; PLA2G4A; CPLA2; cPLA2 DE08Z3W UC PA24A_HUMAN DE08Z3W RD Urethane DE08Z3W GI 5321 DE08Z3W E1 3: Hydrolases DE08Z3W E2 3.1: Ester bond hydrolase DE08Z3W E3 3.1.1: Carboxylic ester hydrolase DE08Z3W EC 3.1.1.4 DE08Z3W RC ADP signalling through P2Y purinoceptor 1:R-HSA-418592; Acyl chain remodeling of CL:R-HSA-1482798; Acyl chain remodelling of PC:R-HSA-1482788; Acyl chain remodelling of PE:R-HSA-1482839; Acyl chain remodelling of PG:R-HSA-1482925; Acyl chain remodelling of PI:R-HSA-1482922; Acyl chain remodelling of PS:R-HSA-1482801; Arachidonic acid metabolism:R-HSA-2142753; COPI-independent Golgi-to-ER retrograde traffic:R-HSA-6811436; Hydrolysis of LPC:R-HSA-1483115; Platelet sensitization by LDL:R-HSA-432142; Synthesis of PA:R-HSA-1483166; phospho-PLA2 pathway:R-HSA-111995 DE08Z3W KG Arachidonic acid metabolism:hsa00590; Choline metabolism in cancer:hsa05231; Ether lipid metabolism:hsa00565; Fc epsilon RI signaling pathway:hsa04664; Fc gamma R-mediated phagocytosis:hsa04666; Glutamatergic synapse:hsa04724; Glycerophospholipid metabolism:hsa00564; GnRH signaling pathway:hsa04912; Inflammatory mediator regulation of TRP channels:hsa04750; Linoleic acid metabolism:hsa00591; Long-term depression:hsa04730; MAPK signaling pathway:hsa04010; Metabolic pathways:hsa01100; Necroptosis:hsa04217; Ovarian steroidogenesis:hsa04913; Oxytocin signaling pathway:hsa04921; Phospholipase D signaling pathway:hsa04072; Platelet activation:hsa04611; Ras signaling pathway:hsa04014; Serotonergic synapse:hsa04726; VEGF signaling pathway:hsa04370; Vascular smooth muscle contraction:hsa04270; alpha-Linolenic acid metabolism:hsa00592 DE08Z3W PD 1BCI; 1CJY; 1RLW DE08Z3W SQ MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEVPFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEGLHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEELENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYRAPGVPRETEEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRRQNPSRCSVSLSNVEARRFFNKEFLSKPKA DE08Z3W TD Primarily distributed in ductus deferens, parathyroid gland and seminal vesicle. DE08Z3W FC This enzyme selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. DE08Z3W KD 33208: Metazoa DE08Z3W PL 7711: Chordata DE08Z3W CL 40674: Mammalia DE08Z3W OD 9443: Primates DE08Z3W FM 9604: Hominidae DE08Z3W GE 9605: Homo DE08Z3W SP 9606: Homo sapiens DEDI4B8 ID DEDI4B8 DEDI4B8 DN Fatty acid desaturase 2 (FADS2) DEDI4B8 GN FADS2 DEDI4B8 SN Acyl-CoA 6-desaturase; Delta(6) desaturase; Delta(6) fatty acid desaturase; Delta-6 desaturase; D6D; FADS2 DEDI4B8 UC FADS2_HUMAN DEDI4B8 RD Omega-6-FA DEDI4B8 GI 9415 DEDI4B8 E1 1: Oxidoreductase DEDI4B8 E2 1.14: Oxygen paired donor oxidoreductase DEDI4B8 E3 1.14.19: Oxygen paired donor oxidoreductase DEDI4B8 EC 1.14.19.3 DEDI4B8 RC Linoleic acid (LA) metabolism:R-HSA-2046105; alpha-linolenic acid (ALA) metabolism:R-HSA-2046106 DEDI4B8 KG Biosynthesis of unsaturated fatty acids:hsa01040; Fatty acid metabolism:hsa01212; Metabolic pathways:hsa01100; PPAR signaling pathway:hsa03320; alpha-Linolenic acid metabolism:hsa00592 DEDI4B8 SQ MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVIGHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVLGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAVSYYIRFFITYIPFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLWLDAYLHK DEDI4B8 TD Primarily distributed in liver, brain, lung, heart and retina. DEDI4B8 FC This enzyme acts as a fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 6 of the fatty acyl chain. It is involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. It catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively. Subsequently, in the biosynthetic pathway of HUFA n- 3 series, desaturates tetracosapentaenoate (24:5n-3) to tetracosahexaenoate (24:6n-3), which is then converted to docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system function. DEDI4B8 KD 33208: Metazoa DEDI4B8 PL 7711: Chordata DEDI4B8 CL 40674: Mammalia DEDI4B8 OD 9443: Primates DEDI4B8 FM 9604: Hominidae DEDI4B8 GE 9605: Homo DEDI4B8 SP 9606: Homo sapiens DE4G629 ID DE4G629 DE4G629 DN Succinic semialdehyde reductase (AKR7A2) DE4G629 GN AKR7A2 DE4G629 SN AFB1 aldehyde reductase 1; Aflatoxin B1 aldehyde reductase member 2; Aldoketoreductase 7; SSA reductase; AFAR; AFAR1; AFB1-AR 1; AKR7; AKR7A2 DE4G629 UC ARK72_HUMAN DE4G629 RD Doxorubicin DE4G629 GI 8574 DE4G629 E1 1: Oxidoreductase DE4G629 E2 1.1: CH-OH donor oxidoreductase DE4G629 E3 1.1.1: NAD/NADP oxidoreductase DE4G629 EC 1.1.1.B47 DE4G629 RC Aflatoxin activation and detoxification:R-HSA-5423646 DE4G629 KG Metabolism of xenobiotics by cytochrome P450:hsa00980 DE4G629 PD 2BP1 DE4G629 SQ MLSAASRVVSRAAVHCALRSPPPEARALAMSRPPPPRVASVLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPWDGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYRNRFWKEHHFEAIALVEKALQAAYGASAPSVTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAATEEGPLEPAVVDAFNQAWHLVAHECPNYFR DE4G629 TD Primarily distributed in brain, liver, small intestine and testis. Also expressed in heart, prostate, skeletal muscle and spleen. DE4G629 FC This enzyme catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. It may have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB) and has broad substrate specificity. It also has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2- aldehyde (in vitro). It can reduce 1,2-naphthoquinone and 9,10- phenanthrenequinone (in vitro) and reduce the dialdehyde protein- binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. It may be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. DE4G629 KD 33208: Metazoa DE4G629 PL 7711: Chordata DE4G629 CL 40674: Mammalia DE4G629 OD 9443: Primates DE4G629 FM 9604: Hominidae DE4G629 GE 9605: Homo DE4G629 SP 9606: Homo sapiens DEON3ED ID DEON3ED DEON3ED DN Phosphodiesterase 7B (PDE7B) DEON3ED GN PDE7B DEON3ED SN Phosphodiesterase class 7B; cAMP-specific 3',5'-cyclic phosphodiesterase 7B; PDE7B DEON3ED UC PDE7B_HUMAN DEON3ED RD Testosterone enanthate DEON3ED GI 27115 DEON3ED E1 3: Hydrolases DEON3ED E2 3.1: Ester bond hydrolase DEON3ED E3 3.1.4: Phosphoric diester hydrolase DEON3ED EC 3.1.4.53 DEON3ED RC G alpha (s) signalling events:R-HSA-418555 DEON3ED KG Metabolic pathways:hsa01100; Morphine addiction:hsa05032; Purine metabolism:hsa00230 DEON3ED PD 1LXW DEON3ED SQ MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYSGEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIFLFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMSVLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHNKDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEISPLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQHRSRGSSGSGPDHDHAGQGTESEEQEGDSP DEON3ED TD Primarily distributed in brain. Also expressed in heart, liver, skeletal muscle and pancreas. DEON3ED FC This enzyme hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. DEON3ED KD 33208: Metazoa DEON3ED PL 7711: Chordata DEON3ED CL 40674: Mammalia DEON3ED OD 9443: Primates DEON3ED FM 9604: Hominidae DEON3ED GE 9605: Homo DEON3ED SP 9606: Homo sapiens DE8RYV5 ID DE8RYV5 DE8RYV5 DN NADPH:quinone reductase (CRYZ) DE8RYV5 GN CRYZ DE8RYV5 SN Quinone oxidoreductase; Zeta-crystallin; Hydrogen:menaquinone oxidoreductase; Hydrogen:quinone oxidoreductase; CRYZ DE8RYV5 UC QOR_HUMAN DE8RYV5 RD Menadione DE8RYV5 GI 1429 DE8RYV5 E1 1: Oxidoreductase DE8RYV5 E2 1.6: NADH/NADPH oxidoreductase DE8RYV5 E3 1.6.5: Quinone acceptor oxidoreductase DE8RYV5 EC 1.6.5.5 DE8RYV5 PD 1YB5 DE8RYV5 SQ MATGQKLMRAVRVFEFGGPEVLKLRSDIAVPIPKDHQVLIKVHACGVNPVETYIRSGTYSRKPLLPYTPGSDVAGVIEAVGDNASAFKKGDRVFTSSTISGGYAEYALAADHTVYKLPEKLDFKQGAAIGIPYFTAYRALIHSACVKAGESVLVHGASGGVGLAACQIARAYGLKILGTAGTEEGQKIVLQNGAHEVFNHREVNYIDKIKKYVGEKGIDIIIEMLANVNLSKDLSLLSHGGRVIVVGSRGTIEINPRDTMAKESSIIGVTLFSSTKEEFQQYAAALQAGMEIGWLKPVIGSQYPLEKVAEAHENIIHGSGATGKMILLL DE8RYV5 TD Primarily distributed in kidney and liver. DE8RYV5 FC This enzyme acts in the detoxification of xenobiotics. DE8RYV5 KD 33208: Metazoa DE8RYV5 PL 7711: Chordata DE8RYV5 CL 40674: Mammalia DE8RYV5 OD 9443: Primates DE8RYV5 FM 9604: Hominidae DE8RYV5 GE 9605: Homo DE8RYV5 SP 9606: Homo sapiens DEZGVDW ID DEZGVDW DEZGVDW DN Steroid 5-alpha-reductase 3 (SRD5A3) DEZGVDW GN SRD5A3 DEZGVDW SN Alpha-reductase steroid 3; 3-oxo-5-alpha-steroid 4-dehydrogenase 3; Polyprenol reductase; S5AR 3; SR type 3; SRD5A2L; SRD5A3; Steroid 5-alpha-reductase 2-like DEZGVDW UC PORED_HUMAN DEZGVDW RD Testosterone cypionate DEZGVDW GI 79644 DEZGVDW E1 1: Oxidoreductase DEZGVDW E2 1.3: CH-CH donor oxidoreductase DEZGVDW E3 1.3.1: NAD/NADP acceptor oxidoreductase DEZGVDW EC 1.3.1.22 DEZGVDW RC Androgen biosynthesis:R-HSA-193048; Defective SRD5A3 causes SRD5A3-CDG (CDG-1q) and KHRZ:R-HSA-4755579; Synthesis of Dolichyl-phosphate:R-HSA-446199 DEZGVDW KG N-Glycan biosynthesis:hsa00510; Steroid hormone biosynthesis:hsa00140 DEZGVDW SQ MAPWAEAEHSALNPLRAVWLTLTAAFLLTLLLQLLPPGLLPGCAIFQDLIRYGKTKCGEPSRPAACRAFDVPKRYFSHFYIISVLWNGFLLWCLTQSLFLGAPFPSWLHGLLRILGAAQFQGGELALSAFLVLVFLWLHSLRRLFECLYVSVFSNVMIHVVQYCFGLVYYVLVGLTVLSQVPMDGRNAYITGKNLLMQARWFHILGMMMFIWSSAHQYKCHVILGNLRKNKAGVVIHCNHRIPFGDWFEYVSSPNYLAELMIYVSMAVTFGFHNLTWWLVVTNVFFNQALSAFLSHQFYKSKFVSYPKHRKAFLPFLF DEZGVDW TD Low tissue/organ specificity. DEZGVDW FC This enzyme plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. It acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism and is also able to convert testosterone (T) into 5- alpha-dihydrotestosterone (DHT). DEZGVDW KD 33208: Metazoa DEZGVDW PL 7711: Chordata DEZGVDW CL 40674: Mammalia DEZGVDW OD 9443: Primates DEZGVDW FM 9604: Hominidae DEZGVDW GE 9605: Homo DEZGVDW SP 9606: Homo sapiens DEOG15F ID DEOG15F DEOG15F DN Steroid 5-alpha-reductase 1 (SRD5A1) DEOG15F GN SRD5A1 DEOG15F SN Alpha-reductase steroid 1; 3-oxo-5-alpha-steroid 4-dehydrogenase 1; S5AR 1; SR type 1; SRD5A1 DEOG15F UC S5A1_HUMAN DEOG15F RD Testosterone cypionate DEOG15F GI 6715 DEOG15F E1 1: Oxidoreductase DEOG15F E2 1.3: CH-CH donor oxidoreductase DEOG15F E3 1.3.1: NAD/NADP acceptor oxidoreductase DEOG15F EC 1.3.1.22 DEOG15F RC Androgen biosynthesis:R-HSA-193048 DEOG15F KG Steroid hormone biosynthesis:hsa00140 DEOG15F SQ MATATGVAEERLLAALAYLQCAVGCAVFARNRQTNSVYGRHALPSHRLRVPARAAWVVQELPSLALPLYQYASESAPRLRSAPNCILLAMFLVHYGHRCLIYPFLMRGGKPMPLLACTMAIMFCTCNGYLQSRYLSHCAVYADDWVTDPRFLIGFGLWLTGMLINIHSDHILRNLRKPGDTGYKIPRGGLFEYVTAANYFGEIMEWCGYALASWSVQGAAFAFFTFCFLSGRAKEHHEWYLRKFEEYPKFRKIIIPFLF DEOG15F TD Primarily distributed in liver. DEOG15F FC This enzyme converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3- oxosteroids. DEOG15F KD 33208: Metazoa DEOG15F PL 7711: Chordata DEOG15F CL 40674: Mammalia DEOG15F OD 9443: Primates DEOG15F FM 9604: Hominidae DEOG15F GE 9605: Homo DEOG15F SP 9606: Homo sapiens DEVJIHS ID DEVJIHS DEVJIHS DN Proline dehydrogenase 1 (PRODH) DEVJIHS GN PRODH DEVJIHS SN Proline oxidase; Proline oxidase 2; Mitochondrial proline dehydrogenase 1; p53-induced gene 6 protein; PIG6; POX2; PRODH; PRODH2 DEVJIHS UC PROD_HUMAN DEVJIHS RD Proline DEVJIHS GI 5625 DEVJIHS E1 1: Oxidoreductase DEVJIHS E2 1.5: CH-NH donor oxidoreductase DEVJIHS E3 1.5.5: Quinone acceptor oxidoreductase DEVJIHS EC 1.5.5.2 DEVJIHS RC Proline catabolism:R-HSA-70688 DEVJIHS KG Arginine and proline metabolism:hsa00330; Metabolic pathways:hsa01100 DEVJIHS SQ MALRRALPALRPCIPRFVQLSTAPASREQPAAGPAAVPGGGSATAVRPPVPAVDFGNAQEAYRSRRTWELARSLLVLRLCAWPALLARHEQLLYVSRKLLGQRLFNKLMKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHRAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSLIDSRTKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRMLQRMDVLAKKATEMGVRLMVDAEQTYFQPAISRLTLEMQRKFNVEKPLIFNTYQCYLKDAYDNVTLDVELARREGWCFGAKLVRGAYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDYVLEELKHNAKAKVMVASHNEDTVRFALRRMEELGLHPADHQVYFGQLLGMCDQISFPLGQAGYPVYKYVPYGPVMEVLPYLSRRALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA DEVJIHS TD Primarily distributed in lung, skeletal muscle, brain and intestine. DEVJIHS FC This enzyme converts proline to delta-1-pyrroline-5-carboxylate. DEVJIHS KD 33208: Metazoa DEVJIHS PL 7711: Chordata DEVJIHS CL 40674: Mammalia DEVJIHS OD 9443: Primates DEVJIHS FM 9604: Hominidae DEVJIHS GE 9605: Homo DEVJIHS SP 9606: Homo sapiens DEIVKZ8 ID DEIVKZ8 DEIVKZ8 DN NADPH-dependent carbonyl reductase 3 (CBR3) DEIVKZ8 GN CBR3 DEIVKZ8 SN Carbonyl reductase [NADPH] 3; Short chain dehydrogenase/reductase family 21C member 2; CBR3 DEIVKZ8 UC CBR3_HUMAN DEIVKZ8 RD Daunorubicin DEIVKZ8 GI 874 DEIVKZ8 E1 1: Oxidoreductase DEIVKZ8 E2 1.1: CH-OH donor oxidoreductase DEIVKZ8 E3 1.1.1: NAD/NADP oxidoreductase DEIVKZ8 EC 1.1.1.184 DEIVKZ8 RC Phase I - Functionalization of compounds:R-HSA-211945 DEIVKZ8 KG Arachidonic acid metabolism:hsa00590; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980 DEIVKZ8 PD 2HRB DEIVKZ8 SQ MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTKNEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDSIRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW DEIVKZ8 TD Primarily distributed in tongue, ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte and prostateand testis. DEIVKZ8 FC This enzyme has low NADPH-dependent oxidoreductase activity towards 4- benzoylpyridine and menadione (in vitro). DEIVKZ8 KD 33208: Metazoa DEIVKZ8 PL 7711: Chordata DEIVKZ8 CL 40674: Mammalia DEIVKZ8 OD 9443: Primates DEIVKZ8 FM 9604: Hominidae DEIVKZ8 GE 9605: Homo DEIVKZ8 SP 9606: Homo sapiens DEBMX7C ID DEBMX7C DEBMX7C DN Dimethylaniline oxidase 5 (FMO5) DEBMX7C GN FMO5 DEBMX7C SN Dimethylaniline monooxygenase [N-oxide-forming] 5; FMO 5; FMO5; Hepatic flavin-containing monooxygenase 5 DEBMX7C UC FMO5_HUMAN DEBMX7C RD Ranitidine DEBMX7C GI 2330 DEBMX7C E1 1: Oxidoreductase DEBMX7C E2 1.14: Oxygen paired donor oxidoreductase DEBMX7C E3 1.14.13: NADH/NADPH donor oxidoreductase DEBMX7C EC 1.14.13.8 DEBMX7C KG Drug metabolism - cytochrome P450:hsa00982 DEBMX7C SQ MTKKRIAVIGGGVSGLSSIKCCVEEGLEPVCFERTDDIGGLWRFQENPEEGRASIYKSVIINTSKEMMCFSDYPIPDHYPNFMHNAQVLEYFRMYAKEFDLLKYIRFKTTVCSVKKQPDFATSGQWEVVTESEGKKEMNVFDGVMVCTGHHTNAHLPLESFPGIEKFKGQYFHSRDYKNPEGFTGKRVIIIGIGNSGGDLAVEISQTAKQVFLSTRRGAWILNRVGDYGYPADVLFSSRLTHFIWKICGQSLANKYLEKKINQRFDHEMFGLKPKHRALSQHPTLNDDLPNRIISGLVKVKGNVKEFTETAAIFEDGSREDDIDAVIFATGYSFDFPFLEDSVKVVKNKISLYKKVFPPNLERPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKTLPSQSEMMAEISKAQEEIDKRYVESQRHTIQGDYIDTMEELADLVGVRPNLLSLAFTDPKLALHLLLGPCTPIHYRVQGPGKWDGARKAILTTDDRIRKPLMTRVVERSSSMTSTMTIGKFMLALAFFAIIIAYF DEBMX7C TD Primarily distributed in intestine, liver and stomach. DEBMX7C FC This enzyme is expressed in fetal and adult liver. Flavin-containing monooxygenases are NADPH-dependent flavoenzymes that catalyzes the oxidation of soft nucleophilic heteroatom centers in drugs, pesticides, and xenobiotics. DEBMX7C KD 33208: Metazoa DEBMX7C PL 7711: Chordata DEBMX7C CL 40674: Mammalia DEBMX7C OD 9443: Primates DEBMX7C FM 9604: Hominidae DEBMX7C GE 9605: Homo DEBMX7C SP 9606: Homo sapiens DEH0J8X ID DEH0J8X DEH0J8X DN Arachidonate 15-lipoxygenase (ALOX15) DEH0J8X GN ALOX15 DEH0J8X SN Arachidonate 12-lipoxygenase leukocyte-type; Arachidonate omega-6 lipoxygenase; LOG15; 12-LOX; 12/15-lipoxygenase; 15-LOX; 15-LOX-1; ALOX15 DEH0J8X UC LOX15_HUMAN DEH0J8X RD Arachidonic acid DEH0J8X GI 246 DEH0J8X E1 1: Oxidoreductase DEH0J8X E2 1.13: Oxygen single donor oxidoreductase DEH0J8X E3 1.13.11: Oxygen single donor oxidoreductase DEH0J8X EC 1.13.11.33 DEH0J8X RC Biosynthesis of DHA-derived SPMs:R-HSA-9018677; Biosynthesis of DPAn-3-derived protectins and resolvins:R-HSA-9026286; Biosynthesis of DPAn-6 SPMs:R-HSA-9025106; Biosynthesis of E-series 18(R)-resolvins:R-HSA-9023661; Biosynthesis of E-series 18(S)-resolvins:R-HSA-9018896; Biosynthesis of protectins:R-HSA-9018681; Interleukin-4 and Interleukin-13 signaling:R-HSA-6785807; Synthesis of 12-eicosatetraenoic acid derivatives:R-HSA-2142712; Synthesis of 15-eicosatetraenoic acid derivatives:R-HSA-2142770; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DEH0J8X KG Arachidonic acid metabolism:hsa00590; Ferroptosis:hsa04216; Linoleic acid metabolism:hsa00591; Metabolic pathways:hsa01100; Necroptosis:hsa04217; Serotonergic synapse:hsa04726 DEH0J8X PD 2ABT DEH0J8X SQ MGLYRIRVSTGASLYAGSNNQVQLWLVGQHGEAALGKRLWPARGKETELKVEVPEYLGPLLFVKLRKRHLLKDDAWFCNWISVQGPGAGDEVRFPCYRWVEGNGVLSLPEGTGRTVGEDPQGLFQKHREEELEERRKLYRWGNWKDGLILNMAGAKLYDLPVDERFLEDKRVDFEVSLAKGLADLAIKDSLNVLTCWKDLDDFNRIFWCGQSKLAERVRDSWKEDALFGYQFLNGANPVVLRRSAHLPARLVFPPGMEELQAQLEKELEGGTLFEADFSLLDGIKANVILCSQQHLAAPLVMLKLQPDGKLLPMVIQLQLPRTGSPPPPLFLPTDPPMAWLLAKCWVRSSDFQLHELQSHLLRGHLMAEVIVVATMRCLPSIHPIFKLIIPHLRYTLEINVRARTGLVSDMGIFDQIMSTGGGGHVQLLKQAGAFLTYSSFCPPDDLADRGLLGVKSSFYAQDALRLWEIIYRYVEGIVSLHYKTDVAVKDDPELQTWCREITEIGLQGAQDRGFPVSLQARDQVCHFVTMCIFTCTGQHASVHLGQLDWYSWVPNAPCTMRLPPPTTKDATLETVMATLPNFHQASLQMSITWQLGRRQPVMVAVGQHEEEYFSGPEPKAVLKKFREELAALDKEIEIRNAKLDMPYEYLRPSVVENSVAI DEH0J8X TD Primarily distributed in adipose tissue, blood and lung. DEH0J8X FC This enzyme catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. It converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12- HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. It also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid and may also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. DEH0J8X KD 33208: Metazoa DEH0J8X PL 7711: Chordata DEH0J8X CL 40674: Mammalia DEH0J8X OD 9443: Primates DEH0J8X FM 9604: Hominidae DEH0J8X GE 9605: Homo DEH0J8X SP 9606: Homo sapiens DEWJATF ID DEWJATF DEWJATF DN Adenosine 5'-monophosphoramidase (HINT1) DEWJATF GN HINT1 DEWJATF SN Histidine triad nucleotide-binding protein 1; HINT; HINT1; PKCI-1; PKCI1; PRKCNH1; Protein kinase C inhibitor 1; Protein kinase C-interacting protein 1 DEWJATF UC HINT1_HUMAN DEWJATF RD Sofosbuvir DEWJATF GI 3094 DEWJATF E1 3: Hydrolases DEWJATF E2 3.2: Glycosylase DEWJATF E3 3.2.1: O/S-glycosyl compound glycosidase DEWJATF EC 3.2.1.45 DEWJATF PD 1KPB; 1KPC; 1KPE; 1KPF; 3TW2; 4EQE; 4EQG; 4EQH; 4ZKL DEWJATF SQ MADEIAKAQVARPGGDTIFGKIIRKEIPAKIIFEDDRCLAFHDISPQAPTHFLVIPKKHISQISVAEDDDESLLGHLMIVGKKCAADLGLNKGYRMVVNEGSDGGQSVYHVHLHVLGGRQMHWPPG DEWJATF TD Low tissue/organ specificity. DEWJATF FC This enzyme hydrolyzes purine nucleotide phosphoramidates with a single phosphate group, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate). It hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester. It can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O- phosphates with concomitant release of hydrogen sulfide. DEWJATF KD 33208: Metazoa DEWJATF PL 7711: Chordata DEWJATF CL 40674: Mammalia DEWJATF OD 9443: Primates DEWJATF FM 9604: Hominidae DEWJATF GE 9605: Homo DEWJATF SP 9606: Homo sapiens DEJ6FSR ID DEJ6FSR DEJ6FSR DN Arylsulfatase A (ARSA) DEJ6FSR GN ARSA DEJ6FSR SN Arylsulfatase A component B; Arylsulfatase A component C; Cerebroside-sulfatase; ARSA; ASA DEJ6FSR UC ARSA_HUMAN DEJ6FSR RD Micafungin DEJ6FSR GI 410 DEJ6FSR E1 3: Hydrolases DEJ6FSR E2 3.1: Ester bond hydrolase DEJ6FSR E3 3.1.6: Sulfuric ester hydrolase DEJ6FSR EC 3.1.6.8 DEJ6FSR RC Glycosphingolipid metabolism:R-HSA-1660662; Neutrophil degranulation:R-HSA-6798695; The activation of arylsulfatases:R-HSA-1663150 DEJ6FSR KG Lysosome:hsa04142; Sphingolipid metabolism:hsa00600 DEJ6FSR PD 1AUK; 1E1Z; 1E2S; 1E33; 1E3C; 1N2K; 1N2L; 2AIJ; 2HI8 DEJ6FSR SQ MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSPLLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSLTAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARGEDPALQICCHPGCTPRPACCHCPDPHA DEJ6FSR TD Low tissue/organ specificity. DEJ6FSR FC This enzyme hydrolyzes cerebroside sulfate. DEJ6FSR KD 33208: Metazoa DEJ6FSR PL 7711: Chordata DEJ6FSR CL 40674: Mammalia DEJ6FSR OD 9443: Primates DEJ6FSR FM 9604: Hominidae DEJ6FSR GE 9605: Homo DEJ6FSR SP 9606: Homo sapiens DEWSHL5 ID DEWSHL5 DEWSHL5 DN Vitamin B12 methionine synthase (MTR) DEWSHL5 GN MTR DEWSHL5 SN Methionine synthase; Vitamin-B12 dependent methionine synthase; 5-methyltetrahydrofolate--homocysteine methyltransferase; MS; MTR DEWSHL5 UC METH_HUMAN DEWSHL5 RD Levomefolic acid DEWSHL5 GI 4548 DEWSHL5 E1 2: Transferase DEWSHL5 E2 2.1: Methylase DEWSHL5 E3 2.1.1: Methyltransferase DEWSHL5 EC 2.1.1.13 DEWSHL5 RC Cobalamin (Cbl, vitamin B12) transport and metabolism:R-HSA-196741; Defective MTR causes methylmalonic aciduria and homocystinuria type cblG:R-HSA-3359469; Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE:R-HSA-3359467; Methylation:R-HSA-156581; Sulfur amino acid metabolism:R-HSA-1614635 DEWSHL5 KG Biosynthesis of amino acids:hsa01230; Cysteine and methionine metabolism:hsa00270; Metabolic pathways:hsa01100; One carbon pool by folate:hsa00670; Selenocompound metabolism:hsa00450 DEWSHL5 PD 2O2K; 4CCZ DEWSHL5 SQ MSPALQDLSQPEGLKKTLRDEINAILQKRIMVLDGGMGTMIQREKLNEEHFRGQEFKDHARPLKGNNDILSITQPDVIYQIHKEYLLAGADIIETNTFSSTSIAQADYGLEHLAYRMNMCSAGVARKAAEEVTLQTGIKRFVAGALGPTNKTLSVSPSVERPDYRNITFDELVEAYQEQAKGLLDGGVDILLIETIFDTANAKAALFALQNLFEEKYAPRPIFISGTIVDKSGRTLSGQTGEGFVISVSHGEPLCIGLNCALGAAEMRPFIEIIGKCTTAYVLCYPNAGLPNTFGDYDETPSMMAKHLKDFAMDGLVNIVGGCCGSTPDHIREIAEAVKNCKPRVPPATAFEGHMLLSGLEPFRIGPYTNFVNIGERCNVAGSRKFAKLIMAGNYEEALCVAKVQVEMGAQVLDVNMDDGMLDGPSAMTRFCNLIASEPDIAKVPLCIDSSNFAVIEAGLKCCQGKCIVNSISLKEGEDDFLEKARKIKKYGAAMVVMAFDEEGQATETDTKIRVCTRAYHLLVKKLGFNPNDIIFDPNILTIGTGMEEHNLYAINFIHATKVIKETLPGARISGGLSNLSFSFRGMEAIREAMHGVFLYHAIKSGMDMGIVNAGNLPVYDDIHKELLQLCEDLIWNKDPEATEKLLRYAQTQGTGGKKVIQTDEWRNGPVEERLEYALVKGIEKHIIEDTEEARLNQKKYPRPLNIIEGPLMNGMKIVGDLFGAGKMFLPQVIKSARVMKKAVGHLIPFMEKEREETRVLNGTVEEEDPYQGTIVLATVKGDVHDIGKNIVGVVLGCNNFRVIDLGVMTPCDKILKAALDHKADIIGLSGLITPSLDEMIFVAKEMERLAIRIPLLIGGATTSKTHTAVKIAPRYSAPVIHVLDASKSVVVCSQLLDENLKDEYFEEIMEEYEDIRQDHYESLKERRYLPLSQARKSGFQMDWLSEPHPVKPTFIGTQVFEDYDLQKLVDYIDWKPFFDVWQLRGKYPNRGFPKIFNDKTVGGEARKVYDDAHNMLNTLISQKKLRARGVVGFWPAQSIQDDIHLYAEAAVPQAAEPIATFYGLRQQAEKDSASTEPYYCLSDFIAPLHSGIRDYLGLFAVACFGVEELSKAYEDDGDDYSSIMVKALGDRLAEAFAEELHERVRRELWAYCGSEQLDVADLRRLRYKGIRPAPGYPSQPDHTEKLTMWRLADIEQSTGIRLTESLAMAPASAVSGLYFSNLKSKYFAVGKISKDQVEDYALRKNISVAEVEKWLGPILGYDTD DEWSHL5 TD Primarily distributed in pancreas, heart, brain, skeletal muscle and placenta. Also expressed at lower levels in lung, liver and kidney. DEWSHL5 FC This enzyme catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. DEWSHL5 KD 33208: Metazoa DEWSHL5 PL 7711: Chordata DEWSHL5 CL 40674: Mammalia DEWSHL5 OD 9443: Primates DEWSHL5 FM 9604: Hominidae DEWSHL5 GE 9605: Homo DEWSHL5 SP 9606: Homo sapiens DEKN1H4 ID DEKN1H4 DEKN1H4 DN Retinal dehydrogenase 2 (ALDH1A2) DEKN1H4 GN ALDH1A2 DEKN1H4 SN Aldehyde dehydrogenase family 1 member A2; Retinaldehyde-specific dehydrogenase type 2; ALDH1A2; RALDH 2; RalDH2; RALDH(II); RALDH2 DEKN1H4 UC AL1A2_HUMAN DEKN1H4 RD NSC-122758 DEKN1H4 GI 8854 DEKN1H4 E1 1: Oxidoreductase DEKN1H4 E2 1.2: Aldehyde/oxo donor oxidoreductase DEKN1H4 E3 1.2.1: NAD/NADP acceptor oxidoreductase DEKN1H4 EC 1.2.1.36 DEKN1H4 RC RA biosynthesis pathway:R-HSA-5365859 DEKN1H4 KG Metabolic pathways:hsa01100; Retinol metabolism:hsa00830 DEKN1H4 PD 4X2Q; 6ALJ; 6B5G; 6B5H; 6B5I DEKN1H4 SQ MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS DEKN1H4 TD Low tissue/organ specificity. DEKN1H4 FC This enzyme converts retinaldehyde to retinoic acid. It recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. It can also metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal. DEKN1H4 KD 33208: Metazoa DEKN1H4 PL 7711: Chordata DEKN1H4 CL 40674: Mammalia DEKN1H4 OD 9443: Primates DEKN1H4 FM 9604: Hominidae DEKN1H4 GE 9605: Homo DEKN1H4 SP 9606: Homo sapiens DEIW03B ID DEIW03B DEIW03B DN NADH-ubiquinone oxidoreductase 20 kDa (NDUFS7) DEIW03B GN NDUFS7 DEIW03B SN NADH-ubiquinone oxidoreductase 20 kDa subunit; Mitochondrial NADH dehydrogenase [ubiquinone] iron-sulfur protein 7; Complex I-20kD; CI-20kD; NDUFS7; PSST subunit DEIW03B UC NDUS7_HUMAN DEIW03B RD Doxorubicin DEIW03B GI 374291 DEIW03B E1 7: Translocase DEIW03B E2 7.1: Hydron translocase DEIW03B E3 7.1.1: Hydron translocase DEIW03B EC 7.1.1.2 DEIW03B RC Complex I biogenesis:R-HSA-6799198; Respiratory electron transport:R-HSA-611105 DEIW03B KG Alzheimer's disease:hsa05010; Huntington's disease:hsa05016; Metabolic pathways:hsa01100; Non-alcoholic fatty liver disease (NAFLD):hsa04932; Oxidative phosphorylation:hsa00190; Parkinson's disease:hsa05012; Retrograde endocannabinoid signaling:hsa04723; Thermogenesis:hsa04714 DEIW03B PD 5XTB; 5XTD; 5XTH; 5XTI DEIW03B SQ MAVLSAPGLRGFRILGLRSSVGPAVQARGVHQSVATDGPSSTQPALPKARAVAPKPSSRGEYVVAKLDDLVNWARRSSLWPMTFGLACCAVEMMHMAAPRYDMDRFGVVFRASPRQSDVMIVAGTLTNKMAPALRKVYDQMPEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDIYIPGCPPTAEALLYGILQLQRKIKRERRLQIWYRR DEIW03B TD Primarily distributed in skeletal. DEIW03B FC This enzyme is the core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I).Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. DEIW03B KD 33208: Metazoa DEIW03B PL 7711: Chordata DEIW03B CL 40674: Mammalia DEIW03B OD 9443: Primates DEIW03B FM 9604: Hominidae DEIW03B GE 9605: Homo DEIW03B SP 9606: Homo sapiens DE5EO4Y ID DE5EO4Y DE5EO4Y DN Sucrase-isomaltase intestinal (SI) DE5EO4Y GN SI DE5EO4Y SN Intestinal sucrase-isomaltase; Isomaltase; Sucrase; SI DE5EO4Y UC SUIS_HUMAN DE5EO4Y RD M-7403 DE5EO4Y GI 6476 DE5EO4Y E1 3: Hydrolases DE5EO4Y E2 3.2: Glycosylase DE5EO4Y E3 3.2.1: O/S-glycosyl compound glycosidase DE5EO4Y EC 3.2.1.48 DE5EO4Y RC Digestion of dietary carbohydrate:R-HSA-189085; Intestinal saccharidase deficiencies:R-HSA-5659898 DE5EO4Y KG Carbohydrate digestion and absorption:hsa04973; Galactose metabolism:hsa00052; Metabolic pathways:hsa01100; Starch and sucrose metabolism:hsa00500 DE5EO4Y PD 3LPO; 3LPP DE5EO4Y SQ MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDSGKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMTTTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEFTGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISTRLPSDYIYGIGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSNAMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRWNYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQKYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNPNCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMYSKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAHWLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSRNHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHEFYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDMYLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDTIQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMNAHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGCVWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRVEVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRSSGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPPGYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGPTPEVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDIDYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVFVKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVDFYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEAEQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGDNYARWDNMDKSIIGMMEFSLFGMSYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNIANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKPTWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDTINLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLYLSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNEDTTNMILRIDLTTHNVTLEEPIEINWS DE5EO4Y TD Primarily distributed in intestine. DE5EO4Y FC This enzyme plays an important role in the final stage of carbohydrate digestion. It is specific for both alpha-1,4- and alpha-1,6-oligosaccharides. DE5EO4Y KD 33208: Metazoa DE5EO4Y PL 7711: Chordata DE5EO4Y CL 40674: Mammalia DE5EO4Y OD 9443: Primates DE5EO4Y FM 9604: Hominidae DE5EO4Y GE 9605: Homo DE5EO4Y SP 9606: Homo sapiens DE3Z1RA ID DE3Z1RA DE3Z1RA DN Pyridoxamine-phosphate oxidase (PNPO) DE3Z1RA GN PNPO DE3Z1RA SN Pyridoxine-5'-phosphate oxidase; Pyridoxaminephosphateoxidase; Pyridoxamine-phosphateoxidase; PNPO DE3Z1RA UC PNPO_HUMAN DE3Z1RA RD BST-4001 DE3Z1RA GI 55163 DE3Z1RA E1 1: Oxidoreductase DE3Z1RA E2 1.4: CH-NH2 donor oxidoreductase DE3Z1RA E3 1.4.3: Oxygen acceptor oxidoreductase DE3Z1RA EC 1.4.3.5 DE3Z1RA RC Vitamins B6 activation to pyridoxal phosphate:R-HSA-964975 DE3Z1RA KG Metabolic pathways:hsa01100; Vitamin B6 metabolism:hsa00750 DE3Z1RA PD 1NRG; 3HY8; 6H00 DE3Z1RA SQ MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTHRGEEDWLYERLAP DE3Z1RA TD Primarily distributed in liver. DE3Z1RA FC This enzyme catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). DE3Z1RA KD 33208: Metazoa DE3Z1RA PL 7711: Chordata DE3Z1RA CL 40674: Mammalia DE3Z1RA OD 9443: Primates DE3Z1RA FM 9604: Hominidae DE3Z1RA GE 9605: Homo DE3Z1RA SP 9606: Homo sapiens DEHX1DZ ID DEHX1DZ DEHX1DZ DN Lactoperoxidase (LPO) DEHX1DZ GN LPO DEHX1DZ SN Salivary peroxidase; Anionic isoperoxidase; Anionic peroxidase A1; LPO; SAPX; SPO DEHX1DZ UC PERL_HUMAN DEHX1DZ RD E-3A DEHX1DZ GI 4025 DEHX1DZ E1 1: Oxidoreductase DEHX1DZ E2 1.11: Peroxidase DEHX1DZ E3 1.11.1: Peroxidase DEHX1DZ EC 1.11.1.7 DEHX1DZ RC Events associated with phagocytolytic activity of PMN cells:R-HSA-8941413 DEHX1DZ KG Salivary secretion:hsa04970 DEHX1DZ SQ MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAMSSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLEVGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTPGKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSEYSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINALTSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTTARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAFVQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDENYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQPTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGLYGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDSLQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN DEHX1DZ TD Primarily distributed in salivary. DEHX1DZ FC This enzyme catalyzes the oxidation of a number of inorganic and organic substrates by hydrogen peroxide. These substrates include bromide and iodide and therefore lactoperoxidase can be categorised as a haloperoxidase. Another important substrate is thiocyanate. DEHX1DZ KD 33208: Metazoa DEHX1DZ PL 7711: Chordata DEHX1DZ CL 40674: Mammalia DEHX1DZ OD 9443: Primates DEHX1DZ FM 9604: Hominidae DEHX1DZ GE 9605: Homo DEHX1DZ SP 9606: Homo sapiens DEA742Z ID DEA742Z DEA742Z DN Cysteinyl-conjugate N-acetyltransferase (NAT8) DEA742Z GN NAT8 DEA742Z SN Acetyltransferase 2; Camello-like protein 1; GLA; N-acetyltransferase 8; ATase2; CCNAT; CML1; NAT8; TSC501 DEA742Z UC NAT8_HUMAN DEA742Z RD Acetyl-CoA DEA742Z GI 9027 DEA742Z E1 2: Transferase DEA742Z E2 2.3: Acyltransferase DEA742Z E3 2.3.1: Acyltransferase DEA742Z EC 2.3.1.80 DEA742Z RC Amyloid fiber formation:R-HSA-977225 DEA742Z KG Glutathione metabolism:hsa00480; Metabolic pathways:hsa01100 DEA742Z SQ MAPCHIRKYQESDRQWVVGLLSRGMAEHAPATFRQLLKLPRTLILLLGGPLALLLVSGSWLLALVFSISLFPALWFLAKKPWTEYVDMTLCTDMSDITKSYLSERGSCFWVAESEEKVVGMVGALPVDDPTLREKRLQLFHLFVDSEHRRQGIAKALVRTVLQFARDQGYSEVILDTGTIQLSAMALYQSMGFKKTGQSFFCVWARLVALHTVHFIYHLPSSKVGSL DEA742Z TD Primarily distributed in liver and kidney. DEA742Z FC This enzyme acetylates the free alpha-amino group of cysteine S-conjugates to form mercapturic acids. This is the final step in a major route for detoxification of a wide variety of reactive electrophiles which starts with their incorporation into glutathione S-conjugates. The glutathione S-conjugates are then further processed into cysteine S-conjugates and finally mercapturic acids which are water soluble and can be readily excreted in urine or bile. Alternatively, it may have a lysine N-acetyltransferase activity catalyzing peptidyl-lysine N6-acetylation of various proteins. DEA742Z KD 33208: Metazoa DEA742Z PL 7711: Chordata DEA742Z CL 40674: Mammalia DEA742Z OD 9443: Primates DEA742Z FM 9604: Hominidae DEA742Z GE 9605: Homo DEA742Z SP 9606: Homo sapiens DE7WS3H ID DE7WS3H DE7WS3H DN Aldo-keto reductase 1B1 (AKR1B1) DE7WS3H GN AKR1B1 DE7WS3H SN Aldo-keto reductase family 1 member B1; Aldose reductase; AKR1B1; ALR2; AR DE7WS3H UC ALDR_HUMAN DE7WS3H RD Brexanolone DE7WS3H GI 231 DE7WS3H E1 1: Oxidoreductase DE7WS3H E2 1.1: CH-OH donor oxidoreductase DE7WS3H E3 1.1.1: NAD/NADP oxidoreductase DE7WS3H EC 1.1.1.21 DE7WS3H RC Fructose biosynthesis:R-HSA-5652227; Pregnenolone biosynthesis:R-HSA-196108 DE7WS3H KG Folate biosynthesis:hsa00790; Fructose and mannose metabolism:hsa00051; Galactose metabolism:hsa00052; Glycerolipid metabolism:hsa00561; Metabolic pathways:hsa01100; Pentose and glucuronate interconversions:hsa00040 DE7WS3H PD 1AZ1; 1AZ2; 1EF3; 1EL3; 1IEI; 1MAR; 1PWL; 1PWM; 1T40 DE7WS3H SQ MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF DE7WS3H TD Primarily distributed in adrenal gland and seminal vesicle. DE7WS3H FC This enzyme catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. It displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosacharides, bile acids and xenobiotics substrates. It displays low enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis- retinal. It can also catalyzes the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2- (5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related phospholipid aldehydes that are generated from the oxydation of phosphotidylcholine and phosphatdyleethanolamides. Besides, it plays a role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls). DE7WS3H KD 33208: Metazoa DE7WS3H PL 7711: Chordata DE7WS3H CL 40674: Mammalia DE7WS3H OD 9443: Primates DE7WS3H FM 9604: Hominidae DE7WS3H GE 9605: Homo DE7WS3H SP 9606: Homo sapiens DEPVE0M ID DEPVE0M DEPVE0M DN Tryptophanyl-tRNA synthetase cytoplasmic (WARS1) DEPVE0M GN WARS1 DEPVE0M SN Interferon-induced protein 53; Cytoplasmic tryptophan--tRNA ligase; Tryptophanyl-tRNA synthetase; T1-TrpRS; T2-TrpRS; TrpRS; IFI53; IFP53; WARS; WARS1; WRS; hWRS DEPVE0M UC SYWC_HUMAN DEPVE0M RD TRP-01 DEPVE0M GI 7453 DEPVE0M E1 6: Ligase DEPVE0M E2 6.1: Carbon-oxygen ligase DEPVE0M E3 6.1.1: Aminoacyl tRNA synthetase DEPVE0M EC 6.1.1.2 DEPVE0M RC Cytosolic tRNA aminoacylation:R-HSA-379716 DEPVE0M KG Aminoacyl-tRNA biosynthesis:hsa00970 DEPVE0M PD 1O5T; 1R6T; 1R6U; 1ULH; 2AKE; 2QUJ; 2QUK; 5UJI; 5UJJ DEPVE0M SQ MPNSEPASLLELFNSIATQGELVRSLKAGNASKDEIDSAVKMLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQIFRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDVDVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQARRKEVTDEIVKEFMTPRKLSFDFQ DEPVE0M TD Primarily distributed in blood and thyroid gland. DEPVE0M FC This enzyme has aminoacylation activity while T2-TrpRS lacks it. DEPVE0M KD 33208: Metazoa DEPVE0M PL 7711: Chordata DEPVE0M CL 40674: Mammalia DEPVE0M OD 9443: Primates DEPVE0M FM 9604: Hominidae DEPVE0M GE 9605: Homo DEPVE0M SP 9606: Homo sapiens DER6XYF ID DER6XYF DER6XYF DN Tryptophan 5-hydroxylase 2 (TPH2) DER6XYF GN TPH2 DER6XYF SN Tryptophan 5-monooxygenase 2; Neuronal tryptophan hydroxylase; NTPH; TPH2 DER6XYF UC TPH2_HUMAN DER6XYF RD TRP-01 DER6XYF GI 121278 DER6XYF E1 1: Oxidoreductase DER6XYF E2 1.14: Oxygen paired donor oxidoreductase DER6XYF E3 1.14.16: Pteridine donor oxidoreductase DER6XYF EC 1.14.16.4 DER6XYF RC Serotonin and melatonin biosynthesis:R-HSA-209931 DER6XYF KG Folate biosynthesis:hsa00790; Metabolic pathways:hsa01100; Serotonergic synapse:hsa04726; Tryptophan metabolism:hsa00380 DER6XYF PD 4V06 DER6XYF SQ MQPAMMMFSSKYWARRGFSLDSAVPEEHQLLGSSTLNKPNSGKNDDKGNKGSSKREAATESGKTAVVFSLKNEVGGLVKALRLFQEKRVNMVHIESRKSRRRSSEVEIFVDCECGKTEFNELIQLLKFQTTIVTLNPPENIWTEEEELEDVPWFPRKISELDKCSHRVLMYGSELDADHPGFKDNVYRQRRKYFVDVAMGYKYGQPIPRVEYTEEETKTWGVVFRELSKLYPTHACREYLKNFPLLTKYCGYREDNVPQLEDVSMFLKERSGFTVRPVAGYLSPRDFLAGLAYRVFHCTQYIRHGSDPLYTPEPDTCHELLGHVPLLADPKFAQFSQEIGLASLGASDEDVQKLATCYFFTIEFGLCKQEGQLRAYGAGLLSSIGELKHALSDKACVKAFDPKTTCLQECLITTFQEAYFVSESFEEAKEKMRDFAKSITRPFSVYFNPYTQSIEILKDTRSIENVVQDLRSDLNTVCDALNKMNQYLGI DER6XYF TD Primarily distributed in brain. DER6XYF FC This enzyme catalyzes the rate-limiting step in 5-HT synthesis. DER6XYF KD 33208: Metazoa DER6XYF PL 7711: Chordata DER6XYF CL 40674: Mammalia DER6XYF OD 9443: Primates DER6XYF FM 9604: Hominidae DER6XYF GE 9605: Homo DER6XYF SP 9606: Homo sapiens DEDMWFX ID DEDMWFX DEDMWFX DN Keto-steroid reductase (HSD17B7) DEDMWFX GN HSD17B7 DEDMWFX SN Estradiol 17-beta-dehydrogenase 7; 17-beta-HSD 7; 17-beta-hydroxysteroid dehydrogenase 7; 3-keto-steroid reductase; Short chain dehydrogenase/reductase family 37C member 1; HSD17B7; SDR37C1; UNQ2563/PRO6243 DEDMWFX UC DHB7_HUMAN DEDMWFX RD Estrone DEDMWFX GI 51478 DEDMWFX E1 1: Oxidoreductase DEDMWFX E2 1.1: CH-OH donor oxidoreductase DEDMWFX E3 1.1.1: NAD/NADP oxidoreductase DEDMWFX EC 1.1.1.270 DEDMWFX RC Cholesterol biosynthesis:R-HSA-191273 DEDMWFX KG Metabolic pathways:hsa01100; Ovarian steroidogenesis:hsa04913; Steroid biosynthesis:hsa00100; Steroid hormone biosynthesis:hsa00140 DEDMWFX SQ MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIVQVDVSNLQSVFRASKELKQRFQRLDCIYLNAGIMPNPQLNIKALFFGLFSRKVIHMFSTAEGLLTQGDKITADGLQEVFETNVFGHFILIRELEPLLCHSDNPSQLIWTSSRSARKSNFSLEDFQHSKGKEPYSSSKYATDLLSVALNRNFNQQGLYSNVACPGTALTNLTYGILPPFIWTLLMPAILLLRFFANAFTLTPYNGTEALVWLFHQKPESLNPLIKYLSATTGFGRNYIMTQKMDLDEDTAEKFYQKLLELEKHIRVTIQKTDNQARLSGSCL DEDMWFX TD Primarily distributed in adrenal gland, liver, lung and thymus. DEDMWFX FC This enzyme is responsible for the reduction of the keto group on the C-3 of sterols. DEDMWFX KD 33208: Metazoa DEDMWFX PL 7711: Chordata DEDMWFX CL 40674: Mammalia DEDMWFX OD 9443: Primates DEDMWFX FM 9604: Hominidae DEDMWFX GE 9605: Homo DEDMWFX SP 9606: Homo sapiens DE8BVKA ID DE8BVKA DE8BVKA DN Indoleamine 2,3-dioxygenase 2 (IDO2) DE8BVKA GN IDO2 DE8BVKA SN Indoleamine 2,3-dioxygenase-like protein 1; Indoleamine-pyrrole 2,3-dioxygenase-like protein 1; IDO-2; IDO2; INDOL1 DE8BVKA UC I23O2_HUMAN DE8BVKA RD TRP-01 DE8BVKA GI 169355 DE8BVKA E1 1: Oxidoreductase DE8BVKA E2 1.13: Oxygen single donor oxidoreductase DE8BVKA E3 1.13.11: Oxygen single donor oxidoreductase DE8BVKA EC 1.13.11.52 DE8BVKA RC Tryptophan catabolism:R-HSA-71240 DE8BVKA KG African trypanosomiasis:hsa05143; Metabolic pathways:hsa01100; Tryptophan metabolism:hsa00380 DE8BVKA SQ MLHFHYYDTSNKIMEPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIANKLPQLIDAHQLQAHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEGEAQPAEVLPRNLALPFVEVSRNLGLPPILVHSDLVLTNWTKKDPDGFLEIGNLETIISFPGGESLHGFILVTALVEKEAVPGIKALVQATNAILQPNQEALLQALQRLRLSIQDITKTLGQMHDYVDPDIFYAGIRIFLSGWKDNPAMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSKESGDFLYRMRDYMPPSHKAFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALAELRSYHITMVTKYLITAAAKAKHGKPNHLPGPPQALKDRGTGGTAVMSFLKSVRDKTLESILHPRG DE8BVKA TD Primarily distributed in liver and placenta. DE8BVKA FC This enzyme catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. DE8BVKA KD 33208: Metazoa DE8BVKA PL 7711: Chordata DE8BVKA CL 40674: Mammalia DE8BVKA OD 9443: Primates DE8BVKA FM 9604: Hominidae DE8BVKA GE 9605: Homo DE8BVKA SP 9606: Homo sapiens DER0XCH ID DER0XCH DER0XCH DN Farnesol dehydrogenase (AKR1B15) DER0XCH GN AKR1B15 DER0XCH SN Aldo-keto reductase family 1 member B15; Testosterone 17beta-dehydrogenase; Estradiol 17-beta-dehydrogenase AKR1B15; AKR1B15 DER0XCH UC AK1BF_HUMAN DER0XCH RD Testosterone cypionate DER0XCH GI 441282 DER0XCH E1 1: Oxidoreductase DER0XCH E2 1.1: CH-OH donor oxidoreductase DER0XCH E3 1.1.1: NAD/NADP oxidoreductase DER0XCH EC 1.1.1.54 DER0XCH RC Estrogen biosynthesis:R-HSA-193144 DER0XCH SQ MATFVELSTKAKMPIVGLGTWRSLLGKVKEAVKVAIDAEYRHIDCAYFYENQHEVGEAIQEKIQEKAVMREDLFIVSKVWPTFFERPLVRKAFEKTLKDLKLSYLDVYLIHWPQGFKTGDDFFPKDDKGNMISGKGTFLDAWEAMEELVDEGLVKALGVSNFNHFQIERLLNKPGLKYKPVTNQVECHPYLTQEKLIQYCHSKGITVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHKKTTAQVLIRFHIQRNVTVIPKSMTPAHIVENIQVFDFKLSDEEMATILSFNRNWRAFDFKEFSHLEDFPFDAEY DER0XCH TD Primarily distributed in breast, placenta, testis and adipose tissue. DER0XCH FC This enzyme catalyzes the NADPH-dependent reduction of a variety of carbonyl substrates, like aromatic aldehydes, alkenals, ketones and alpha-dicarbonyl compounds. In addition, it catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta- hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It displays strong enzymatic activity toward all-trans- retinal and 9-cis-retinal and may play a physiological role in retinoid metabolism. DER0XCH KD 33208: Metazoa DER0XCH PL 7711: Chordata DER0XCH CL 40674: Mammalia DER0XCH OD 9443: Primates DER0XCH FM 9604: Hominidae DER0XCH GE 9605: Homo DER0XCH SP 9606: Homo sapiens DELTYX6 ID DELTYX6 DELTYX6 DN Alpha-L-iduronidase (IDUA) DELTYX6 GN IDUA DELTYX6 SN Iduronidase; L-iduronidase; Alpha iduronidase; Laronidase; IDUA DELTYX6 UC IDUA_HUMAN DELTYX6 RD Chondroitin sulfate DELTYX6 GI 3425 DELTYX6 E1 3: Hydrolases DELTYX6 E2 3.2: Glycosylase DELTYX6 E3 3.2.1: O/S-glycosyl compound glycosidase DELTYX6 EC 3.2.1.76 DELTYX6 RC CS/DS degradation:R-HSA-2024101; HS-GAG degradation:R-HSA-2024096; MPS I - Hurler syndrome:R-HSA-2206302 DELTYX6 KG Glycosaminoglycan degradation:hsa00531; Lysosome:hsa04142; Metabolic pathways:hsa01100 DELTYX6 PD 3W82; 4KGJ; 4KGL; 4KH2; 4MJ2; 4MJ4; 4OBR; 4OBS; 6I6R DELTYX6 SQ MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP DELTYX6 TD Low tissue/organ specificity. DELTYX6 FC This enzyme catalyses the hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate. DELTYX6 KD 33208: Metazoa DELTYX6 PL 7711: Chordata DELTYX6 CL 40674: Mammalia DELTYX6 OD 9443: Primates DELTYX6 FM 9604: Hominidae DELTYX6 GE 9605: Homo DELTYX6 SP 9606: Homo sapiens DE8RJ3F ID DE8RJ3F DE8RJ3F DN Hydroxyacid-oxoacid transhydrogenase (ADHFE1) DE8RJ3F GN ADHFE1 DE8RJ3F SN Fe-containing alcohol dehydrogenase; Alcohol dehydrogenase iron-containing protein 1; Mitochondrial hydroxyacid-oxoacid transhydrogenase; ADHFE1; HMFT2263; HOT DE8RJ3F UC HOT_HUMAN DE8RJ3F RD Sodium oxybate DE8RJ3F GI 137872 DE8RJ3F E1 1: Oxidoreductase DE8RJ3F E2 1.1: CH-OH donor oxidoreductase DE8RJ3F E3 1.1.99: CH-OH donor oxidoreductase DE8RJ3F EC 1.1.99.24 DE8RJ3F RC Interconversion of 2-oxoglutarate and 2-hydroxyglutarate:R-HSA-880009 DE8RJ3F SQ MAAAARARVAYLLRQLQRAACQCPTHSHTYSQAPGLSPSGKTTDYAFEMAVSNIRYGAAVTKEVGMDLKNMGAKNVCLMTDKNLSKLPPVQVAMDSLVKNGIPFTVYDNVRVEPTDSSFMEAIEFAQKGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVSAPIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKIGITSRAIKPTLGLIDPLHTLHMPARVVANSGFDVLCHALESYTTLPYHLRSPCPSNPITRPAYQGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSHMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASMKLY DE8RJ3F TD Primarily distributed in liver. DE8RJ3F FC This enzyme catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). D,L-3-hydroxyisobutyrate and L-3-hydroxybutyrate (L-3-OHB) are also substrates for HOT with 10-fold lower activities. DE8RJ3F KD 33208: Metazoa DE8RJ3F PL 7711: Chordata DE8RJ3F CL 40674: Mammalia DE8RJ3F OD 9443: Primates DE8RJ3F FM 9604: Hominidae DE8RJ3F GE 9605: Homo DE8RJ3F SP 9606: Homo sapiens DEDMAGE ID DEDMAGE DEDMAGE DN Brain form hexokinase (HK1) DEDMAGE GN HK1 DEDMAGE SN Hexokinase-A; Hexokinase type I; Hexokinase-1; HK I; HK1 DEDMAGE UC HXK1_HUMAN DEDMAGE RD D-glucose DEDMAGE GI 3098 DEDMAGE E1 2: Transferase DEDMAGE E2 2.7: Kinase DEDMAGE E3 2.7.1: Phosphotransferase DEDMAGE EC 2.7.1.1 DEDMAGE RC Defective HK1 causes hexokinase deficiency (HK deficiency):R-HSA-5619056; Glycolysis:R-HSA-70171 DEDMAGE KG Amino sugar and nucleotide sugar metabolism:hsa00520; Carbohydrate digestion and absorption:hsa04973; Carbon metabolism:hsa01200; Central carbon metabolism in cancer:hsa05230; Fructose and mannose metabolism:hsa00051; Galactose metabolism:hsa00052; Glycolysis / Gluconeogenesis:hsa00010; HIF-1 signaling pathway:hsa04066; Insulin signaling pathway:hsa04910; Metabolic pathways:hsa01100; Neomycin, kanamycin and gentamicin biosynthesis:hsa00524; Shigellosis:hsa05131; Starch and sucrose metabolism:hsa00500; Type II diabetes mellitus:hsa04930 DEDMAGE PD 1CZA; 1DGK; 1HKB; 1HKC; 1QHA; 4F9O; 4FOI; 4FPA; 4FPB DEDMAGE SQ MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDETLIDIMTRFRKEMKNGLSRDFNPTATVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVHMESEVYDTPENIVHGSGSQLFDHVAECLGDFMEKRKIKDKKLPVGFTFSFPCQQSKIDEAILITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQHCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDREIDRGSLNPGKQLFEKMVSGMYLGELVRLILVKMAKEGLLFEGRITPELLTRGKFNTSDVSAIEKNKEGLHNAKEILTRLGVEPSDDDCVSVQHVCTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTTVGVDGSLYKTHPQYSRRFHKTLRRLVPDSDVRFLLSESGSGKGAAMVTAVAYRLAEQHRQIEETLAHFHLTKDMLLEVKKRMRAEMELGLRKQTHNNAVVKMLPSFVRRTPDGTENGDFLALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYAIPIEIMQGTGEELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCQQTSLDAGILITWTKGFKATDCVGHDVVTLLRDAIKRREEFDLDVVAVVNDTVGTMMTCAYEEPTCEVGLIVGTGSNACYMEEMKNVEMVEGDQGQMCINMEWGAFGDNGCLDDIRTHYDRLVDEYSLNAGKQRYEKMISGMYLGEIVRNILIDFTKKGFLFRGQISETLKTRGIFETKFLSQIESDRLALLQVRAILQQLGLNSTCDDSILVKTVCGVVSRRAAQLCGAGMAAVVDKIRENRGLDRLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCNVSFLLSEDGSGKGAALITAVGVRLRTEASS DEDMAGE TD Primarily distributed in testis. DEDMAGE FC This enzyme catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6- phosphate, respectively) but does not phosphorylate N-acetyl-D-glucosamine. DEDMAGE KD 33208: Metazoa DEDMAGE PL 7711: Chordata DEDMAGE CL 40674: Mammalia DEDMAGE OD 9443: Primates DEDMAGE FM 9604: Hominidae DEDMAGE GE 9605: Homo DEDMAGE SP 9606: Homo sapiens DEE76VW ID DEE76VW DEE76VW DN Acetyl-CoA synthetase (ACSS2) DEE76VW GN ACSS2 DEE76VW SN Acetate--CoA ligase; Acetyl-CoA synthetase 1; Acetyl-coenzyme A synthetase, cytoplasmic; Acyl-CoA synthetase short-chain family member 2; Acyl-activating enzyme; Propionate--CoA ligase; ACAS2; ACS; ACSS2; AceCS; AceCS1 DEE76VW UC ACSA_HUMAN DEE76VW RD Sodium acetate DEE76VW GI 55902 DEE76VW E1 6: Ligase DEE76VW E2 6.2: Carbon-sulfur ligase DEE76VW E3 6.2.1: Acid-thiol ligase DEE76VW EC 6.2.1.1 DEE76VW RC Ethanol oxidation:R-HSA-71384; Transcriptional activation of mitochondrial biogenesis:R-HSA-2151201 DEE76VW KG Carbon metabolism:hsa01200; Glycolysis / Gluconeogenesis:hsa00010; Glyoxylate and dicarboxylate metabolism:hsa00630; Metabolic pathways:hsa01100; Propanoate metabolism:hsa00640; Pyruvate metabolism:hsa00620 DEE76VW SQ MGLPEERVRSGSGSRGQEEAGAGGRARSWSPPPEVSRSAHVPSLQRYRELHRRSVEEPREFWGDIAKEFYWKTPCPGPFLRYNFDVTKGKIFIEWMKGATTNICYNVLDRNVHEKKLGDKVAFYWEGNEPGETTQITYHQLLVQVCQFSNVLRKQGIQKGDRVAIYMPMIPELVVAMLACARIGALHSIVFAGFSSESLCERILDSSCSLLITTDAFYRGEKLVNLKELADEALQKCQEKGFPVRCCIVVKHLGRAELGMGDSTSQSPPIKRSCPDVQISWNQGIDLWWHELMQEAGDECEPEWCDAEDPLFILYTSGSTGKPKGVVHTVGGYMLYVATTFKYVFDFHAEDVFWCTADIGWITGHSYVTYGPLANGATSVLFEGIPTYPDVNRLWSIVDKYKVTKFYTAPTAIRLLMKFGDEPVTKHSRASLQVLGTVGEPINPEAWLWYHRVVGAQRCPIVDTFWQTETGGHMLTPLPGATPMKPGSATFPFFGVAPAILNESGEELEGEAEGYLVFKQPWPGIMRTVYGNHERFETTYFKKFPGYYVTGDGCQRDQDGYYWITGRIDDMLNVSGHLLSTAEVESALVEHEAVAEAAVVGHPHPVKGECLYCFVTLCDGHTFSPKLTEELKKQIREKIGPIATPDYIQNAPGLPKTRSGKIMRRVLRKIAQNDHDLGDMSTVADPSVISHLFSHRCLTIQ DEE76VW TD Primarily distributed in skeletal. DEE76VW FC This enzyme catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Acetate is the preferred substrate. And it can also utilize propionate with a much lower affinity. DEE76VW KD 33208: Metazoa DEE76VW PL 7711: Chordata DEE76VW CL 40674: Mammalia DEE76VW OD 9443: Primates DEE76VW FM 9604: Hominidae DEE76VW GE 9605: Homo DEE76VW SP 9606: Homo sapiens DE5NGOW ID DE5NGOW DE5NGOW DN Choline O-acetyltransferase (CHAT) DE5NGOW GN CHAT DE5NGOW SN Choline acetylase; CHOACTase; CHOACTASE; CMS1A; CMS1A2; CMS6; CHAT; ChAT DE5NGOW UC CLAT_HUMAN DE5NGOW RD Choline salicylate DE5NGOW GI 1103 DE5NGOW E1 2: Transferase DE5NGOW E2 2.3: Acyltransferase DE5NGOW E3 2.3.1: Acyltransferase DE5NGOW EC 2.3.1.6 DE5NGOW RC Acetylcholine Neurotransmitter Release Cycle:R-HSA-264642; Synthesis of PC:R-HSA-1483191 DE5NGOW KG Cholinergic synapse:hsa04725; Glycerophospholipid metabolism:hsa00564 DE5NGOW PD 2FY2; 2FY3; 2FY4; 2FY5 DE5NGOW SQ MGLRTAKKRGLGGGGKWKREEGGGTRGRREVRPACFLQSGGRGDPGDVGGPAGNPGCSPHPRAATRPPPLPAHTPAHTPEWCGAASAEAAEPRRAGPHLCIPAPGLTKTPILEKVPRKMAAKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSSYRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHVTQSSRKLIRADSVSELPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLKDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCKELPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLIDMRDLCSLLPPTESKPLATKEKATRPSQGHQP DE5NGOW TD Primarily distributed in brain and placenta. DE5NGOW FC This enzyme catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. DE5NGOW KD 33208: Metazoa DE5NGOW PL 7711: Chordata DE5NGOW CL 40674: Mammalia DE5NGOW OD 9443: Primates DE5NGOW FM 9604: Hominidae DE5NGOW GE 9605: Homo DE5NGOW SP 9606: Homo sapiens DEGSUI0 ID DEGSUI0 DEGSUI0 DN Xylosyl phosphatase (PXYLP1) DEGSUI0 GN PXYLP1 DEGSUI0 SN Acid phosphatase-like protein 2; Epididymis luminal protein 124; 2-phosphoxylose phosphatase 1; ACPL2; HEL124; PXYLP1; UNQ370/PRO706; XYLP DEGSUI0 UC PXYP1_HUMAN DEGSUI0 RD Riboflavin DEGSUI0 GI 92370 DEGSUI0 E1 3: Hydrolases DEGSUI0 E2 3.1: Ester bond hydrolase DEGSUI0 E3 3.1.1: Carboxylic ester hydrolase DEGSUI0 EC 3.1.3.2 DEGSUI0 SQ MLFRNRFLLLLALAALLAFVSLSLQFFHLIPVSTPKNGMSSKSRKRIMPDPVTEPPVTDPVYEALLYCNIPSVAERSMEGHAPHHFKLVSVHVFIRHGDRYPLYVIPKTKRPEIDCTLVANRKPYHPKLEAFISHMSKGSGASFESPLNSLPLYPNHPLCEMGELTQTGVVQHLQNGQLLRDIYLKKHKLLPNDWSADQLYLETTGKSRTLQSGLALLYGFLPDFDWKKIYFRHQPSALFCSGSCYCPVRNQYLEKEQRRQYLLRLKNSQLEKTYGEMAKIVDVPTKQLRAANPIDSMLCHFCHNVSFPCTRNGCVDMEHFKVIKTHQIEDERERREKKLYFGYSLLGAHPILNQTIGRMQRATEGRKEELFALYSAHDVTLSPVLSALGLSEARFPRFAARLIFELWQDREKPSEHSVRILYNGVDVTFHTSFCQDHHKRSPKPMCPLENLVRFVKRDMFVALGGSGTNYYDACHREGF DEGSUI0 TD Primarily distributed in spleen and fetal liver. Also expressed in placenta, pancreas, kidney, thymus and colon. DEGSUI0 FC This enzyme is responsible for the 2-O-dephosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature glycosaminoglycan (GAG) chains. DEGSUI0 KD 33208: Metazoa DEGSUI0 PL 7711: Chordata DEGSUI0 CL 40674: Mammalia DEGSUI0 OD 9443: Primates DEGSUI0 FM 9604: Hominidae DEGSUI0 GE 9605: Homo DEGSUI0 SP 9606: Homo sapiens DEDW5H6 ID DEDW5H6 DEDW5H6 DN Prostatic acid phosphatase (ACP3) DEDW5H6 GN ACP3 DEDW5H6 SN Thiamine monophosphatase; Acid phosphatase 3; TMPase; ACP3; ACPP; PAP; PAPf39 DEDW5H6 UC PPAP_HUMAN DEDW5H6 RD Riboflavin DEDW5H6 GI 55 DEDW5H6 E1 3: Hydrolases DEDW5H6 E2 3.1: Ester bond hydrolase DEDW5H6 E3 3.1.3: Phosphoric monoester hydrolase DEDW5H6 EC 3.1.3.2 DEDW5H6 RC Neutrophil degranulation:R-HSA-6798695 DEDW5H6 PD 1CVI; 1ND5; 1ND6; 2HPA; 2L3H; 2L77; 2L79; 2MG0; 3PPD DEDW5H6 SQ MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQGTEDSTD DEDW5H6 TD Primarily distributed in prostate, restricted toglandular and ductal epithelial cells. DEDW5H6 FC This enzyme dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. It has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma. DEDW5H6 KD 33208: Metazoa DEDW5H6 PL 7711: Chordata DEDW5H6 CL 40674: Mammalia DEDW5H6 OD 9443: Primates DEDW5H6 FM 9604: Hominidae DEDW5H6 GE 9605: Homo DEDW5H6 SP 9606: Homo sapiens DEQYXD4 ID DEQYXD4 DEQYXD4 DN Phosphorylcholine transferase A (PCYT1A) DEQYXD4 GN PCYT1A DEQYXD4 SN CTP:phosphocholine cytidylyltransferase A; Choline-phosphate cytidylyltransferase A; CCT-alpha; CCT A; CT A; CTPCT; PCYT1; PCYT1A DEQYXD4 UC PCY1A_HUMAN DEQYXD4 RD Lamivudine DEQYXD4 GI 5130 DEQYXD4 E1 2: Transferase DEQYXD4 E2 2.7: Kinase DEQYXD4 E3 2.7.7: Nucleotidyltransferase DEQYXD4 EC 2.7.7.15 DEQYXD4 RC Synthesis of PC:R-HSA-1483191 DEQYXD4 KG Choline metabolism in cancer:hsa05231; Glycerophospholipid metabolism:hsa00564; Metabolic pathways:hsa01100; Phosphonate and phosphinate metabolism:hsa00440 DEQYXD4 SQ MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYDISEDEED DEQYXD4 TD Low tissue/organ specificity. DEQYXD4 FC This enzyme controls phosphatidylcholine synthesis. DEQYXD4 KD 33208: Metazoa DEQYXD4 PL 7711: Chordata DEQYXD4 CL 40674: Mammalia DEQYXD4 OD 9443: Primates DEQYXD4 FM 9604: Hominidae DEQYXD4 GE 9605: Homo DEQYXD4 SP 9606: Homo sapiens DEL87ZT ID DEL87ZT DEL87ZT DN Choline/ethanolaminephosphotransferase 1 (CEPT1) DEL87ZT GN CEPT1 DEL87ZT SN Aminoalcohol phosphotransferase 1; Choline/ethanolamine phosphotransferase 1; CEPT1; PRO1101; hCEPT1 DEL87ZT UC CEPT1_HUMAN DEL87ZT RD Choline salicylate DEL87ZT GI 10390 DEL87ZT E1 2: Transferase DEL87ZT E2 2.7: Kinase DEL87ZT E3 2.7.8: Phosphotransferase DEL87ZT EC 2.7.8.1 DEL87ZT RC Synthesis of PC:R-HSA-1483191; Synthesis of PE:R-HSA-1483213 DEL87ZT KG Ether lipid metabolism:hsa00565; Glycerophospholipid metabolism:hsa00564; Metabolic pathways:hsa01100; Phosphonate and phosphinate metabolism:hsa00440 DEL87ZT SQ MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAGRSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYIACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPDWMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIPVLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLAAMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLDQYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH DEL87ZT TD Low tissue/organ specificity. DEL87ZT FC This enzyme catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. It is involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. It has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity. DEL87ZT KD 33208: Metazoa DEL87ZT PL 7711: Chordata DEL87ZT CL 40674: Mammalia DEL87ZT OD 9443: Primates DEL87ZT FM 9604: Hominidae DEL87ZT GE 9605: Homo DEL87ZT SP 9606: Homo sapiens DER6BCE ID DER6BCE DER6BCE DN Acid phosphatase-like protein 1 (ACP6) DER6BCE GN ACP6 DER6BCE SN Lysophosphatidic acid phosphatase type 6; Acid phosphatase 6 lysophosphatidic; ACP6; ACPL1; LPAP; PACPL1; UNQ205/PRO231 DER6BCE UC PPA6_HUMAN DER6BCE RD Riboflavin DER6BCE GI 51205 DER6BCE E1 3: Hydrolases DER6BCE E2 3.1: Ester bond hydrolase DER6BCE E3 3.1.3: Phosphoric monoester hydrolase DER6BCE EC 3.1.3.2 DER6BCE RC Synthesis of PA:R-HSA-1483166 DER6BCE PD 4JOB; 4JOC; 4JOD DER6BCE SQ MITGVFSMRLWTPVGVLTSLAYCLHQRRVALAELQEADGQCPVDRSLLKLKMVQVVFRHGARSPLKPLPLEEQVEWNPQLLEVPPQTQFDYTVTNLAGGPKPYSPYDSQYHETTLKGGMFAGQLTKVGMQQMFALGERLRKNYVEDIPFLSPTFNPQEVFIRSTNIFRNLESTRCLLAGLFQCQKEGPIIIHTDEADSEVLYPNYQSCWSLRQRTRGRRQTASLQPGISEDLKKVKDRMGIDSSDKVDFFILLDNVAAEQAHNLPSCPMLKRFARMIEQRAVDTSLYILPKEDRESLQMAVGPFLHILESNLLKAMDSATAPDKIRKLYLYAAHDVTFIPLLMTLGIFDHKWPPFAVDLTMELYQHLESKEWFVQLYYHGKEQVPRGCPDGLCPLDMFLNAMSVYTLSPEKYHALCSQTQVMEVGNEE DER6BCE TD Primarily distributed in kidney, heart, small intestine,muscle, liver, prostate, testis and ovary. DER6BCE FC This enzyme hydrolyzes lysophosphatidic acid (LPA) containing a medium length fatty acid chain to the corresponding monoacylglycerol. It has highest activity with lysophosphatidic acid containing myristate (C14:0), monounsaturated oleate (C18:1) or palmitate (C16:0), and lower activity with C18:0 and C6:0 lysophosphatidic acid. DER6BCE KD 33208: Metazoa DER6BCE PL 7711: Chordata DER6BCE CL 40674: Mammalia DER6BCE OD 9443: Primates DER6BCE FM 9604: Hominidae DER6BCE GE 9605: Homo DER6BCE SP 9606: Homo sapiens DEBQ2WU ID DEBQ2WU DEBQ2WU DN Uridine phosphorylase 2 (UPP2) DEBQ2WU GN UPP2 DEBQ2WU SN Pyrimidine nucleoside phosphorylase 2; Uridinephosphorylase 2; UrdPase 2; UPase 2; UPP2 DEBQ2WU UC UPP2_HUMAN DEBQ2WU RD Fluorouracilo DEBQ2WU GI 151531 DEBQ2WU E1 2: Transferase DEBQ2WU E2 2.4: Glycosyltransferases DEBQ2WU E3 2.4.2: Pentosyltransferase DEBQ2WU EC 2.4.2.3 DEBQ2WU RC Pyrimidine catabolism:R-HSA-73621; Pyrimidine salvage:R-HSA-73614 DEBQ2WU KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DEBQ2WU PD 2XRF; 3P0E; 3P0F DEBQ2WU SQ MASVIPASNRSMRSDRNTYVGKRFVHVKNPYLDLMDEDILYHLDLGTKTHNLPAMFGDVKFVCVGGSPNRMKAFALFMHKELGFEEAEEDIKDICAGTDRYCMYKTGPVLAISHGMGIPSISIMLHELIKLLHHARCCDVTIIRIGTSGGIGIAPGTVVITDIAVDSFFKPRFEQVILDNIVTRSTELDKELSEELFNCSKEIPNFPTLVGHTMCTYDFYEGQGRLDGALCSFSREKKLDYLKRAFKAGVRNIEMESTVFAAMCGLCGLKAAVVCVTLLDRLDCDQINLPHDVLVEYQQRPQLLISNFIRRRLGLCD DEBQ2WU TD Primarily distributed in kidney and liver. DEBQ2WU FC This enzyme catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. It shows substrate specificity and accepts uridine, deoxyuridine, and thymidine as well as the two pyrimidine nucleoside analogs 5-fluorouridine and 5-fluoro-2(')-deoxyuridine as substrates. DEBQ2WU KD 33208: Metazoa DEBQ2WU PL 7711: Chordata DEBQ2WU CL 40674: Mammalia DEBQ2WU OD 9443: Primates DEBQ2WU FM 9604: Hominidae DEBQ2WU GE 9605: Homo DEBQ2WU SP 9606: Homo sapiens DEXVHDB ID DEXVHDB DEXVHDB DN Friedreich ataxia protein (FXN) DEXVHDB GN FXN DEXVHDB SN Frataxin intermediate form; Frataxin mature form; Frataxin(56-210); Frataxin(78-210); Frataxin(81-210); Frataxin, mitochondrial; X25; d-FXN; i-FXN; m56-FXN; m78-FXN; FRDA; FXN; Fxn; m81-FXN DEXVHDB UC FRDA_HUMAN DEXVHDB RD Ferrum metallicum DEXVHDB GI 2395 DEXVHDB E1 1: Oxidoreductase DEXVHDB E2 1.16: Metal ion oxidoreductase DEXVHDB E3 1.16.3: Oxygen acceptor oxidoreductase DEXVHDB EC 1.16.3.1 DEXVHDB RC Mitochondrial iron-sulfur cluster biogenesis:R-HSA-1362409; Mitochondrial protein import:R-HSA-1268020 DEXVHDB KG Porphyrin and chlorophyll metabolism:hsa00860 DEXVHDB PD 3S4M; 3S5D; 3S5E; 3S5F; 3T3J; 3T3K; 3T3L; 3T3T; 3T3X DEXVHDB SQ MWTLGRRAVAGLLASPSPAQAQTLTRVPRPAELAPLCGRRGLRTDIDATCTPRRASSNQRGLNQIWNVKKQSVYLMNLRKSGTLGHPGSLDETTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSGKDA DEXVHDB TD Primarily distributed in heart, peripheral blood lymphocytes and dermal fibroblasts. DEXVHDB FC This enzyme promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. It may play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. It may be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization. DEXVHDB KD 33208: Metazoa DEXVHDB PL 7711: Chordata DEXVHDB CL 40674: Mammalia DEXVHDB OD 9443: Primates DEXVHDB FM 9604: Hominidae DEXVHDB GE 9605: Homo DEXVHDB SP 9606: Homo sapiens DECH1VP ID DECH1VP DECH1VP DN Bleomycin hydrolase (BLMH) DECH1VP GN BLMH DECH1VP SN BLM hydrolase; Reactive electrophile homocysteine thiolactone hydrolase; BH; BLMH; BMH DECH1VP UC BLMH_HUMAN DECH1VP RD Bleomycin DECH1VP GI 642 DECH1VP E1 3: Hydrolases DECH1VP E2 3.4: Peptidase DECH1VP E3 3.4.22: Cysteine protease DECH1VP EC 3.4.22.40 DECH1VP RC Antigen processing-Ubiquitination & Proteasome degradation:R-HSA-983168 DECH1VP PD 1CB5; 2CB5 DECH1VP SQ MSSSGLNSEKVAALIQKLNSDPQFVLAQNVGTTHDLLDICLKRATVQRAQHVFQHAVPQEGKPITNQKSSGRCWIFSCLNVMRLPFMKKLNIEEFEFSQSYLFFWDKVERCYFFLSAFVDTAQRKEPEDGRLVQFLLMNPANDGGQWDMLVNIVEKYGVIPKKCFPESYTTEATRRMNDILNHKMREFCIRLRNLVHSGATKGEISATQDVMMEEIFRVVCICLGNPPETFTWEYRDKDKNYQKIGPITPLEFYREHVKPLFNMEDKICLVNDPRPQHKYNKLYTVEYLSNMVGGRKTLYNNQPIDFLKKMVAASIKDGEAVWFGCDVGKHFNSKLGLSDMNLYDHELVFGVSLKNMNKAERLTFGESLMTHAMTFTAVSEKDDQDGAFTKWRVENSWGEDHGHKGYLCMTDEWFSEYVYEVVVDRKHVPEEVLAVLEQEPIILPAWDPMGALAE DECH1VP TD Primarily distributed in skin. DECH1VP FC This enzyme catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity. DECH1VP KD 33208: Metazoa DECH1VP PL 7711: Chordata DECH1VP CL 40674: Mammalia DECH1VP OD 9443: Primates DECH1VP FM 9604: Hominidae DECH1VP GE 9605: Homo DECH1VP SP 9606: Homo sapiens DEIOH6A ID DEIOH6A DEIOH6A DN Alcohol dehydrogenase class-III (ADH5) DEIOH6A GN ADH5 DEIOH6A SN Alcohol dehydrogenase 5; Alcohol dehydrogenase class chi chain; Alcohol dehydrogenase class-3; Glutathione-dependent formaldehyde dehydrogenase; S-(hydroxymethyl)glutathione dehydrogenase; ADH5; ADHX; FALDH; FDH; GSH-FDH DEIOH6A UC ADHX_HUMAN DEIOH6A RD Polyethylene glycol 400 DEIOH6A GI 128 DEIOH6A E1 1: Oxidoreductase DEIOH6A E2 1.1: CH-OH donor oxidoreductase DEIOH6A E3 1.1.1: NAD/NADP oxidoreductase DEIOH6A EC 1.1.1.1 DEIOH6A RC Ethanol oxidation:R-HSA-71384 DEIOH6A KG Carbon metabolism:hsa01200; Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Fatty acid degradation:hsa00071; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Tyrosine metabolism:hsa00350 DEIOH6A PD 1M6H; 1M6W; 1MA0; 1MC5; 1MP0; 1TEH; 2FZE; 2FZW; 3QJ5 DEIOH6A SQ MANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFELMHSGKSIRTVVKI DEIOH6A TD Low tissue/organ specificity. DEIOH6A FC This enzyme catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione, and oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. DEIOH6A KD 33208: Metazoa DEIOH6A PL 7711: Chordata DEIOH6A CL 40674: Mammalia DEIOH6A OD 9443: Primates DEIOH6A FM 9604: Hominidae DEIOH6A GE 9605: Homo DEIOH6A SP 9606: Homo sapiens DEEN9RD ID DEEN9RD DEEN9RD DN Alcohol dehydrogenase class-I beta (ADH1B) DEEN9RD GN ADH1B DEEN9RD SN Alcohol dehydrogenase 1B; Alcohol dehydrogenase subunit beta; All-trans-retinol dehydrogenase [NAD(+)] ADH1B; ADH1B; ADH2 DEEN9RD UC ADH1B_HUMAN DEEN9RD RD Ethanol DEEN9RD GI 125 DEEN9RD E1 1: Oxidoreductase DEEN9RD E2 1.1: CH-OH donor oxidoreductase DEEN9RD E3 1.1.1: NAD/NADP oxidoreductase DEEN9RD EC 1.1.1.105 DEEN9RD RC Ethanol oxidation:R-HSA-71384 DEEN9RD KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Fatty acid degradation:hsa00071; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Tyrosine metabolism:hsa00350 DEEN9RD PD 1DEH; 1HDX; 1HDY; 1HDZ; 1HSZ; 1HTB; 1U3U; 1U3V; 3HUD DEEN9RD SQ MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTVLTF DEEN9RD TD Primarily distributed in adipose tissue and liver. DEEN9RD FC This enzyme catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate to retinoid metabolism. In vitro it can also catalyzes the NADH-dependent reduction of all-trans- retinal and its derivatives such as all-trans-4-oxoretinal. DEEN9RD KD 33208: Metazoa DEEN9RD PL 7711: Chordata DEEN9RD CL 40674: Mammalia DEEN9RD OD 9443: Primates DEEN9RD FM 9604: Hominidae DEEN9RD GE 9605: Homo DEEN9RD SP 9606: Homo sapiens DELNBKF ID DELNBKF DELNBKF DN Glutamate racemase (MurI) DELNBKF GN murI DELNBKF SN D-glutamate racemase; MurI; murI; BAS0806; BAS4379; BcGR; BsGR; BsRacE; DapF; FnGR; GBAA_0847; GBAA_4717; JW5550; b3967; dga; glr; yijA DELNBKF UC MURI_ECOLI DELNBKF RD L-glutamine DELNBKF GI 948467 DELNBKF E1 5: Isomerase DELNBKF E2 5.1: Racemase/epimerase DELNBKF E3 5.1.1: Amino acid racemase/epimerase DELNBKF EC 5.1.1.3 DELNBKF KG D-Glutamine and D-glutamate metabolism:ecj00471; Metabolic pathways:ecj01100 DELNBKF PD 2JFN DELNBKF SQ MATKLQDGNTPCLAATPSEPRPTVLVFDSGVGGLSVYDEIRHLLPDLHYIYAFDNVAFPYGEKSEAFIVERVVAIVTAVQERYPLALAVVACNTASTVSLPALREKFDFPVVGVVPAIKPAARLTANGIVGLLATRGTVKRSYTHELIARFANECQIEMLGSAEMVELAEAKLHGEDVSLDALKRILRPWLRMKEPPDTVVLGCTHFPLLQEELLQVLPEGTRLVDSGAAIARRTAWLLEHEAPDAKSADANIAFCMAMTPGAEQLLPVLQRYGFETLEKLAVLG DELNBKF TD Primarily distributed in human gut. DELNBKF FC This enzyme is a pyridoxal-phosphate protein providing the (R)-glutamate required for cell wall biosynthesis and converting L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine. DELNBKF KD 2: Bacteria DELNBKF PL 1224: Proteobacteria DELNBKF CL 1236: Gammaproteobacteria DELNBKF OD 91347: Enterobacterales DELNBKF FM 543: Enterobacteriaceae DELNBKF GE 561: Escherichia DELNBKF SP 562: Escherichia coli DELNBKF SU Escherichia coli K-12 DERQ6GA ID DERQ6GA DERQ6GA DN Glutamate decarboxylase (gadB) DERQ6GA GN gadB DERQ6GA SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; GAD-beta; JW1488; b1493 DERQ6GA UC DCEB_ECOLI DERQ6GA RD L-glutamine DERQ6GA GI 946058 DERQ6GA E1 4: Lyases DERQ6GA E2 4.1: Carbon-carbon lyase DERQ6GA E3 4.1.1: Carboxy-lyase DERQ6GA EC 4.1.1.15 DERQ6GA KG Alanine, aspartate and glutamate metabolism:ecj00250; Biosynthesis of secondary metabolites:ecj01110; Butanoate metabolism:ecj00650; Metabolic pathways:ecj01100; Microbial metabolism in diverse environments:ecj01120; Quorum sensing:ecj02024; Taurine and hypotaurine metabolism:ecj00430; beta-Alanine metabolism:ecj00410 DERQ6GA PD 1PMM; 1PMO; 2DGK; 2DGL; 2DGM; 3FZ6; 3FZ7; 3FZ8 DERQ6GA SQ MDKKQVTDLRSELLDSRFGAKSISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT DERQ6GA TD Primarily distributed in human gut. DERQ6GA FC This enzyme converts glutamate to gamma-aminobutyrate (GABA). The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DERQ6GA KD 2: Bacteria DERQ6GA PL 1224: Proteobacteria DERQ6GA CL 1236: Gammaproteobacteria DERQ6GA OD 91347: Enterobacterales DERQ6GA FM 543: Enterobacteriaceae DERQ6GA GE 561: Escherichia DERQ6GA SP 562: Escherichia coli DEAMEF2 ID DEAMEF2 DEAMEF2 DN NADH dehydrogenase (nuoE) DEAMEF2 GN nuoE DEAMEF2 SN DPNH-menadione reductase; FMN-dependent NADH-quinone reductase; D-diaphorase; Reduced nicotinamide adenine dinucleotide (quinone); FMN-dependent NADH:quinone oxidoreductase; H+(NA+)-translocating NADH-quinone oxidoreductase; NADH-dependent 1,4-benzoquinone reductase; NADH-Q oxidoreductase; NADH dehydrogenase subunit E; nuoE DEAMEF2 UC J9VB37_9ACTN DEAMEF2 RD Doxorubicin DEAMEF2 E1 1: Oxidoreductase DEAMEF2 E2 1.6: NADH/NADPH oxidoreductase DEAMEF2 E3 1.6.5: Quinone acceptor oxidoreductase DEAMEF2 EC 1.6.5.11 DEAMEF2 SQ MTDGQTSLGMPQLPAPDYPAEVRARLEADAEEIIARYPGSRSALLPLLHLVQSEEGHVTRTGMKFCAEILGLTTAEVTAVATFYTMYRRKPSGDYQVGVCTNTLCAVMGGDAIFEELKEHLGVGNNETTEDGKVTLEHIECNAACDFAPVVMVNWEFFDNQTPDSAKKIVDDLRAGRPVEPTRGAPLCTYKETARILAGFPDEREGAVEATGGAGPASLVGLRLAKGETPHHKIVHPRGESASGEGE DEAMEF2 TD Primarily distributed in human gut. DEAMEF2 FC This enzyme is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. DEAMEF2 KD 2: Bacteria DEAMEF2 PL 201174: Actinobacteria DEAMEF2 CL 1760: Actinobacteria DEAMEF2 OD 85011: Streptomycetales DEAMEF2 FM 2062: Streptomycetaceae DEAMEF2 GE 1883: Streptomyces DEAMEF2 SP 1911: Streptomyces griseus DEME01W ID DEME01W DEME01W DN Molybdopterin-dependent enzyme (molD) DEME01W GN molD DEME01W SN Molybdopterin-dependent oxidoreductase; Oxidoreductase molD; molD DEME01W UC A0A327UAE0_9ACTN DEME01W RD Doxorubicin DEME01W E1 1: Oxidoreductase DEME01W E2 1.1: CH-OH donor oxidoreductase DEME01W E3 1.1.1: NAD/NADP oxidoreductase DEME01W EC 1.1.1.40 DEME01W SQ MNPPEEDPGTPEPRIGPVPEKKPAFRPYHHPAAGWGAAKSVTRFLTKERELIDGPRAIAKMNHENGGFDCPGCAWPDDIKGLKLDICENGIKHVTWEMTRKRVGREFFAAHSVSELSGWSDFRLEDQGRLTEPMVYDPESDHYEPISWKDAFELVGRTLRGLDSPHQASFYTSGRLGNEATFLYQLWARELGTNNLPDCSNMCHEASGRALQAALGTGKGTCDLKDWESADALFIMGVNAASNAPRMLTALAEAYRRGAQVVHVNPLVEAAATRTIIPHDIADMAMFKSTRTSTLNLQVRIGGDMAFLRGVAKAVLKQAETDPKALDREFIDRYTDGFDAYRALCEATGWDEIERQSGLSRDAVLAAARVYGEADRSIISWCLGVTQHDHGVDTIREIVNVLLLRGNLGREGAGPSPVRGHSNVQGNRTCGINHRPPEEFLDRLADACGIEPPREHGLDTVGTIRAMHDGDVKVFVGMGGNFALAAPDTPYTYEALRNCDLTVQVSTKLNRSHLVHGRAALILPCLGRTEKDEQRAGLQSTSVEDSMSMVHLSVGMKRPASRHLLSEPAIIAGMARATLPGSSTPWEWYVEDYDRIRDSMARVVEGFEDCNRRVRLPLGFRIRQPARELVFMTESGRAEFSTAPLPDVVPEPGTLALGTMRSHDQWNTTIYSDDDRYRGITNLRTLVFMNKDDMRERGVEEFGPVDITSTARDGSRRRVEGYLAVPYDIPRGCAAGYMPEMNVLCALVDYSTQSDQPLMKHVKVTITPSG DEME01W TD Primarily distributed in human gut. DEME01W FC This enzyme catalyzes the conversion of doxorubicin to 7-deoxydoxorubicinol and 7-deoxydoxorubicinolone via a reductive deglycosylation mechanism. DEME01W KD 2: Bacteria DEME01W PL 1224: Proteobacteria DEME01W CL 1236: Gammaproteobacteria DEME01W OD 91347: Enterobacterales DEME01W FM 543: Enterobacteriaceae DEME01W GE 561: Escherichia DEME01W SP 562: Escherichia coli DEME01W SU Escherichia coli BW25113 DECNUXP ID DECNUXP DECNUXP DN Glutamate racemase (MurI) DECNUXP GN murI DECNUXP SN D-glutamate racemase; MurI; murI; BAS0806; BAS4379; BcGR; BsGR; BsRacE; DapF; FnGR; GBAA_0847; GBAA_4717; SMU_1718 DECNUXP UC MURI_STRMU DECNUXP RD L-glutamine DECNUXP GI 1028943 DECNUXP E1 5: Isomerase DECNUXP E2 5.1: Racemase/epimerase DECNUXP E3 5.1.1: Amino acid racemase/epimerase DECNUXP EC 5.1.1.3 DECNUXP KG D-Glutamine and D-glutamate metabolism:smu00471; Metabolic pathways:smu01100 DECNUXP SQ MDNRPIGFLDSGVGGLTVVRELMRQLPHEEVIYIGDSARAPYGPRPAKQIKTYTWELVNFLLTKKVKMIVFACNTATAVVWEEVKEKLDIPVLGVILPGSSAAIKSTISGQIGIIGTPMTIKSNIYEQKIRDLSPQMKVRSLACPKFVPIVESNKMNSSVAKKIVYESLSPLVGKIDTLVLGCTHYPLLRPIIQNVMGPDVELIDSGAECVRDISVLLNYFDLNRSRTSKVLHHRFYTTASVASFKEIASDWLPLAIEVEHVTL DECNUXP TD Primarily distributed in human oral cavity. DECNUXP FC This enzyme is a pyridoxal-phosphate protein providing the (R)-glutamate required for cell wall biosynthesis and converting L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine. DECNUXP KD 2: Bacteria DECNUXP PL 1239: Firmicutes DECNUXP CL 91061: Bacilli DECNUXP OD 186826: Lactobacillales DECNUXP FM 1300: Streptococcaceae DECNUXP GE 1301: Streptococcus DECNUXP SP 1309: Streptococcus mutans DEFADPU ID DEFADPU DEFADPU DN Methionine-R-sulfoxide reductase B1 (MSRB1) DEFADPU GN MSRB1 DEFADPU SN Selenoprotein X; Methionine-sulfoxide reductase B1; Reductase methionine-sulfoxide B1; HSPC270; MSRB1; MsrB1; SEPX1; SelX DEFADPU UC MSRB1_HUMAN DEFADPU RD Methionine DEFADPU GI 51734 DEFADPU E1 1: Oxidoreductase DEFADPU E2 1.8: Sulfur donor oxidoreductase DEFADPU E3 1.8.4: Disulfide acceptor oxidoreductase DEFADPU EC 1.8.4.12 DEFADPU RC Protein repair:R-HSA-5676934 DEFADPU PD 3MAO DEFADPU SQ MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVSCGKCGNGLGHEFLNDGPKPGQSRFUIFSSSLKFVPKGKETSASQGH DEFADPU TD Primarily distributed in blood, liver and pancreas. DEFADPU FC This enzyme specifically reduces methionine (R)-sulfoxide back to methionine. DEFADPU KD 33208: Metazoa DEFADPU PL 7711: Chordata DEFADPU CL 40674: Mammalia DEFADPU OD 9443: Primates DEFADPU FM 9604: Hominidae DEFADPU GE 9605: Homo DEFADPU SP 9606: Homo sapiens DE82GV7 ID DE82GV7 DE82GV7 DN NADPH-dependent oxidoreductase (nfrA) DE82GV7 GN nfrA DE82GV7 SN NADPH-dependent FMN and FAD-containing oxidoreductase; Novel reductase 1; SAOUHSC_00366; nfrA DE82GV7 UC NRFA_STAA8 DE82GV7 RD Riboflavin DE82GV7 GI 3919785 DE82GV7 E1 1: Oxidoreductase DE82GV7 E2 1.6: NADH/NADPH oxidoreductase DE82GV7 E3 1.6.5: Quinone acceptor oxidoreductase DE82GV7 EC 1.6.5.2 DE82GV7 KG Metabolic pathways:sao01100; Riboflavin metabolism:sao00740 DE82GV7 SQ MSEHVYNLVKKHHSVRKFKNKPLSEDVVKKLVEAGQSASTSSFLQAYSIIGIDDEKIKENLREVSGQPYVVENGYLFVFVIDYYRHHLVDQHAETDMENAYGSTEGLLVGAIDAALVAENIAVTAEDMGYGIVFLGSLRNDVERVREILDLPDYVFPVFGMAVGEPADDENGAAKPRLPFDHVFHHNKYHADKETQYAQMADYDQTISEYYDQRTNGNRKETWSQQIEMFLGNKARLDMLEQLQKSGLIQR DE82GV7 TD Primarily distributed in human gut. DE82GV7 FC This enzyme reduces FMN, organic nitro compounds and disulfide DTNB. And it is involved in maintenance of the cellular redox state and the disulfide stress response. DE82GV7 KD 2: Bacteria DE82GV7 PL 1239: Firmicutes DE82GV7 CL 91061: Bacilli DE82GV7 OD 1385: Bacillales DE82GV7 FM 90964: Staphylococcaceae DE82GV7 GE 1279: Staphylococcus DE82GV7 SP 1280: Staphylococcus aureus DEVOTU4 ID DEVOTU4 DEVOTU4 DN Aquaporin adipose (AQP7) DEVOTU4 GN AQP7 DEVOTU4 SN Aquaglyceroporin-7; Aquaporin-7; Aquaporin-7-like; AQP-7; AQP7; AQP7L; AQP9; AQPap DEVOTU4 UC AQP7_HUMAN DEVOTU4 RD Glycerol DEVOTU4 GI 364 DEVOTU4 E1 3: Hydrolases DEVOTU4 E2 3.1: Ester bond hydrolase DEVOTU4 E3 3.1.1: Carboxylic ester hydrolase DEVOTU4 EC 3.1.1.- DEVOTU4 RC Passive transport by Aquaporins:R-HSA-432047; Transport of glycerol from adipocytes to the liver by Aquaporins:R-HSA-432030 DEVOTU4 KG PPAR signaling pathway:hsa03320; Regulation of lipolysis in adipocytes:hsa04923 DEVOTU4 PD 6KXW; 6N1G; 6QZI; 6QZJ DEVOTU4 SQ MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF DEVOTU4 TD Primarily distributed in adipose tissue, breast and heart muscle. DEVOTU4 FC This enzyme functions as important facilitator of glycerol transport across the cell membrane and modulators in controlling the metabolism of glycerol, contributing to the pathophysiology of obesity and diabetes. DEVOTU4 KD 33208: Metazoa DEVOTU4 PL 7711: Chordata DEVOTU4 CL 40674: Mammalia DEVOTU4 OD 9443: Primates DEVOTU4 FM 9604: Hominidae DEVOTU4 GE 9605: Homo DEVOTU4 SP 9606: Homo sapiens DE0QLUZ ID DE0QLUZ DE0QLUZ DN Oxygen-insensitive NADPH nitroreductase B (nfsB) DE0QLUZ GN nfsB DE0QLUZ SN Oxygen-insensitive NAD(P)H nitroreductase B; Dihydropteridine reductase; FMN-dependent nitroreductase; JW0567; b0578; ntr; pnrB DE0QLUZ UC NFSB_ECOLI DE0QLUZ RD Clonazepam DE0QLUZ GI 945778 DE0QLUZ E1 1: Oxidoreductase DE0QLUZ E2 1.5: CH-NH donor oxidoreductase DE0QLUZ E3 1.5.1: NAD/NADP acceptor oxidoreductase DE0QLUZ EC 1.5.1.34 DE0QLUZ KG Microbial metabolism in diverse environments:ecj01120; Nitrotoluene degradation:ecj00633 DE0QLUZ PD 1DS7; 1ICR; 1ICU; 1ICV; 1IDT; 1OO5; 1OO6; 1OON; 1OOQ; 1YKI; 1YLR; 1YLU; 3X21; 3X22 DE0QLUZ SQ MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV DE0QLUZ TD Primarily distributed in human gut. DE0QLUZ FC This enzyme can reduce a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. And it can reduce nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). DE0QLUZ KD 2: Bacteria DE0QLUZ PL 1224: Proteobacteria DE0QLUZ CL 1236: Gammaproteobacteria DE0QLUZ OD 91347: Enterobacterales DE0QLUZ FM 543: Enterobacteriaceae DE0QLUZ GE 561: Escherichia DE0QLUZ SP 562: Escherichia coli DE9RA0I ID DE9RA0I DE9RA0I DN Beta-glucuronidase (uidA) DE9RA0I GN uidA DE9RA0I SN Beta-galactosidase/beta-glucuronidase; Beta-galactosidase BgaB; GUS; JW1609; b1617; gurA; gusA; uidA DE9RA0I UC BGLR_ECOLI DE9RA0I RD Irinotecan hydrochloride DE9RA0I GI 946149 DE9RA0I E1 3: Hydrolases DE9RA0I E2 3.2: Glycosylase DE9RA0I E3 3.2.1: O/S-glycosyl compound glycosidase DE9RA0I EC 3.2.1.31 DE9RA0I KG Biosynthesis of secondary metabolites:ecj01110; Metabolic pathways:ecj01100; Pentose and glucuronate interconversions:ecj00040; Porphyrin and chlorophyll metabolism:ecj00860 DE9RA0I PD 3K46; 3K4A; 3K4D; 3LPF; 3LPG; 4JHZ; 5CZK DE9RA0I SQ MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDWIGANSYRTSHYPYAEEMLDWADEHGIVVIDETAAVGFNLSLGIGFEAGNKPKELYSEEAVNGETQQAHLQAIKELIARDKNHPSVVMWSIANEPDTRPQGAREYFAPLAEATRKLDPTRPITCVNVMFCDAHTDTISDLFDVLCLNRYYGWYVQSGDLETAEKVLEKELLAWQEKLHQPIIITEYGVDTLAGLHSMYTDMWSEEYQCAWLDMYHRVFDRVSAVVGEQVWNFADFATSQGILRVGGNKKGIFTRDRKPKSAAFLLQKRWTGMNFGEKPQQGGKQ DE9RA0I TD Primarily distributed in human gut. DE9RA0I FC This enzyme takes part in glucuronoside catabolic process. DE9RA0I KD 2: Bacteria DE9RA0I PL 1224: Proteobacteria DE9RA0I CL 1236: Gammaproteobacteria DE9RA0I OD 91347: Enterobacterales DE9RA0I FM 543: Enterobacteriaceae DE9RA0I GE 561: Escherichia DE9RA0I SP 562: Escherichia coli DE9RA0I SU Escherichia coli K-12 DEZWDKE ID DEZWDKE DEZWDKE DN NADPH-dependent curcumin reductase (curA) DEZWDKE GN curA DEZWDKE SN NADPH-dependent curcumin/dihydrocurcumin reductase; b1449; JW5907; curA; yncB DEZWDKE UC CURA_ECOLI DEZWDKE RD SRT-501 DEZWDKE GI 946012 DEZWDKE E1 1: Oxidoreductase DEZWDKE E2 1.3: CH-CH donor oxidoreductase DEZWDKE E3 1.3.1: NAD/NADP acceptor oxidoreductase DEZWDKE EC 1.3.1.- DEZWDKE SQ MGQQKQRNRRWVLASRPHGAPVPENFRLEEDDVATPGEGQVLLRTVYLSLDPYMRGRMSDEPSYSPPVDIGGVMVGGTVSRVVESNHPDYQSGDWVLGYSGWQDYDISSGDDLVKLGDHPQNPSWSLGVLGMPGFTAYMGLLDIGQPKEGETLVVAAATGPVGATVGQIGKLKGCRVVGVAGGAEKCRHATEVLGFDVCLDHHADDFAEQLAKACPKGIDIYYENVGGKVFDAVLPLLNTSARIPVCGLVSSYNATELPPGPDRLPLLMATVLKKRIRLQGFIIAQDYGHRIHEFQREMGQWVKEDKIHYREEITDGLENAPQTFIGLLKGKNFGKVVIRVAGDD DEZWDKE TD Primarily distributed in human gut. DEZWDKE FC This enzyme catalyzes the metal-independent reduction of curcumin to dihydrocurcumin (DHC) as an intermediate product, followed by further reduction to tetrahydrocurcumin (THC) as an end product. And the enzyme also acts on 3-octene-2-one, 3-hepten-2-one, resveratrol, and trans-2-octenal. DEZWDKE KD 2: Bacteria DEZWDKE PL 1224: Proteobacteria DEZWDKE CL 1236: Gammaproteobacteria DEZWDKE OD 91347: Enterobacterales DEZWDKE FM 543: Enterobacteriaceae DEZWDKE GE 561: Escherichia DEZWDKE SP 562: Escherichia coli DEZSNJD ID DEZSNJD DEZSNJD DN Glutathione S-transferase omega-1 (GSTO1) DEZSNJD GN GSTO1 DEZSNJD SN Glutathione S-transferase omega 1-1; Glutathione-dependent dehydroascorbate reductase; MMA(V) reductase; Monomethylarsonic acid reductase; S-(Phenacyl)glutathione reductase; SPG-R; GSTO 1-1; GSTO-1; GSTO1; GSTTLP28 DEZSNJD UC GSTO1_HUMAN DEZSNJD RD ANW-43980 DEZSNJD GI 9446 DEZSNJD E1 2: Transferase DEZSNJD E2 2.5: Alkyl/aryl transferase DEZSNJD E3 2.5.1: Alkyl/aryl transferase DEZSNJD EC 2.5.1.18 DEZSNJD RC Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation:R-HSA-8950505; Glutathione conjugation:R-HSA-156590; Methylation:R-HSA-156581; Vitamin C (ascorbate) metabolism:R-HSA-196836 DEZSNJD KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DEZSNJD PD 3VLN; 4IS0; 4YQM; 4YQU; 4YQV; 5UEH; 5V3Q; 5YVN; 5YVO DEZSNJD SQ MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELFSKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYGL DEZSNJD TD Primarily distributed in pancreas, skeletal muscle, spleen, thymus, colon, blood leukocyte and heart. DEZSNJD FC This enzyme exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. It has both S-(phenacyl)glutathione reductase and glutathione S-transferase activity. It participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid. DEZSNJD KD 33208: Metazoa DEZSNJD PL 7711: Chordata DEZSNJD CL 40674: Mammalia DEZSNJD OD 9443: Primates DEZSNJD FM 9604: Hominidae DEZSNJD GE 9605: Homo DEZSNJD SP 9606: Homo sapiens DEG7L5K ID DEG7L5K DEG7L5K DN Arylamine N-acetyltransferase (NAT) DEG7L5K GN nat DEG7L5K SN N-hydroxyarylamine O-acetyltransferase; nhoA; nat; TUEID40_02779; SAMEA4873640_00320 DEG7L5K UC A0A5E5R1G5_PSEAI DEG7L5K RD Asacolitin DEG7L5K E1 2: Transferase DEG7L5K E2 2.3: Acyltransferase DEG7L5K E3 2.3.1: Acyltransferase DEG7L5K EC 2.3.1.5 DEG7L5K SQ MTPLTPEQTHAYLHHIGIDDPGPPSLANLDRLIDAHLRRVAFENLDVLLDRPIEIDADKVFAKVVEGSRGGYCFELNSLFARLLLALGYELELLVARVRWGLPEDVPLTQQSHLMLRLYLAEGEFLVDVGFGSANPPRALPLPGDEADAGQVHCVRLVDPHAGLYESAVRGRSGWLPLYRFDLRPQLWIDYIPRNWYTSTHPHSVFRQGLKAAITEGDLRLTLADGLFGQRAGNGETLQRQLRDVEELLDILQTRFRLRLDPASEVPALARRLAGLISA DEG7L5K TD Primarily distributed in human gut. DEG7L5K FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DEG7L5K KD 2: Bacteria DEG7L5K PL 1224: Proteobacteria DEG7L5K CL 1236: Gammaproteobacteria DEG7L5K OD 72274: Pseudomonadales DEG7L5K FM 135621: Pseudomonadaceae DEG7L5K GE 286: Pseudomonas DEG7L5K SP 287: Pseudomonas aeruginosa DEDPI65 ID DEDPI65 DEDPI65 DN Oxygen-insensitive NADPH nitroreductase A (nfsA) DEDPI65 GN nfsA DEDPI65 SN Oxygen-insensitive NAD(P)H nitroreductase A; Modulator of drug activity A; JW0835; b0851; mda18; mdaA; nfsA; pnrA; ybjB DEDPI65 UC NFSA_ECOLI DEDPI65 RD Loperamide hydrochloride DEDPI65 GI 945483 DEDPI65 E1 1: Oxidoreductase DEDPI65 E2 1.5: CH-NH donor oxidoreductase DEDPI65 E3 1.5.1: NAD/NADP acceptor oxidoreductase DEDPI65 EC 1.5.1.38 DEDPI65 KG Microbial metabolism in diverse environments:ecj01120; Nitrotoluene degradation:ecj00633 DEDPI65 PD 1F5V DEDPI65 SQ MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR DEDPI65 TD Primarily distributed in human gut. DEDPI65 FC This enzyme is major oxygen-insensitive nitroreductase in E.coli. And it catalyzes the reduction of nitroaromatic compounds using NADPH, and has a broad electron acceptor specificity. Moreover, it reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. DEDPI65 KD 2: Bacteria DEDPI65 PL 1224: Proteobacteria DEDPI65 CL 1236: Gammaproteobacteria DEDPI65 OD 91347: Enterobacterales DEDPI65 FM 543: Enterobacteriaceae DEDPI65 GE 561: Escherichia DEDPI65 SP 562: Escherichia coli DE3IV6Q ID DE3IV6Q DE3IV6Q DN Hydroxybenzoate 3-monooxygenase (pobA) DE3IV6Q GN pobA DE3IV6Q SN Hydroxybenzoate hydroxylase; 4-hydroxybenzoate 3-monooxygenase; p-hydroxybenzoate hydroxylase; PA0247; PHBH; pobA DE3IV6Q UC PHHY_PSEAE DE3IV6Q RD Tetracycline DE3IV6Q GI 882128 DE3IV6Q E1 1: Oxidoreductase DE3IV6Q E2 1.14: Oxygen paired donor oxidoreductase DE3IV6Q E3 1.14.13: NADH/NADPH donor oxidoreductase DE3IV6Q EC 1.14.13.2 DE3IV6Q KG Benzoate degradation:pae00362; Degradation of aromatic compounds:pae01220; Metabolic pathways:pae01100; Microbial metabolism in diverse environments:pae01120 DE3IV6Q PD 1D7L; 1DOB; 1DOC; 1DOD; 1DOE; 1IUS; 1IUT; 1IUU; 1IUV; 1IUW; 1IUX; 1K0I; 1K0J; 1K0L; 1PXA DE3IV6Q SQ MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE DE3IV6Q TD Primarily distributed in human gut. DE3IV6Q FC This enzyme is a flavoprotein (FAD) and can catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). DE3IV6Q KD 2: Bacteria DE3IV6Q PL 1224: Proteobacteria DE3IV6Q CL 1236: Gammaproteobacteria DE3IV6Q OD 72274: Pseudomonadales DE3IV6Q FM 135621: Pseudomonadaceae DE3IV6Q GE 286: Pseudomonas DE3IV6Q SP 287: Pseudomonas aeruginosa DEBIHM3 ID DEBIHM3 DEBIHM3 DN Vitamin D 25-hydroxylase (CYP2R1) DEBIHM3 GN CYP2R1 DEBIHM3 SN Cytochrome P450 family 2 subfamily R member 1; Cytochrome P450 2R1; CYP2R1 DEBIHM3 UC CP2R1_HUMAN DEBIHM3 RD Ergocalciferol DEBIHM3 GI 120227 DEBIHM3 E1 1: Oxidoreductase DEBIHM3 E2 1.14: Oxygen paired donor oxidoreductase DEBIHM3 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEBIHM3 EC 1.14.14.24 DEBIHM3 RC Defective CYP2R1 causes Rickets vitamin D-dependent 1B (VDDR1B):R-HSA-5579027; Vitamin D (calciferol) metabolism:R-HSA-196791; Vitamins:R-HSA-211916 DEBIHM3 KG Metabolic pathways:hsa01100; Steroid biosynthesis:hsa00100 DEBIHM3 PD 3C6G; 3CZH; 3DL9 DEBIHM3 SQ MWKLWRAEEGAAALGGALFLLLFALGVRQLLKQRRPMGFPPGPPGLPFIGNIYSLAASSELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWVDHRRLAVNSFRYFGYGQKSFESKILEETKFFNDAIETYKGRPFDFKQLITNAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAFPWIGILPFGKHQQLFRNAAVVYDFLSRLIEKASVNRKPQLPQHFVDAYLDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEHLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLICAERR DEBIHM3 TD Low tissue/organ specificity. DEBIHM3 FC This enzyme has a D-25-hydroxylase activity on both forms of vitamin D, vitamin D(2) and D(3). DEBIHM3 KD 33208: Metazoa DEBIHM3 PL 7711: Chordata DEBIHM3 CL 40674: Mammalia DEBIHM3 OD 9443: Primates DEBIHM3 FM 9604: Hominidae DEBIHM3 GE 9605: Homo DEBIHM3 SP 9606: Homo sapiens DEOCWU3 ID DEOCWU3 DEOCWU3 DN Alcohol dehydrogenase class-II (ADH4) DEOCWU3 GN ADH4 DEOCWU3 SN Alcohol dehydrogenase 4; Alcohol dehydrogenase class II pi chain; All-trans-retinol dehydrogenase [NAD(+)] ADH4; ADH4 DEOCWU3 UC ADH4_HUMAN DEOCWU3 RD BRN-2217626 DEOCWU3 GI 127 DEOCWU3 E1 1: Oxidoreductase DEOCWU3 E2 1.1: CH-OH donor oxidoreductase DEOCWU3 E3 1.1.1: NAD/NADP oxidoreductase DEOCWU3 EC 1.1.1.105 DEOCWU3 RC Ethanol oxidation:R-HSA-71384; RA biosynthesis pathway:R-HSA-5365859 DEOCWU3 KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Fatty acid degradation:hsa00071; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Tyrosine metabolism:hsa00350 DEOCWU3 PD 3COS DEOCWU3 SQ MGTKGKVIKCKAAIAWEAGKPLCIEEVEVAPPKAHEVRIQIIATSLCHTDATVIDSKFEGLAFPVIVGHEAAGIVESIGPGVTNVKPGDKVIPLYAPLCRKCKFCLSPLTNLCGKISNLKSPASDQQLMEDKTSRFTCKGKPVYHFFGTSTFSQYTVVSDINLAKIDDDANLERVCLLGCGFSTGYGAAINNAKVTPGSTCAVFGLGGVGLSAVMGCKAAGASRIIGIDINSEKFVKAKALGATDCLNPRDLHKPIQEVIIELTKGGVDFALDCAGGSETMKAALDCTTAGWGSCTFIGVAAGSKGLTIFPEELIIGRTINGTFFGGWKSVDSIPKLVTDYKNKKFNLDALVTHTLPFDKISEAFDLMNQGKSVRTILIF DEOCWU3 TD Primarily distributed in liver. DEOCWU3 FC This enzyme catalyzes the NAD-dependent oxidation of either all-trans- retinol or 9-cis-retinol.It also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Besides, it can also catalyzes the reduction of benzoquinones. DEOCWU3 KD 33208: Metazoa DEOCWU3 PL 7711: Chordata DEOCWU3 CL 40674: Mammalia DEOCWU3 OD 9443: Primates DEOCWU3 FM 9604: Hominidae DEOCWU3 GE 9605: Homo DEOCWU3 SP 9606: Homo sapiens DEMQOF7 ID DEMQOF7 DEMQOF7 DN Methionine-R-sulfoxide reductase B2 (MSRB2) DEMQOF7 GN MSRB2 DEMQOF7 SN Mitochondrial methionine-R-sulfoxide reductase B2; CBS-1; CGI-131; MSRB; MSRB2; MsrB2 DEMQOF7 UC MSRB2_HUMAN DEMQOF7 RD Methionine DEMQOF7 GI 22921 DEMQOF7 E1 1: Oxidoreductase DEMQOF7 E2 1.8: Sulfur donor oxidoreductase DEMQOF7 E3 1.8.4: Disulfide acceptor oxidoreductase DEMQOF7 EC 1.8.4.12 DEMQOF7 RC Protein repair:R-HSA-5676934 DEMQOF7 SQ MARLLWLLRGLTLGTAPRRAVRGQAGGGGPGTGPGLGEAGSLATCELPLAKSEWQKKLTPEQFYVTREKGTEPPFSGIYLNNKEAGMYHCVCCDSPLFSSEKKYCSGTGWPSFSEAHGTSGSDESHTGILRRLDTSLGSARTEVVCKQCEAHLGHVFPDGPGPNGQRFCINSVALKFKPRKH DEMQOF7 TD Primarily distributed in heart. DEMQOF7 FC This enzyme specifically reduces methionine (R)-sulfoxide back to methionine. DEMQOF7 KD 33208: Metazoa DEMQOF7 PL 7711: Chordata DEMQOF7 CL 40674: Mammalia DEMQOF7 OD 9443: Primates DEMQOF7 FM 9604: Hominidae DEMQOF7 GE 9605: Homo DEMQOF7 SP 9606: Homo sapiens DE3PKUG ID DE3PKUG DE3PKUG DN Glutathione S-transferase theta-1 (GSTT1) DE3PKUG GN GSTT1 DE3PKUG SN Glutathione S-transferase T1-1; Glutathione transferase T1-1; GST class-theta-1; GSTT1 DE3PKUG UC GSTT1_HUMAN DE3PKUG RD Oxaliplatin DE3PKUG GI 2952 DE3PKUG E1 2: Transferase DE3PKUG E2 2.5: Alkyl/aryl transferase DE3PKUG E3 2.5.1: Alkyl/aryl transferase DE3PKUG EC 2.5.1.18 DE3PKUG RC Glutathione conjugation:R-HSA-156590 DE3PKUG KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DE3PKUG PD 2C3N; 2C3Q; 2C3T DE3PKUG SQ MGLELYLDLLSQPCRAVYIFAKKNDIPFELRIVDLIKGQHLSDAFAQVNPLKKVPALKDGDFTLTESVAILLYLTRKYKVPDYWYPQDLQARARVDEYLAWQHTTLRRSCLRALWHKVMFPVFLGEPVSPQTLAATLAELDVTLQLLEDKFLQNKAFLTGPHISLADLVAITELMHPVGAGCQVFEGRPKLATWRQRVEAAVGEDLFQEAHEVILKAKDFPPADPTIKQKLMPWVLAMIR DE3PKUG TD Primarily distributed in liver and lung. DE3PKUG FC This enzyme conjugates reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. It acts on 1,2-epoxy- 3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl chloride and 4-nitrophenethyl bromide and displays glutathione peroxidase activity with cumene hydroperoxide. DE3PKUG KD 33208: Metazoa DE3PKUG PL 7711: Chordata DE3PKUG CL 40674: Mammalia DE3PKUG OD 9443: Primates DE3PKUG FM 9604: Hominidae DE3PKUG GE 9605: Homo DE3PKUG SP 9606: Homo sapiens DEB3TNR ID DEB3TNR DEB3TNR DN Tyramine oxidase (tynA) DEB3TNR GN tynA DEB3TNR SN Copper amine oxidase; Primary amine oxidase; 2-phenylethylamine oxidase; JW1381; b1386; Bacterial maoA; tynA DEB3TNR UC AMO_ECOLI DEB3TNR RD Amphetamine DEB3TNR GI 945939 DEB3TNR E1 1: Oxidoreductase DEB3TNR E2 1.4: CH-NH2 donor oxidoreductase DEB3TNR E3 1.4.3: Oxygen acceptor oxidoreductase DEB3TNR EC 1.4.3.21 DEB3TNR KG Biosynthesis of secondary metabolites:ecj01110; Glycine, serine and threonine metabolism:ecj00260; Metabolic pathways:ecj01100; Phenylalanine metabolism:ecj00360; Tyrosine metabolism:ecj00350; beta-Alanine metabolism:ecj00410 DEB3TNR PD 1D6U; 1D6Y; 1D6Z; 1DYU; 1JRQ; 1LVN; 1OAC; 1QAF; 1QAK; 1QAL; 1SPU; 2W0Q; 2WGQ; 2WO0; 2WOF DEB3TNR SQ MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK DEB3TNR TD Primarily distributed in human gut. DEB3TNR FC This enzyme can oxidize primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. DEB3TNR KD 2: Bacteria DEB3TNR PL 1224: Proteobacteria DEB3TNR CL 1236: Gammaproteobacteria DEB3TNR OD 91347: Enterobacterales DEB3TNR FM 543: Enterobacteriaceae DEB3TNR GE 561: Escherichia DEB3TNR SP 562: Escherichia coli DE1FR8H ID DE1FR8H DE1FR8H DN N-ethylmaleimide reductase (nemA) DE1FR8H GN nemA DE1FR8H SN N-ethylmaleimide reducing enzyme; NEM reductase; JW1642; b1650; nemA; ydhN DE1FR8H UC NEMA_ECOLI DE1FR8H RD CBL-954 DE1FR8H GI 946164 DE1FR8H E1 1: Oxidoreductase DE1FR8H E2 1.3: CH-CH donor oxidoreductase DE1FR8H E3 1.3.1: NAD/NADP acceptor oxidoreductase DE1FR8H EC 1.3.1.- DE1FR8H KG Microbial metabolism in diverse environments:ecj01120; Nitrotoluene degradation:ecj00633 DE1FR8H SQ MSSEKLYSPLKVGAITAANRIFMAPLTRLRSIEPGDIPTPLMAEYYRQRASAGLIISEATQISAQAKGYAGAPGIHSPEQIAAWKKITAGVHAENGHMAVQLWHTGRISHASLQPGGQAPVAPSALSAGTRTSLRDENGQAIRVETSMPRALELEEIPGIVNDFRQAIANAREAGFDLVELHSAHGYLLHQFLSPSSNHRTDQYGGSVENRARLVLEVVDAGIEEWGADRIGIRVSPIGTFQNTDNGPNEEADALYLIEQLGKRGIAYLHMSEPDWAGGEPYTDAFREKVRARFHGPIIGAGAYTVEKAETLIGKGLIDAVAFGRDWIANPDLVARLQRKAELNPQRAESFYGGGAEGYTDYPTL DE1FR8H TD Primarily distributed in human gut. DE1FR8H FC This enzyme is involved in the degradation of toxic compounds. And it can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones. Moreover, it also can catalyze the reduction of N-ethylmaleimide (NEM) to N-ethylsuccinimide. Together with NfsA and NfsB, can use the nitroaromatic explosive 2,4,6-trinitrotoluene (TNT). DE1FR8H KD 2: Bacteria DE1FR8H PL 1224: Proteobacteria DE1FR8H CL 1236: Gammaproteobacteria DE1FR8H OD 91347: Enterobacterales DE1FR8H FM 543: Enterobacteriaceae DE1FR8H GE 561: Escherichia DE1FR8H SP 562: Escherichia coli DE26V9J ID DE26V9J DE26V9J DN Chloramphenicolase (chlR) DE26V9J GN chlR DE26V9J SN Chloramphenicol reductase; Enzyme chloramphenicolase; Reductase chloramphenicol DE26V9J UC A0A5M4B0P0_9BACT DE26V9J RD Chloramphenicol DE26V9J E1 2: Transferase DE26V9J E2 2.3: Acyltransferase DE26V9J E3 2.3.1: Acyltransferase DE26V9J EC 2.3.1.28 DE26V9J SQ MKKIDLNSWNRREHFAFFSQFDEPFFSIVAEVDCTVAYRKAKEQDIPFFIWYLYQSLLAANQVEPFRYRIIDNEVVVLDEIHASSTVAREDHTFGFTFMPYREDIKAFVAEALPEIERVQQLEGLCFDEKTSRTDVIHYSSIPWINFTALTHARHNARKDSVPKISFGQYQEKEGKLMMPVSVTVHHGLMDGYHVGLFLTKFQKLLES DE26V9J TD Primarily distributed in human gut. DE26V9J FC This enzyme catalyzes the hydrolysis of the amide bond in chloramphenicol. DE26V9J KD 2: Bacteria DE26V9J PL 1224: Proteobacteria DE26V9J CL 1236: Gammaproteobacteria DE26V9J OD 91347: Enterobacterales DE26V9J FM 543: Enterobacteriaceae DE26V9J GE 561: Escherichia DE26V9J SP 562: Escherichia coli DEEHWOG ID DEEHWOG DEEHWOG DN Azoreductase (azoR) DEEHWOG GN azoR DEEHWOG SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; JW1409; acpD; b1412 DEEHWOG UC AZOR_ECOLI DEEHWOG RD Balsalazide DEEHWOG GI 947569 DEEHWOG E1 1: Oxidoreductase DEEHWOG E2 1.7: Cytochrome acceptor oxidoreductase DEEHWOG E3 1.7.1: NAD/NADP acceptor oxidoreductase DEEHWOG EC 1.7.1.6 DEEHWOG PD 1TIK; 1V4B; 2D5I; 2Z98; 2Z9B; 2Z9C; 2Z9D DEEHWOG SQ MSKVLVLKSSILAGYSQSNQLSDYFVEQWREKHSADEITVRDLAANPIPVLDGELVGALRPSDAPLTPRQQEALALSDELIAELKAHDVIVIAAPMYNFNISTQLKNYFDLVARAGVTFRYTENGPEGLVTGKKAIVITSRGGIHKDGPTDLVTPYLSTFLGFIGITDVKFVFAEGIAYGPEMAAKAQSDAKAAIDSIVSA DEEHWOG TD Primarily distributed in human gut. DEEHWOG FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. And it requires NADH, but not NADPH, as an electron donor for its activity. And it can reduce ethyl red and methyl red, but is not able to convert sulfonated azo dyes. DEEHWOG KD 2: Bacteria DEEHWOG PL 1224: Proteobacteria DEEHWOG CL 1236: Gammaproteobacteria DEEHWOG OD 91347: Enterobacterales DEEHWOG FM 543: Enterobacteriaceae DEEHWOG GE 561: Escherichia DEEHWOG SP 562: Escherichia coli DE97WM8 ID DE97WM8 DE97WM8 DN NADP-dependent malic enzyme (ME1) DE97WM8 GN ME1 DE97WM8 SN NADP-specific-malic enzyme; Malic enzyme 1 NADP-specific; Malic enzyme 1; ME1; NADP-ME DE97WM8 UC MAOX_HUMAN DE97WM8 RD Malate DE97WM8 GI 4199 DE97WM8 E1 1: Oxidoreductase DE97WM8 E2 1.1: CH-OH donor oxidoreductase DE97WM8 E3 1.1.1: NAD/NADP oxidoreductase DE97WM8 EC 1.1.1.40 DE97WM8 RC PPARA activates gene expression:R-HSA-1989781; Pyruvate metabolism:R-HSA-70268 DE97WM8 KG Carbon metabolism:hsa01200; Metabolic pathways:hsa01100; PPAR signaling pathway:hsa03320; Pyruvate metabolism:hsa00620 DE97WM8 PD 2AW5; 3WJA DE97WM8 SQ MEPEAPRRRHTHQRGYLLTRNPHLNKDLAFTLEERQQLNIHGLLPPSFNSQEIQVLRVVKNFEHLNSDFDRYLLLMDLQDRNEKLFYRVLTSDIEKFMPIVYTPTVGLACQQYSLVFRKPRGLFITIHDRGHIASVLNAWPEDVIKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGMNPQECLPVILDVGTENEELLKDPLYIGLRQRRVRGSEYDDFLDEFMEAVSSKYGMNCLIQFEDFANVNAFRLLNKYRNQYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTILFQGAGEAALGIAHLIVMALEKEGLPKEKAIKKIWLVDSKGLIVKGRASLTQEKEKFAHEHEEMKNLEAIVQEIKPTALIGVAAIGGAFSEQILKDMAAFNERPIIFALSNPTSKAECSAEQCYKITKGRAIFASGSPFDPVTLPNGQTLYPGQGNNSYVFPGVALGVVACGLRQITDNIFLTTAEVIAQQVSDKHLEEGRLYPPLNTIRDVSLKIAEKIVKDAYQEKTATVYPEPQNKEAFVRSQMYSTDYDQILPDCYSWPEEVQKIQTKVDQ DE97WM8 TD Primarily distributed in liver, placenta and white adipose tissue. DE97WM8 FC This enzyme is reversible oxidative decarboxylation of malate to pyruvate, links the glycolytic and citric acid cycles. DE97WM8 KD 33208: Metazoa DE97WM8 PL 7711: Chordata DE97WM8 CL 40674: Mammalia DE97WM8 OD 9443: Primates DE97WM8 FM 9604: Hominidae DE97WM8 GE 9605: Homo DE97WM8 SP 9606: Homo sapiens DEN8V7Z ID DEN8V7Z DEN8V7Z DN Glutamate carboxypeptidase II (FOLH1) DEN8V7Z GN FOLH1 DEN8V7Z SN Glutamate carboxypeptidase 2; Membrane glutamate carboxypeptidase; N-acetylated-alpha-linked acidic dipeptidase I; Prostate-specific membrane antigen; Cell growth-inhibiting gene 27 protein; Folate hydrolase 1; Folylpoly-gamma-glutamate carboxypeptidase; Pteroylpoly-gamma-glutamate carboxypeptidase; mGCP; FGCP; FOLH; FOLH1; NAALAD1; NAALADase I; PSM; PSMA; GCPII; GIG27 DEN8V7Z UC FOLH1_HUMAN DEN8V7Z RD Methotrexate DEN8V7Z GI 2346 DEN8V7Z E1 3: Hydrolases DEN8V7Z E2 3.4: Peptidase DEN8V7Z E3 3.4.17: Metallocarboxypeptidase DEN8V7Z EC 3.4.17.21 DEN8V7Z RC Aspartate and asparagine metabolism:R-HSA-8963693 DEN8V7Z KG Alanine, aspartate and glutamate metabolism:hsa00250; Metabolic pathways:hsa01100; Vitamin digestion and absorption:hsa04977 DEN8V7Z PD 2C6G; 2C6P; 2CIJ; 2JBJ; 2JBK; 2OOT; 2OR4; 2PVV; 2PVW DEN8V7Z SQ MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA DEN8V7Z TD Primarily distributed in brain, intestine and prostate. DEN8V7Z FC This enzyme has both folate hydrolase and N-acetylated-alpha-linked- acidic dipeptidase (NAALADase) activity. It has a preference for tri- alpha-glutamate peptides. It also exhibits a dipeptidyl-peptidase IV type activity. In vitro, it cleaves Gly-Pro-AMC. DEN8V7Z KD 33208: Metazoa DEN8V7Z PL 7711: Chordata DEN8V7Z CL 40674: Mammalia DEN8V7Z OD 9443: Primates DEN8V7Z FM 9604: Hominidae DEN8V7Z GE 9605: Homo DEN8V7Z SP 9606: Homo sapiens DEGKWJB ID DEGKWJB DEGKWJB DN Alpha-methylacyl-CoA racemase (AMACR) DEGKWJB GN AMACR DEGKWJB SN Methylacyl-CoA racemase; 2-methylacyl-CoA racemase; 2-methylacyl-CoA 2-epimerase; AMACR; AMACRD; CBAS4; RACE; P504S DEGKWJB UC AMACR_HUMAN DEGKWJB RD Ibuprofen DEGKWJB GI 23600 DEGKWJB E1 5: Isomerase DEGKWJB E2 5.1: Racemase/epimerase DEGKWJB E3 5.1.99: Racemase/epimerase DEGKWJB EC 5.1.99.4 DEGKWJB RC Beta-oxidation of pristanoyl-CoA:R-HSA-389887; Peroxisomal protein import:R-HSA-9033241; Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DEGKWJB KG Metabolic pathways:hsa01100; Peroxisome:hsa04146; Primary bile acid biosynthesis:hsa00120 DEGKWJB SQ MALQGISVVELSGLAPGPFCAMVLADFGARVVRVDRPGSRYDVSRLGRGKRSLVLDLKQPRGAAVLRRLCKRSDVLLEPFRRGVMEKLQLGPEILQRENPRLIYARLSGFGQSGSFCRLAGHDINYLALSGVLSKIGRSGENPYAPLNLLADFAGGGLMCALGIIMALFDRTRTGKGQVIDANMVEGTAYLSSFLWKTQKLSLWEAPRGQNMLDGGAPFYTTYRTADGEFMAVGAIEPQFYELLIKGLGLKSDELPNQMSMDDWPEMKKKFADVFAEKTKAEWCQIFDGTDACVTPVLTFEEVVHHDHNKERGSFITSEEQDVSPRPAPLLLNTPAIPSFKRDPFIGEHTEEILEEFGFSREEIYQLNSDKIIESNKVKASL DEGKWJB TD Primarily distributed in kidney and liver. DEGKWJB FC This enzyme catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters. DEGKWJB KD 33208: Metazoa DEGKWJB PL 7711: Chordata DEGKWJB CL 40674: Mammalia DEGKWJB OD 9443: Primates DEGKWJB FM 9604: Hominidae DEGKWJB GE 9605: Homo DEGKWJB SP 9606: Homo sapiens DEYMAD4 ID DEYMAD4 DEYMAD4 DN Sulfotransferase 1C2 (SULT1C2) DEYMAD4 GN SULT1C2 DEYMAD4 SN Sulfotransferase family cytosolic 1C member 2; Sulfotransferase 1C1; humSULTC2; ST1C2; SULT1C#1; SULT1C1; SULT1C2 DEYMAD4 UC ST1C2_HUMAN DEYMAD4 RD SRT-501 DEYMAD4 GI 6819 DEYMAD4 E1 2: Transferase DEYMAD4 E2 2.8: Sulfotransferase DEYMAD4 E3 2.8.2: Sulfotransferase DEYMAD4 EC 2.8.2.1 DEYMAD4 RC Cytosolic sulfonation of small molecules:R-HSA-156584 DEYMAD4 PD 3BFX DEYMAD4 SQ MALTSDLGKQIKLKEVEGTLLQPATVDNWSQIQSFEAKPDDLLICTYPKAGTTWIQEIVDMIEQNGDVEKCQRAIIQHRHPFIEWARPPQPSGVEKAKAMPSPRILKTHLSTQLLPPSFWENNCKFLYVARNAKDCMVSYYHFQRMNHMLPDPGTWEEYFETFINGKVVWGSWFDHVKGWWEMKDRHQILFLFYEDIKRDPKHEIRKVMQFMGKKVDETVLDKIVQETSFEKMKENPMTNRSTVSKSILDQSISSFMRKGTVGDWKNHFTVAQNERFDEIYRRKMEGTSINFCMEL DEYMAD4 TD Primarily distributed in gallbladder, kidney and stomach. DEYMAD4 FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. DEYMAD4 KD 33208: Metazoa DEYMAD4 PL 7711: Chordata DEYMAD4 CL 40674: Mammalia DEYMAD4 OD 9443: Primates DEYMAD4 FM 9604: Hominidae DEYMAD4 GE 9605: Homo DEYMAD4 SP 9606: Homo sapiens DEV0J5F ID DEV0J5F DEV0J5F DN Liver-type arginase (ARG1) DEV0J5F GN ARG1 DEV0J5F SN Arginine amidinase 1; Canavanase 1; L-arginase 1; Arginine transamidinase 1; Arginase-1; Type I arginase; ARGAH1; ARG1 DEV0J5F UC ARGI1_HUMAN DEV0J5F RD L-arginine DEV0J5F GI 383 DEV0J5F E1 3: Hydrolases DEV0J5F E2 3.5: Carbon-nitrogen hydrolase DEV0J5F E3 3.5.3: Linear amidine hydrolase DEV0J5F EC 3.5.3.1 DEV0J5F RC Neutrophil degranulation:R-HSA-6798695; Urea cycle:R-HSA-70635 DEV0J5F KG Amoebiasis:hsa05146; Arginine and proline metabolism:hsa00330; Arginine biosynthesis:hsa00220; Biosynthesis of amino acids:hsa01230; Metabolic pathways:hsa01100 DEV0J5F PD 2AEB; 2PHA; 2PHO; 2PLL; 2ZAV; 3DJ8; 3E6K; 3E6V; 3F80 DEV0J5F SQ MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK DEV0J5F TD Primarily distributed in liver. DEV0J5F FC This enzyme is a key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides. DEV0J5F KD 33208: Metazoa DEV0J5F PL 7711: Chordata DEV0J5F CL 40674: Mammalia DEV0J5F OD 9443: Primates DEV0J5F FM 9604: Hominidae DEV0J5F GE 9605: Homo DEV0J5F SP 9606: Homo sapiens DE9OSW8 ID DE9OSW8 DE9OSW8 DN Insulin-degrading enzyme (IDE) DE9OSW8 GN IDE DE9OSW8 SN Abeta-degrading protease; Insulin protease; Insulinase; Insulysin; IDE DE9OSW8 UC IDE_HUMAN DE9OSW8 RD Insulin DE9OSW8 GI 3416 DE9OSW8 E1 3: Hydrolases DE9OSW8 E2 3.4: Peptidase DE9OSW8 E3 3.4.24: Metallopeptidase DE9OSW8 EC 3.4.24.56 DE9OSW8 RC Peroxisomal protein import:R-HSA-9033241; Ub-specific processing proteases:R-HSA-5689880 DE9OSW8 KG Alzheimer's disease:hsa05010 DE9OSW8 PD 2G49; 2G54; 2G56; 2JBU; 2JG4; 2WBY; 2WC0; 2WK3; 2YPU DE9OSW8 SQ MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSCPVVGEFPCQNDINLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMAAKL DE9OSW8 TD Low tissue/organ specificity. DE9OSW8 FC This enzyme plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, glucagon, bradykinin, kallidin and other peptides. Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin. It plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia. DE9OSW8 KD 33208: Metazoa DE9OSW8 PL 7711: Chordata DE9OSW8 CL 40674: Mammalia DE9OSW8 OD 9443: Primates DE9OSW8 FM 9604: Hominidae DE9OSW8 GE 9605: Homo DE9OSW8 SP 9606: Homo sapiens DERQ52Z ID DERQ52Z DERQ52Z DN Glutathione S-transferase mu-4 (GSTM4) DERQ52Z GN GSTM4 DERQ52Z SN Glutathione S-transferase Mu 4; GST class-mu 4; GST-Mu2; GSTM4; GSTM4-4 DERQ52Z UC GSTM4_HUMAN DERQ52Z RD Amodiaquine DERQ52Z GI 2948 DERQ52Z E1 2: Transferase DERQ52Z E2 2.5: Alkyl/aryl transferase DERQ52Z E3 2.5.1: Alkyl/aryl transferase DERQ52Z EC 2.5.1.18 DERQ52Z RC Biosynthesis of maresin conjugates in tissue regeneration (MCTR):R-HSA-9026762; Glutathione conjugation:R-HSA-156590 DERQ52Z KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DERQ52Z PD 4GTU DERQ52Z SQ MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDFEKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK DERQ52Z TD Primarily distributed in intestine. DERQ52Z FC This enzyme actives on 1-chloro-2,4-dinitrobenzene and it conjugates of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. DERQ52Z KD 33208: Metazoa DERQ52Z PL 7711: Chordata DERQ52Z CL 40674: Mammalia DERQ52Z OD 9443: Primates DERQ52Z FM 9604: Hominidae DERQ52Z GE 9605: Homo DERQ52Z SP 9606: Homo sapiens DEOS3FD ID DEOS3FD DEOS3FD DN Glutathione peroxidase 6 (GPX6) DEOS3FD GN GPX6 DEOS3FD SN Cellular glutathione peroxidase; 3,3'-telluro-bis(proapne-3,1-diyl)adamantane carboxylate; ADA-Te-OH; ARMEP24; AtGPX1; ATGPX3; c-GPx4; GPX6; GPx-6; GSHPx-6 DEOS3FD UC GPX6_HUMAN DEOS3FD RD ANW-43980 DEOS3FD GI 257202 DEOS3FD E1 1: Oxidoreductase DEOS3FD E2 1.11: Peroxidase DEOS3FD E3 1.11.1: Peroxidase DEOS3FD EC 1.11.1.9 DEOS3FD RC Detoxification of Reactive Oxygen Species:R-HSA-3299685 DEOS3FD KG Amyotrophic lateral sclerosis (ALS):hsa05014; Arachidonic acid metabolism:hsa00590; Glutathione metabolism:hsa00480; Huntington's disease:hsa05016; Metabolic pathways:hsa01100; Thyroid hormone synthesis:hsa04918 DEOS3FD SQ MFQQFQASCLVLFFLVGFAQQTLKPQNRKVDCNKGVTGTIYEYGALTLNGEEYIQFKQFAGKHVLFVNVAAYUGLAAQYPELNALQEELKNFGVIVLAFPCNQFGKQEPGTNSEILLGLKYVCPGSGFVPSFQLFEKGDVNGEKEQKVFTFLKNSCPPTSDLLGSSSQLFWEPMKVHDIRWNFEKFLVGPDGVPVMHWFHQAPVSTVKSDILEYLKQFNTH DEOS3FD TD Primarily distributed in epididymis. DEOS3FD FC This enzyme has glutathione peroxidase activity and peroxidase activity. DEOS3FD KD 33208: Metazoa DEOS3FD PL 7711: Chordata DEOS3FD CL 40674: Mammalia DEOS3FD OD 9443: Primates DEOS3FD FM 9604: Hominidae DEOS3FD GE 9605: Homo DEOS3FD SP 9606: Homo sapiens DEIZLTN ID DEIZLTN DEIZLTN DN Docosahexaenoic acid omega-hydroxylase (CYP4F11) DEIZLTN GN CYP4F11 DEIZLTN SN Phylloquinone omega-hydroxylase CYP4F11; Cytochrome P450 4F11; Long-chain fatty acid omega-monooxygenase; 3-hydroxy fatty acids omega-hydroxylase CYP4F11; CYP4F11; CYPIVF11 DEIZLTN UC CP4FB_HUMAN DEIZLTN RD Benzphetamine DEIZLTN GI 57834 DEIZLTN E1 1: Oxidoreductase DEIZLTN E2 1.14: Oxygen paired donor oxidoreductase DEIZLTN E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEIZLTN EC 1.14.14.1 DEIZLTN RC Eicosanoids:R-HSA-211979; Fatty acids:R-HSA-211935; Miscellaneous substrates:R-HSA-211958; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DEIZLTN SQ MPQLSLSWLGLGPVAASPWLLLLLVGGSWLLARVLAWTYTFYDNCRRLQCFPQPPKQNWFWGHQGLVTPTEEGMKTLTQLVTTYPQGFKLWLGPTFPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILELSAFVEKRNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPRRKPELILRAEGGLWLRVEPLGANSQ DEIZLTN TD Primarily distributed in liver. Also expressed in kidney, heart and skeletal muscle. DEIZLTN FC This enzyme involves in the metabolism of various endogenous substrates, including fatty acids and their oxygenated derivatives. DEIZLTN KD 33208: Metazoa DEIZLTN PL 7711: Chordata DEIZLTN CL 40674: Mammalia DEIZLTN OD 9443: Primates DEIZLTN FM 9604: Hominidae DEIZLTN GE 9605: Homo DEIZLTN SP 9606: Homo sapiens DEM1HNL ID DEM1HNL DEM1HNL DN Alcohol dehydrogenase class-I gamma (ADH1C) DEM1HNL GN ADH1C DEM1HNL SN Alcohol dehydrogenase 1C; Alcohol dehydrogenase subunit gamma; ADH1C; ADH3 DEM1HNL UC ADH1G_HUMAN DEM1HNL RD Ethanol DEM1HNL GI 126 DEM1HNL E1 1: Oxidoreductase DEM1HNL E2 1.1: CH-OH donor oxidoreductase DEM1HNL E3 1.1.1: NAD/NADP oxidoreductase DEM1HNL EC 1.1.1.1 DEM1HNL RC Ethanol oxidation:R-HSA-71384; RA biosynthesis pathway:R-HSA-5365859 DEM1HNL KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Fatty acid degradation:hsa00071; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830; Tyrosine metabolism:hsa00350 DEM1HNL PD 1DDA; 1HT0; 1U3W DEM1HNL SQ MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAAGICRSDEHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNPRGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSINPMLLLTGRTWKGAIFGGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGFDLLRSGKSIRTVLTF DEM1HNL TD Primarily distributed in intestine, liver and stomach. DEM1HNL FC This enzyme metabolizes a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. DEM1HNL KD 33208: Metazoa DEM1HNL PL 7711: Chordata DEM1HNL CL 40674: Mammalia DEM1HNL OD 9443: Primates DEM1HNL FM 9604: Hominidae DEM1HNL GE 9605: Homo DEM1HNL SP 9606: Homo sapiens DEH6CAO ID DEH6CAO DEH6CAO DN Gamma-glutamyltranspeptidase 5 (GGT5) DEH6CAO GN GGT5 DEH6CAO SN Glutathione hydrolase 5 proenzyme; Gamma-glutamyl transpeptidase-related enzyme; Gamma-glutamyltransferase 5; Gamma-glutamyltransferase-like activity 1; Glutathione hydrolase 5 heavy chain; Glutathione hydrolase 5 light chain; GGT 5; GGT-rel; GGT5; GGTLA1 DEH6CAO UC GGT5_HUMAN DEH6CAO RD ANW-43980 DEH6CAO GI 2687 DEH6CAO E1 3: Hydrolases DEH6CAO E2 3.4: Peptidase DEH6CAO E3 3.4.19: Omega peptidase DEH6CAO EC 3.4.19.13 DEH6CAO RC Aflatoxin activation and detoxification:R-HSA-5423646; Glutathione synthesis and recycling:R-HSA-174403; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DEH6CAO KG Arachidonic acid metabolism:hsa00590; Glutathione metabolism:hsa00480; Metabolic pathways:hsa01100; Taurine and hypotaurine metabolism:hsa00430 DEH6CAO SQ MARGYGATVSLVLLGLGLALAVIVLAVVLSRHQAPCGPQAFAHAAVAADSKVCSDIGRAILQQQGSPVDATIAALVCTSVVNPQSMGLGGGVIFTIYNVTTGKVEVINARETVPASHAPSLLDQCAQALPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLRGGHVVAPVLSRFLHNSILRPSLQASTLRQLFFNGTEPLRPQDPLPWPALATTLETVATEGVEVFYTGRLGQMLVEDIAKEGSQLTLQDLAKFQPEVVDALEVPLGDYTLYSPPPPAGGAILSFILNVLRGFNFSTESMARPEGRVNVYHHLVETLKFAKGQRWRLGDPRSHPKLQNASRDLLGETLAQLIRQQIDGRGDHQLSHYSLAEAWGHGTGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRTGIILNNELLDLCERCPRGSGTTPSPVSGDRVGGAPGRCWPPVPGERSPSSMVPSILINKAQGSKLVIGGAGGELIISAVAQAIMSKLWLGFDLRAAIAAPILHVNSKGCVEYEPNFSQEVQRGLQDRGQNQTQRPFFLNVVQAVSQEGACVYAVSDLRKSGEAAGY DEH6CAO TD Low tissue/organ specificity. DEH6CAO FC This enzyme cleaves the gamma-glutamyl peptide bond of glutathione conjugates, but maybe not glutathione itself. It converts leukotriene C4 (LTC4) to leukotriene D4 (LTD4). DEH6CAO KD 33208: Metazoa DEH6CAO PL 7711: Chordata DEH6CAO CL 40674: Mammalia DEH6CAO OD 9443: Primates DEH6CAO FM 9604: Hominidae DEH6CAO GE 9605: Homo DEH6CAO SP 9606: Homo sapiens DEXL3P2 ID DEXL3P2 DEXL3P2 DN Deoxycytidylate deaminase (DCTD) DEXL3P2 GN DCTD DEXL3P2 SN Methyldeoxycytidine monophosphate deaminase; 5-methyldeoxycytidine monophosphate deaminase; dCMP-dCTP deaminase; dCMP deaminase; DCTD DEXL3P2 UC DCTD_HUMAN DEXL3P2 RD Cytarabine DEXL3P2 GI 1635 DEXL3P2 E1 3: Hydrolases DEXL3P2 E2 3.5: Carbon-nitrogen hydrolase DEXL3P2 E3 3.5.4: Cyclic amidine hydrolase DEXL3P2 EC 3.5.4.12 DEXL3P2 RC Interconversion of nucleotide di- and triphosphates:R-HSA-499943 DEXL3P2 KG Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DEXL3P2 PD 2W4L DEXL3P2 SQ MSEVSCKKRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMPNGCSDDVLPWRRTAENKLDTKYPYVCHAELNAIMNKNSTDVKGCSMYVALFPCNECAKLIIQAGIKEVIFMSDKYHDSDEATAARLLFNMAGVTFRKFIPKCSKIVIDFDSINSRPSQKLQ DEXL3P2 TD Low tissue/organ specificity. DEXL3P2 FC This enzyme supplies the nucleotide substrate for thymidylate synthetase. DEXL3P2 KD 33208: Metazoa DEXL3P2 PL 7711: Chordata DEXL3P2 CL 40674: Mammalia DEXL3P2 OD 9443: Primates DEXL3P2 FM 9604: Hominidae DEXL3P2 GE 9605: Homo DEXL3P2 SP 9606: Homo sapiens DEMOQG5 ID DEMOQG5 DEMOQG5 DN Glutamate racemase (MurI) DEMOQG5 GN racE DEMOQG5 SN D-glutamate racemase; MurI; murI; BAS0806; BAS4379; BSU28390; BcGR; BsGR; BsRacE; DapF; FnGR; GBAA_0847; GBAA_4717 DEMOQG5 UC MURI1_BACSU DEMOQG5 RD L-glutamine DEMOQG5 GI 935934 DEMOQG5 E1 5: Isomerase DEMOQG5 E2 5.1: Racemase/epimerase DEMOQG5 E3 5.1.1: Amino acid racemase/epimerase DEMOQG5 EC 5.1.1.3 DEMOQG5 KG D-Glutamine and D-glutamate metabolism:bsu00471; Metabolic pathways:bsu01100 DEMOQG5 PD 1ZUW DEMOQG5 SQ MLEQPIGVIDSGVGGLTVAKEIMRQLPKENIIYVGDTKRCPYGPRPEEEVLQYTWELTNYLLENHHIKMLVIACNTATAIALDDIQRSVGIPVVGVIQPGARAAIKVTDNQHIGVIGTENTIKSNAYEEALLALNPDLKVENLACPLLVPFVESGKFLDKTADEIVKTSLYPLKDTSIDSLILGCTHYPILKEAIQRYMGEHVNIISSGDETAREVSTILSYKGLLNQSPIAPDHQFLTTGARDQFAKIADDWFGHEVGHVECISLQEPIKR DEMOQG5 TD Primarily distributed in human gut. DEMOQG5 FC This enzyme is a pyridoxal-phosphate protein providing the (R)-glutamate required for cell wall biosynthesis and converting L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine. DEMOQG5 KD 2: Bacteria DEMOQG5 PL 1239: Firmicutes DEMOQG5 CL 91061: Bacilli DEMOQG5 OD 1385: Bacillales DEMOQG5 FM 186817: Bacillaceae DEMOQG5 GE 1386: Bacillus DEMOQG5 SP 1423: Bacillus subtilis DEYB8JQ ID DEYB8JQ DEYB8JQ DN Glutamate racemase (MurI) DEYB8JQ GN yrpC DEYB8JQ SN D-glutamate racemase; MurI; murI; BAS0806; BAS4379; BSU26810; BcGR; BsGR; BsRacE; DapF; FnGR; GBAA_0847; GBAA_4717; yrpC DEYB8JQ UC MURI2_BACSU DEYB8JQ RD L-glutamine DEYB8JQ GI 937619 DEYB8JQ E1 5: Isomerase DEYB8JQ E2 5.1: Racemase/epimerase DEYB8JQ E3 5.1.1: Amino acid racemase/epimerase DEYB8JQ EC 5.1.1.3 DEYB8JQ KG D-Glutamine and D-glutamate metabolism:bsu00471; Metabolic pathways:bsu01100 DEYB8JQ SQ MKIGFFDSGIGGMTVLYEAIKVLPYEDYIFYADTLNVPYGEKSKGKVKEYIFNAAEFLASQNIKALVIACNTATSIAIEDLRRNFDFPIIGIEPAVKPAINKCTEERKRVLVVATNLTLKEEKFHNLVKEIDHHDLVDCLALPGLVEFAENFDFSEDKIIKYLKNELSSFDLKQYGTIVLGCTHFPFFKNSFEKLFGIKVDMISGSVGTAKQLKKVLADRNQLGKGSGSITFFNSGHKIVDQEVISKYKRLFEILDETQRSHVGH DEYB8JQ TD Primarily distributed in human gut. DEYB8JQ FC This enzyme is a pyridoxal-phosphate protein providing the (R)-glutamate required for cell wall biosynthesis and converting L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine. DEYB8JQ KD 2: Bacteria DEYB8JQ PL 1239: Firmicutes DEYB8JQ CL 91061: Bacilli DEYB8JQ OD 1385: Bacillales DEYB8JQ FM 186817: Bacillaceae DEYB8JQ GE 1386: Bacillus DEYB8JQ SP 1408: Bacillus pumilus DE21PLI ID DE21PLI DE21PLI DN NADPH-dependent nitroreductase (nfrA1) DE21PLI GN nfrA1 DE21PLI SN NADPH-dependent FMN reductase; NADPH-dependent nitro/flavin reductase; NADPH-dependent oxidoreductase; FMN reductase (NADPH); BSU38110; ipa-43d; nfrA1; ywcG DE21PLI UC NFRA1_BACSU DE21PLI RD Nitrofurantoin DE21PLI GI 937279 DE21PLI E1 1: Oxidoreductase DE21PLI E2 1.5: CH-NH donor oxidoreductase DE21PLI E3 1.5.1: NAD/NADP acceptor oxidoreductase DE21PLI EC 1.5.1.38 DE21PLI KG Metabolic pathways:bsu01100; Riboflavin metabolism:bsu00740 DE21PLI PD 3N2S DE21PLI SQ MNNTIETILNHRSIRSFTDQLLTAEEIDTLVKSAQAASTSSYVQAYSIIGVSDPEKKRELSVLAGNQPYVEKNGHFFVFCADLYRHQQLAEEKGEHISELLENTEMFMVSLIDAALAAQNMSIAAESMGLGICYIGGIRNELDKVTEVLQTPDHVLPLFGLAVGHPANLSGKKPRLPKQAVYHENTYNVNTDDFRHTMNTYDKTISDYYRERTNGKREETWSDQILNFMKQKPRTYLNDYVKEKGFNKN DE21PLI TD Primarily distributed in human gut. DE21PLI FC This enzyme can reduce FMNH(2) to FMN, with NADPH as reductant, and also can reduce nitroaromatic compounds, quinones and azo dyes. DE21PLI KD 2: Bacteria DE21PLI PL 1239: Firmicutes DE21PLI CL 91061: Bacilli DE21PLI OD 1385: Bacillales DE21PLI FM 186817: Bacillaceae DE21PLI GE 1386: Bacillus DE21PLI SP 1423: Bacillus subtilis DE2S6QE ID DE2S6QE DE2S6QE DN Arylamine N-acetyltransferase (NAT) DE2S6QE GN nat DE2S6QE SN N-hydroxyarylamine O-acetyltransferase; nhoA; nat; PWN146_00756 DE2S6QE UC A0A1C3HAL9_SERMA DE2S6QE RD Asacolitin DE2S6QE E1 2: Transferase DE2S6QE E2 2.3: Acyltransferase DE2S6QE E3 2.3.1: Acyltransferase DE2S6QE EC 2.3.1.5 DE2S6QE SQ MDTQRYLQHIGFIGAARPDLPTLQQLHHRHMLSVPFENLSIIYHQGIRLAPEALFSKVVERNRGGFCYELNTLFALLLREIGFKVSFISGEIRARDGHFGPPYDHLALRVDLEDQAWLVDVGFGDSFLTPLKIVVAEPQPQASGTFHLEQEGEYYLLERRNGDQRSHAKTLYRFTIQPRALHEFDEMCRFHSTSPQSHFTQRLVCSRPTDHGRVTLSDMKLIVTEDHQRHETTLHSEEERRAALWQHFAIDLDR DE2S6QE TD Primarily distributed in human gut. DE2S6QE FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DE2S6QE KD 2: Bacteria DE2S6QE PL 1224: Proteobacteria DE2S6QE CL 1236: Gammaproteobacteria DE2S6QE OD 91347: Enterobacterales DE2S6QE FM 1903411: Yersiniaceae DE2S6QE GE 613: Serratia DE2S6QE SP 615: Serratia marcescens DE07EIQ ID DE07EIQ DE07EIQ DN General stress protein 14 (ywrO) DE07EIQ GN ywrO DE07EIQ SN Alkyl hydroperoxide reductase; Reductase alkyl hydroperoxide; GS protein 14; GSP14; BSU35990; ywrO DE07EIQ UC GS14_BACSU DE07EIQ RD CBL-954 DE07EIQ GI 936853 DE07EIQ E1 1: Oxidoreductase DE07EIQ E2 1.6: NADH/NADPH oxidoreductase DE07EIQ E3 1.6.99: Other acceptor oxidoreductase DE07EIQ EC 1.6.99.- DE07EIQ SQ MKILVLAVHPHMETSVVNKAWAEELSKHDNITVRDLYKEYPDEAIDVAKEQQLCEEYDRIVFQFPLYWYSSPPLLKKWQDLVLTYGWAFGSEGNALHGKELMLAVSTGSEAEKYQAGGANHYSISELLKPFQATSNLIGMKYLPPYVFYGVNYAAAEDISHSAKRLAEYIQQPFV DE07EIQ TD Primarily distributed in human gut. DE07EIQ FC This enzyme has electron transfer activity, FMN binding, and NAD(P)H dehydrogenase (quinone) activity. DE07EIQ KD 2: Bacteria DE07EIQ PL 1239: Firmicutes DE07EIQ CL 91061: Bacilli DE07EIQ OD 1385: Bacillales DE07EIQ FM 186817: Bacillaceae DE07EIQ GE 1386: Bacillus DE07EIQ SP 1423: Bacillus subtilis DEYSOD0 ID DEYSOD0 DEYSOD0 DN Molybdopterin-dependent enzyme (molD) DEYSOD0 GN molD DEYSOD0 SN Molybdopterin-dependent oxidoreductase; Oxidoreductase molD; molD DEYSOD0 UC A0A327SQQ7_9ACTN DEYSOD0 RD Doxorubicin DEYSOD0 E1 1: Oxidoreductase DEYSOD0 E2 1.1: CH-OH donor oxidoreductase DEYSOD0 E3 1.1.1: NAD/NADP oxidoreductase DEYSOD0 EC 1.1.1.40 DEYSOD0 SQ MATFTPGFHGHRRTRGGRLPPGQFLTEDFPVLSAGPTPDIPLDRWEFTLTAESGERRRWNWQEFSALPQQEVTTDLHCVTRWSKFDTRWRGVSLDTLLNGVTTDARHALAECHGGYTTNLPLTDLRGGKAWIAHTYDGEPLTAEHGGPARLLVPHLYFWKSAKWISGITLRAEDHRGFWEQLGYHDHGDPWREQRTWND DEYSOD0 TD Primarily distributed in human gut. DEYSOD0 FC This enzyme catalyzes the conversion of doxorubicin to 7-deoxydoxorubicinol and 7-deoxydoxorubicinolone via a reductive deglycosylation mechanism. DEYSOD0 KD 2: Bacteria DEYSOD0 PL 1224: Proteobacteria DEYSOD0 CL 1236: Gammaproteobacteria DEYSOD0 OD 91347: Enterobacterales DEYSOD0 FM 543: Enterobacteriaceae DEYSOD0 GE 570: Klebsiella DEYSOD0 SP 573: Klebsiella pneumoniae DE0QGHP ID DE0QGHP DE0QGHP DN Insulin-degrading enzyme (ide) DE0QGHP GN ide DE0QGHP SN Insulin-degrading protein; Bacterial insulin protease; Bacterial insulinase; Bacterial insulysin DE0QGHP UC A0A0C1JXV9_9BACT DE0QGHP RD Insulin DE0QGHP E1 3: Hydrolases DE0QGHP E2 3.4: Peptidase DE0QGHP E3 3.4.24: Metallopeptidase DE0QGHP EC 3.4.24.56 DE0QGHP SQ MSDPLYSIFFKPSTIKAMKINYLIITLGCIGSLLGFPLLPALENKGYTLIEDKALLKVKTPTFSQTQVLKIKLNNGLQAVLISDPQTDQSSATLVVGAGSWQDPDPYPGLAHFVEHMLFLGTKKYPNESEFQRFITEHGGFSNAFTANDHTAYMFSIDNEAFPQALDRFASFFKEPLFNVSGIVRELNAIDQEYAKNYENDDVREVMVMKHIQNPRHPNYRFNIGNSTTLKAASQEILKAWYNEHYSSNIMRLLLVSNLPLEEMTRLTVDEFGDVADKHKVCYVPPMDLNNPDMEAKLFYITPIQNIRKLTLVWDLPQEFAEMKDTYPDRLICQVLGHEGKESLLAQLKREKLAENLGCSTFNLGEKNLVLFVQMELTDKGVQSIDRIILRCFQTLALMKEKPFPRYIYDEVRQINLLNYEYQQREEVFTAAMKNADLLVRENIATYPEQTKVIQKFSQADVQNLLDYLTPSNCRFLIQAPSSLTGVEPTHQEEWLQVAYAMKAIEPFKMQEWASATPIAEITLPLPNPFLPKSLDLLHALPSKETHLSRLPHPHLIEDSEHGTIYYAKDQHFLIPQLYLNFNIRTPAIDIGDANKIVMGDIYIKAVEENLSKFSYAATVAGLNFSVARTEYGLAFKITGYNDHAFLLFEEILKQLKDLKLSEQAFKIIKQSLLRRYQNFNKRAPLKRAKELFQQTIYKKYAAEHQKISAIRKLSFAKFQEDVQSLFRQSFVEGLIYGNVTENQAKEYADNLIKTLDSAPYPKQMHKHAEIINLSSAEGPLLLEMKIPVQGSATLLAIENSSFTLKERAAQQILMKAMKEPFFAELRTRQQTGYLISSAAEEIERKLFLAFVVQSNTHDPRDLLARFELFIESFLQGIEKNYLTLKNFEIIKNSLLEELEKPPHNMESLGALLHSLAFKYEGRFDWIDKRIQALRALTHGELLSFTHACIGKDNKRRLGLLIKGHMDKAKGLYYTLINTPEQLKQKSTFSSSWGNEEKERKLE DE0QGHP TD Primarily distributed in human gut. DE0QGHP FC This enzyme catalyzes the hydrolysis of insulin. DE0QGHP KD 2: Bacteria DE0QGHP PL 1224: Proteobacteria DE0QGHP CL 1236: Gammaproteobacteria DE0QGHP OD 135623: Vibrionales DE0QGHP FM 641: Vibrionaceae DE0QGHP GE 662: Vibrio DE0QGHP SP 672: Vibrio vulnificus DE5WGIM ID DE5WGIM DE5WGIM DN Aminoglycoside phosphotransferase (aph-Ib) DE5WGIM GN aph(2'')-Ib DE5WGIM SN Campylobacter jejuni aminoglycoside phosphotransferase; 2''-aminoglycoside phosphotransferase; Aph(2'')-Ib DE5WGIM UC A0A075C7U3_CAMJU DE5WGIM RD Sisomicin DE5WGIM E1 2: Transferase DE5WGIM E2 2.7: Kinase DE5WGIM E3 2.7.1: Phosphotransferase DE5WGIM EC 2.7.1.190 DE5WGIM SQ MIDLDVEIYQHLNEQIKINKLCYLSSGDDSDTFLCNEQYVVKVPKRDSVRFAQKREFELYRFLENCNLSYQTPAVVYQSDRFNIMKYIKGERITYEQYHKLSEKEKDALAYDEATFLKELHSIEIDCSVSLFSDALVNKKDKFLQDKKLLISILEKEQLLTDEMLEHIETIYENISSNAVIFNYIPCLVHNDFSANNLIFRNNRLFGVIDFGDFNVGDPDNDFLCLLDCSTDDFGKEFGRKVLKYYQHKAPEVAERKAELNDVYWSIDQIIYGYERKDREMLIKGVSELLQTQAEMFIF DE5WGIM TD Primarily distributed in human gut. DE5WGIM FC This enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci. And this bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. DE5WGIM KD 2: Bacteria DE5WGIM PL 1224: Proteobacteria DE5WGIM CL 29547: Epsilonproteobacteria DE5WGIM OD 213849: Campylobacterales DE5WGIM FM 72294: Campylobacteraceae DE5WGIM GE 194: Campylobacter DE5WGIM SP 197: Campylobacter jejuni DE0K82S ID DE0K82S DE0K82S DN Nitroreductase (NTR) DE0K82S GN yieF DE0K82S SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; AAK29_19565; AAP89_17340; ABO94_21460; AF480_20870; AF488_23150; AF489_23340; AIC76_20195; AU613_12225; AXR84_20760; AXU58_04975; C2253_16765; CD48_22070; CE87_20375; CET98_22760; CQG18_18555; CVR97_26810; D4369_19420; D4380_20855; D4401_19160; D4E62_20230; D6360_18430; D7F20_19765; D7H43_20545; DJ388_15780; DKJ11_20120; DKU57_16540; DLM31_17395; DNV30_18555; DO698_18905; DOJ90_20570; DOQ88_18330; DPJ93_20300; DQ848_17880; DRM14_15155; DSF69_18065; DSR36_20995; DUW48_14845; EBO41_17185; EBP31_19365; EGU67_18695; EHB24_16995; EHC98_18885; EIW53_20245; GW08_19510; LZ63_23085; NG18_18155; NU83_21515; QA89_14925; QB40_21055; QD15_17380; RJ78_20865; SAMEA4398682_04794; SBOV39431; Y934_22205; YG50_14570; YI33_18440; YR17_18395; ZA53_16690; ZB89_19155 DE0K82S UC A0A5K1UB29_SALTM DE0K82S RD Niclosamide DE0K82S E1 1: Oxidoreductase DE0K82S E2 1.5: CH-NH donor oxidoreductase DE0K82S E3 1.5.1: NAD/NADP acceptor oxidoreductase DE0K82S EC 1.5.1.39 DE0K82S SQ MKKGARMSETLNVVTLLGSLRKGSFNGMVARTLPKVAPAGMTVSPLPSIGDIPLYDADIQQEEGFPASVEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDWLSRLPEQPLAGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNKPEFMGGVIQNKVDPQTGEVVDQGTLDHLTGQLTAFGEFIQRVKA DE0K82S TD Primarily distributed in human gut. DE0K82S FC This enzyme catalyzes the reduction of a variety of nitroaromatic compounds. DE0K82S KD 2: Bacteria DE0K82S PL 1224: Proteobacteria DE0K82S CL 1236: Gammaproteobacteria DE0K82S OD 91347: Enterobacterales DE0K82S FM 543: Enterobacteriaceae DE0K82S GE 590: Salmonella DE0K82S SP 90371: Salmonella typhimurium DE0K82S SU Salmonella typhimurium subsp. enterica serovar Typhimurium DEPG9C0 ID DEPG9C0 DEPG9C0 DN Nitroreductase (NTR) DEPG9C0 GN yieF DEPG9C0 SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; AAK29_19565; AAP89_17340; ABO94_21460; AF480_20870; AF488_23150; AF489_23340; AIC76_20195; AU613_12225; AXR84_20760; AXU58_04975; C2253_16765; CD48_22070; CE87_20375; CET98_22760; CQG18_18555; CVR97_26810; D4369_19420; D4380_20855; D4401_19160; D4E62_20230; D6360_18430; D7F20_19765; D7H43_20545; DJ388_15780; DKJ11_20120; DKU57_16540; DLM31_17395; DNV30_18555; DO698_18905; DOJ90_20570; DOQ88_18330; DPJ93_20300; DQ848_17880; DRM14_15155; DSF69_18065; DSR36_20995; DUW48_14845; EBO41_17185; EBP31_19365; EGU67_18695; EHB24_16995; EHC98_18885; EIW53_20245; GW08_19510; LZ63_23085; NG18_18155; NU83_21515; QA89_14925; QB40_21055; QD15_17380; RJ78_20865; SAMEA4398682_04794; SBOV39431; Y934_22205; YG50_14570; YI33_18440; YR17_18395; ZA53_16690; ZB89_19155 DEPG9C0 UC A0A5K1UB29_SALTM DEPG9C0 RD Menadione DEPG9C0 E1 1: Oxidoreductase DEPG9C0 E2 1.5: CH-NH donor oxidoreductase DEPG9C0 E3 1.5.1: NAD/NADP acceptor oxidoreductase DEPG9C0 EC 1.5.1.39 DEPG9C0 SQ MKKGARMSETLNVVTLLGSLRKGSFNGMVARTLPKVAPAGMTVSPLPSIGDIPLYDADIQQEEGFPASVEALAEQIRNADGVVIVTPEYNYSVPGGLKNAIDWLSRLPEQPLAGKPVLIQTSSMGAIGGARCQYHLRQILVFLDAMVMNKPEFMGGVIQNKVDPQTGEVVDQGTLDHLTGQLTAFGEFIQRVKA DEPG9C0 TD Primarily distributed in human gut. DEPG9C0 FC This enzyme can reduce other azo dyes, such as Methyl Red, Rocceline, Solar Orange and Sumifix Black B. DEPG9C0 KD 2: Bacteria DEPG9C0 PL 1224: Proteobacteria DEPG9C0 CL 1236: Gammaproteobacteria DEPG9C0 OD 91347: Enterobacterales DEPG9C0 FM 543: Enterobacteriaceae DEPG9C0 GE 590: Salmonella DEPG9C0 SP 28901: Salmonella enterica DEPG9C0 SU Salmonella enterica subsp. enterica serovar Typhimurium DER6EU8 ID DER6EU8 DER6EU8 DN Homoserine-O-transsuccinylase (metAA) DER6EU8 GN metAA DER6EU8 SN Homoserine O-acetyltransferase; Homoserine acetyltransferase; Homoserine transacetylase; HTS-like HTA; HAT; HTA DER6EU8 UC METAA_THEMA DER6EU8 RD Methionine DER6EU8 E1 2: Transferase DER6EU8 E2 2.3: Acyltransferase DER6EU8 E3 2.3.1: Acyltransferase DER6EU8 EC 2.3.1.46 DER6EU8 KG Biosynthesis of amino acids:tma01230; Biosynthesis of secondary metabolites:tma01110; Cysteine and methionine metabolism:tma00270; Metabolic pathways:tma01100; Sulfur metabolism:tma00920 DER6EU8 PD 2H2W DER6EU8 SQ MPINVPSGLPAVKVLAKEGIFVMTEKRAIHQDIRPLEILILNLMPDKIKTEIQLLRLLGNTPLQVNVTLLYTETHKPKHTPIEHILKFYTTFSAVKDRKFDGFIITGAPVELLPFEEVDYWEELTEIMEWSRHNVYSTMFICWAAQAGLYYFYGIPKYELPQKLSGVYKHRVAKDSVLFRGHDDFFWAPHSRYTEVKKEDIDKVPELEILAESDEAGVYVVANKSERQIFVTGHPEYDRYTLRDEYYRDIGRNLKVPIPANYFPNDDPTKTPILTWWSHAHLFFSNWLNYCIYQKTPYRLEDIH DER6EU8 TD Primarily distributed in human gut. DER6EU8 FC This enzyme catalyzes the conversion of L-homoserine to O-succinyl-L-homoserine and takes part in methionine metabolism and sulfur metabolism. DER6EU8 KD 2: Bacteria DER6EU8 PL 1224: Proteobacteria DER6EU8 CL 1236: Gammaproteobacteria DER6EU8 OD 91347: Enterobacterales DER6EU8 FM 543: Enterobacteriaceae DER6EU8 GE 590: Salmonella DER6EU8 SP 28901: Salmonella enterica DER6EU8 SU Salmonella enterica subsp. enterica serovar Typhimurium DEP0IWS ID DEP0IWS DEP0IWS DN Beta-lactamase (blaB) DEP0IWS GN bla_2 DEP0IWS SN Penicillinase; Cephalosporinase; Beta-lactam; bla_2; NCTC5046_06338 DEP0IWS UC A0A378EHS6_KLEPR DEP0IWS RD Aztreonam DEP0IWS E1 3: Hydrolases DEP0IWS E2 3.5: Carbon-nitrogen hydrolase DEP0IWS E3 3.5.2: Cyclic amide hydrolase DEP0IWS EC 3.5.2.6 DEP0IWS SQ MVMRYIRLCIISLLATLPLAVHASPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPRRRPATPLPRPAWPRPCASC DEP0IWS TD Primarily distributed in human lung. DEP0IWS FC This enzyme hydrolyzes beta-lactam. DEP0IWS KD 2: Bacteria DEP0IWS PL 1224: Proteobacteria DEP0IWS CL 1236: Gammaproteobacteria DEP0IWS OD 91347: Enterobacterales DEP0IWS FM 543: Enterobacteriaceae DEP0IWS GE 570: Klebsiella DEP0IWS SP 573: Klebsiella pneumoniae DEP0IWS SU Klebsiella pneumoniae subsp. Rhinoscleromatis DEEAL81 ID DEEAL81 DEEAL81 DN Beta-lactamase (blaB) DEEAL81 GN bla DEEAL81 SN Penicillinase; Cephalosporinase; Beta-lactam; Beta-lactamase SHV-2; SHV-2A; bla; shv2 DEEAL81 UC BLA2_KLEPO DEEAL81 RD Ceftriaxone DEEAL81 E1 3: Hydrolases DEEAL81 E2 3.5: Carbon-nitrogen hydrolase DEEAL81 E3 3.5.2: Cyclic amide hydrolase DEEAL81 EC 3.5.2.6 DEEAL81 SQ MRYIRLCIISLLATLPLAVHASPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGASERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR DEEAL81 TD Primarily distributed in human lung. DEEAL81 FC This enzyme hydrolyzes cefotaxime, ceftazidime and other broad spectrum cephalosporins. DEEAL81 KD 2: Bacteria DEEAL81 PL 1224: Proteobacteria DEEAL81 CL 1236: Gammaproteobacteria DEEAL81 OD 91347: Enterobacterales DEEAL81 FM 543: Enterobacteriaceae DEEAL81 GE 570: Klebsiella DEEAL81 SP 244366: Klebsiella variicola DEEAL81 SU Klebsiella variicola subsp. Ozaenae DETX3A5 ID DETX3A5 DETX3A5 DN Cytidine deaminase (cdd) DETX3A5 GN cdd DETX3A5 SN Cytidine aminohydrolase; Activation-induced cytidine deaminase; Canine hepatic cyd deaminase; AICDA; JW2131; b2143 DETX3A5 UC CDD_ECOLI DETX3A5 RD Gemcitabine DETX3A5 GI 946663 DETX3A5 E1 3: Hydrolases DETX3A5 E2 3.5: Carbon-nitrogen hydrolase DETX3A5 E3 3.5.4: Cyclic amidine hydrolase DETX3A5 EC 3.5.4.5 DETX3A5 KG Metabolic pathways:ecj01100; Pyrimidine metabolism:ecj00240 DETX3A5 PD 1AF2; 1ALN; 1CTT; 1CTU DETX3A5 SQ MHPRFQTAFAQLADNLQSALEPILADKYFPALLTGEQVSSLKSATGLDEDALAFALLPLAAACARTPLSNFNVGAIARGVSGTWYFGANMEFIGATMQQTVHAEQSAISHAWLSGEKALAAITVNYTPCGHCRQFMNELNSGLDLRIHLPGREAHALRDYLPDAFGPKDLEIKTLLMDEQDHGYALTGDALSQAAIAAANRSHMPYSKSPSGVALECKDGRIFSGSYAENAAFNPTLPPLQGALILLNLKGYDYPDIQRAVLAEKADAPLIQWDATSATLKALGCHSIDRVLLA DETX3A5 TD Primarily distributed in human gut. DETX3A5 FC This enzyme catalyzes the deamination of cytidine and 2'-deoxycytidine with similar efficiencies. It is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. DETX3A5 KD 2: Bacteria DETX3A5 PL 1224: Proteobacteria DETX3A5 CL 1236: Gammaproteobacteria DETX3A5 OD 91347: Enterobacterales DETX3A5 FM 543: Enterobacteriaceae DETX3A5 GE 561: Escherichia DETX3A5 SP 562: Escherichia coli DETX3A5 SU Escherichia coli K-12 DEFVABT ID DEFVABT DEFVABT DN Cytidine deaminase (cdd) DEFVABT GN cdd DEFVABT SN Cytidine aminohydrolase; Activation-induced cytidine deaminase; Canine hepatic cyd deaminase; AICDA; KPN78578_25410; KPN_02584 DEFVABT UC CDD_KLEP7 DEFVABT RD Gemcitabine DEFVABT E1 3: Hydrolases DEFVABT E2 3.5: Carbon-nitrogen hydrolase DEFVABT E3 3.5.4: Cyclic amidine hydrolase DEFVABT EC 3.5.4.5 DEFVABT KG Metabolic pathways:kpn01100; Pyrimidine metabolism:kpn00240 DEFVABT PD 6K63 DEFVABT SQ MHSRFQAALTTLAADLQAAIAPMLADPHFPALLEADQVATLQHATGLDEDALAFALLPLAAACARPDLSHFNVGAIARGVSGRWYFGGNMEFLGATMQQTVHAEQSAISHAWLRGETSLRAITVNYTPCGHCRQFMNELNSGLALRIHLPGREAHALEHYLPDAFGPKDLEIKTLLMDEQDHGFPVSGDALTQAAIQAANRCHAPYSHSPSGVALELKDGTIFSGSYAENAAFNPTLPPLQGALNLLSLNGYDYPAIQRAILAEKADAALIQWDATVATLKALGCHNIERVLLG DEFVABT TD Primarily distributed in human gut. DEFVABT FC This enzyme catalyzes the deamination of cytidine and 2'-deoxycytidine with similar efficiencies. It is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. DEFVABT KD 2: Bacteria DEFVABT PL 1224: Proteobacteria DEFVABT CL 1236: Gammaproteobacteria DEFVABT OD 91347: Enterobacterales DEFVABT FM 543: Enterobacteriaceae DEFVABT GE 570: Klebsiella DEFVABT SP 573: Klebsiella pneumoniae DEF5JD3 ID DEF5JD3 DEF5JD3 DN Arylamine N-acetyltransferase (NAT) DEF5JD3 GN nhoA_1 DEF5JD3 SN N-hydroxyarylamine O-acetyltransferase; nhoA; nhoA_1; SAMEA1713070_01652 DEF5JD3 UC A0A1C3Q7F5_KLEPN DEF5JD3 RD Asacolitin DEF5JD3 E1 2: Transferase DEF5JD3 E2 2.3: Acyltransferase DEF5JD3 E3 2.3.1: Acyltransferase DEF5JD3 EC 2.3.1.5 DEF5JD3 SQ MSPFLRAYFSRLGWTGEPDVSIDTLRQLHLQHNSAIPFENLDVLLPREIHLDDLALEAKLIAGRRGGYCFEQNGLLERALREIGFNVRSLLGRVVLANPPQMPPRTHRLLLVEVAGERWIADVGFGGQTLTAPIKLLADIPQQTPHGSYRLVHEGDEWTLQFNHHEHWQSMYHFDLGRQYASDYVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKMTLTNFHFTHWENNHVVEKVDFADVSALYEGLQTRFGLGVDDPKHGFSEAALAAVMAAFDTHPEAGK DEF5JD3 TD Primarily distributed in human gut. DEF5JD3 FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DEF5JD3 KD 2: Bacteria DEF5JD3 PL 1224: Proteobacteria DEF5JD3 CL 1236: Gammaproteobacteria DEF5JD3 OD 91347: Enterobacterales DEF5JD3 FM 543: Enterobacteriaceae DEF5JD3 GE 570: Klebsiella DEF5JD3 SP 573: Klebsiella pneumoniae DEF5JD3 SU Klebsiella pneumoniae subsp. Ozaenae; Klebsiella pneumoniae subsp. Rhinoscleromatis DE1DR6Y ID DE1DR6Y DE1DR6Y DN S-adenosylhomocysteine nucleosidase (mtnN) DE1DR6Y GN mtnN DE1DR6Y SN AdoHcy nucleosidase; DOA nucleosidase; MTA nucleosidase; MTA/SAH nucleosidase; MTAN; SAH nucleosidase; SRH nucleosidase; dAdo nucleosidase; 5'-deoxyadenosine nucleosidase; 5'-methylthioadenosine nucleosidase; 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase; mtnN DE1DR6Y UC MTNN_KLEPN DE1DR6Y RD Methylthioadenosine DE1DR6Y E1 3: Hydrolases DE1DR6Y E2 3.2: Glycosylase DE1DR6Y E3 3.2.2: N-Glycosyl compound glycosidase DE1DR6Y EC 3.2.2.9 DE1DR6Y SQ MKIGIIGAMEEEVTLLRDKIENRQTITIGGSEIYT DE1DR6Y TD Primarily distributed in human gut. DE1DR6Y FC This enzyme acts on S-methyl-5'-thioadenosine to give adenine and S-methyl-5-thioribose. DE1DR6Y KD 2: Bacteria DE1DR6Y PL 1224: Proteobacteria DE1DR6Y CL 1236: Gammaproteobacteria DE1DR6Y OD 91347: Enterobacterales DE1DR6Y FM 543: Enterobacteriaceae DE1DR6Y GE 570: Klebsiella DE1DR6Y SP 573: Klebsiella pneumoniae DEX5D46 ID DEX5D46 DEX5D46 DN Oxygen-insensitive NADPH nitroreductase A (nfsA) DEX5D46 GN nfsA DEX5D46 SN Oxygen-insensitive NAD(P)H nitroreductase A; Modulator of drug activity A; STM0874; mdaA; nfsA; pnrA; snrA DEX5D46 UC NFSA_SALTY DEX5D46 RD RO-7-0207 DEX5D46 GI 1252393 DEX5D46 E1 1: Oxidoreductase DEX5D46 E2 1.5: CH-NH donor oxidoreductase DEX5D46 E3 1.5.1: NAD/NADP acceptor oxidoreductase DEX5D46 EC 1.5.1.38 DEX5D46 KG Microbial metabolism in diverse environments:stm01120; Nitrotoluene degradation:stm00633 DEX5D46 SQ MSPTIELLCGHRSIRHFTDEPVTDAQREAIIAAARSTSSSSFLQCSSIIRITDRALREALVPLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMGQNALTAAESLGLGGVYIGGIRNNIESVTELLKLPKHVLPLFGLCLGWPADNPDLKPRLPAELVVHENQYQPLDEKLLARYDEQLAEYYLTRGSNTRRDTWSDHIRRTLIKENRPFILEYLHKQGWATR DEX5D46 TD Primarily distributed in human gut. DEX5D46 FC This enzyme catalyzes the reduction of nitroaromatic compounds using NADPH, and has a broad electron acceptor specificity. Moreover, it reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. DEX5D46 KD 2: Bacteria DEX5D46 PL 1224: Proteobacteria DEX5D46 CL 1236: Gammaproteobacteria DEX5D46 OD 91347: Enterobacterales DEX5D46 FM 543: Enterobacteriaceae DEX5D46 GE 590: Salmonella DEX5D46 SP 28901: Salmonella enterica DEX5D46 SU Salmonella enterica subsp. enterica serovar Typhimurium; Salmonella enterica subsp. enterica serovar Typhimurium TA100 DEK9VG2 ID DEK9VG2 DEK9VG2 DN Metallo-beta-lactamase (blaM) DEK9VG2 GN blaNDM-1 DEK9VG2 SN Metallo-beta-lactamase NDM-1; New Delhi metallo-beta-lactamase-1; Metallo-beta-lactamase type 2c; Metallo-beta-lactamase type IIc; B2 metallo-beta-lactamase; Beta-lactamase type IIc; NDM-1; blaNDM-1 DEK9VG2 UC BLAN1_KLEPN DEK9VG2 RD Amoxicillin DEK9VG2 GI 11934636 DEK9VG2 E1 3: Hydrolases DEK9VG2 E2 3.5: Carbon-nitrogen hydrolase DEK9VG2 E3 3.5.2: Cyclic amide hydrolase DEK9VG2 EC 3.5.2.6 DEK9VG2 PD 3PG4; 3RKJ; 3RKK; 3SBL; 3SFP; 3SPU; A/B/C/D/E=27-270; 3SRX; 3ZR9; 4EXS; 4EXY; 4EY2; 4EYB; 4EYF; 4EYL; 4GYQ; 4GYU; 4H0D; 4HKY; 4HL1; 4HL2; 4RAM; 4RAW; 4RBS; 4RL0; 4RL2; 4RM5; 4U4L; 5A5Z; 5JQJ; 5K4M; 5N0H; 5N0I; 5NBK; 5O2E; 5O2F; 5WIG; 5XP6; 5XP9; 5ZGE; 5ZGF; 5ZGI; 5ZGP; 5ZGQ; 5ZGR; 5ZGT; 5ZGU; 5ZGV; 5ZGW; 5ZGX; 5ZGY; 5ZGZ; 5ZH1; 5ZIO; 5ZJ1; 5ZJ2; 5ZJ7; 5ZJ8; 5ZJC; 6C6I; 6CAC; 6D1A; 6D1B; 6D1C; 6D1D; 6D1E; 6D1F; 6D1G; 6D1H; 6D1I; 6D1J; 6D1K; 6EFJ; 6EX7; 6IBS; 6IBV; 6MDU; 6MGY; 6MGZ; 6Q2Y; 6Q30; 6RMF DEK9VG2 SQ MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR DEK9VG2 TD Primarily distributed in human gut. DEK9VG2 FC This enzyme confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring but does not confer resistance to the polymixin colistin or the fluoroquinolone ciprofloxacin. DEK9VG2 KD 2: Bacteria DEK9VG2 PL 1224: Proteobacteria DEK9VG2 CL 1236: Gammaproteobacteria DEK9VG2 OD 91347: Enterobacterales DEK9VG2 FM 543: Enterobacteriaceae DEK9VG2 GE 570: Klebsiella DEK9VG2 SP 573: Klebsiella pneumoniae DEK9VG2 SU Klebsiella pneumoniae KUN5033 DEOG0C9 ID DEOG0C9 DEOG0C9 DN Glutamate decarboxylase (gadB) DEOG0C9 GN gadB DEOG0C9 SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; GAD-beta; lmo2363 DEOG0C9 UC DCEB_LISMO DEOG0C9 RD L-glutamine DEOG0C9 GI 985123 DEOG0C9 E1 4: Lyases DEOG0C9 E2 4.1: Carbon-carbon lyase DEOG0C9 E3 4.1.1: Carboxy-lyase DEOG0C9 EC 4.1.1.15 DEOG0C9 KG Alanine, aspartate and glutamate metabolism:lmo00250; Biosynthesis of secondary metabolites:lmo01110; Butanoate metabolism:lmo00650; Metabolic pathways:lmo01100; Microbial metabolism in diverse environments:lmo01120; Quorum sensing:lmo02024; Taurine and hypotaurine metabolism:lmo00430; beta-Alanine metabolism:lmo00410 DEOG0C9 SQ MLYSKENKESYLEPVFGSSAEDRDIPKYTLGKEPLEPRIAYRLVKDELLDEGSARQNLATFCQTYMEDEATKLMSETLEKNAIDKSEYPRTAELENRCVNIIADLWHAPKDQKFMGTSTIGSSEACMLGGMAMKFAWRKRAEKLGLDIYAKKPNLVISSGYQVCWEKFCVYWDIDMRVVPMDKEHMQLNTDQVLDYVDEYTIGVVGILGITYTGRYDDIYALNEKLEEYNSKTDYKVYIHVDAASGGFFTPFVEPDIIWDFRLKNVISINTSGHKYGLVYPGIGWVLWKDESYLPEELIFKVSYLGGEMPTMQINFSRSASHIIGQYYNFLRYGFEGYRTIHQKTSDVAQYLAHAVEQTGYFDIFNDGSHLPIVCYKLKDDANVNWTLYDLADRLQMRGWQVPAYPLPKSLENIIIQRYVCRADLGFNMAEEFIQDFQASIQELNNAHILFHDTQQSGVHGFTH DEOG0C9 TD Primarily distributed in human gut. DEOG0C9 FC This enzyme converts internalized glutamate to GABA. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DEOG0C9 KD 2: Bacteria DEOG0C9 PL 1239: Firmicutes DEOG0C9 CL 91061: Bacilli DEOG0C9 OD 1385: Bacillales DEOG0C9 FM 186820: Listeriaceae DEOG0C9 GE 1637: Listeria DEOG0C9 SP 1639: Listeria monocytogenes DEW193R ID DEW193R DEW193R DN Beta-lactamase (blaB) DEW193R GN bla DEW193R SN Penicillinase; Cephalosporinase; Beta-lactam; Beta-lactamase SHV-1; PIT-2; bla; shv1 DEW193R UC BLA1_KLEPN DEW193R RD Amoxicillin DEW193R GI 39633152 DEW193R E1 3: Hydrolases DEW193R E2 3.5: Carbon-nitrogen hydrolase DEW193R E3 3.5.2: Cyclic amide hydrolase DEW193R EC 3.5.2.6 DEW193R PD 1ONG; 1Q2P; 1RCJ; 1SHV; 1TDG; 1TDL; 1VM1; 2A3U; 2A49; 2G2U; 2G2W; 2H0T; 2H0Y; 2H10; 2H5S; 3D4F; 3MKE; 3MKF; 3MXR; 3MXS; 3N4I; 3OPH; 3OPL; 3OPP; 3OPR; 3V50; 3V5M; 4FCF; 4FD8; 4FH2; 4FH4; 4GD6; 4GD8; 4GDB; 4JPM; 4MBF; 4MBH; 4MBK; 4R3B; 4ZAM; 5EE8 DEW193R SQ MRYIRLCIISLLATLPLAVHASPQPLEQIKLSESQLSGRVGMIEMDLASGRTLTAWRADERFPMMSTFKVVLCGAVLARVDAGDEQLERKIHYRQQDLVDYSPVSEKHLADGMTVGELCAAAITMSDNSAANLLLATVGGPAGLTAFLRQIGDNVTRLDRWETELNEALPGDARDTTTPASMAATLRKLLTSQRLSARSQRQLLQWMVDDRVAGPLIRSVLPAGWFIADKTGAGERGARGIVALLGPNNKAERIVVIYLRDTPASMAERNQQIAGIGAALIEHWQR DEW193R TD Primarily distributed in human gut. DEW193R FC This enzyme hydrolyzes beta-lactam. DEW193R KD 2: Bacteria DEW193R PL 1224: Proteobacteria DEW193R CL 1236: Gammaproteobacteria DEW193R OD 91347: Enterobacterales DEW193R FM 543: Enterobacteriaceae DEW193R GE 570: Klebsiella DEW193R SP 548: Klebsiella aerogenes DEW193R SU Klebsiella aerogenes KUN4843 DEJ01UG ID DEJ01UG DEJ01UG DN Arylamine N-acetyltransferase (NAT) DEJ01UG GN nhoA DEJ01UG SN N-hydroxyarylamine O-acetyltransferase; nhoA; Arylamine N-acetyltransferase/N-hydroxyarylamine O-acetyltransferase; Arylhydroxamate N,O-acetyltransferase; NAT101; STM1582 DEJ01UG UC NHOA_SALTY DEJ01UG RD Asacolitin DEJ01UG GI 1253100 DEJ01UG E1 2: Transferase DEJ01UG E2 2.3: Acyltransferase DEJ01UG E3 2.3.1: Acyltransferase DEJ01UG EC 2.3.1.5 DEJ01UG PD 1E2T DEJ01UG SQ MTSFLHAYFTRLHCQPLGVPTVEALRTLHLAHNCAIPFENLDVLLPREIQLDETALEEKLLYARRGGYCFELNGLFERALRDIGFNVRSLLGRVILSHPASLPPRTHRLLLVDVEDEQWIADVGFGGQTLTAPLRLQAEIAQQTPHGEYRLMQEGSTWILQFRHHEHWQSMYCFDLGVQQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTRYHQGHAVEQVNVPDVPSLYQLLQQQFGLGVNDVKHGFTEAELAAVMAAFDTHPEAGK DEJ01UG TD Primarily distributed in human gut. DEJ01UG FC This enzyme catalyzes both the acetyl-CoA-dependent N-acetylation of aromatic amines and the O-acetylation of N-hydroxyarylamines. And in vitro, it catalyzes the O-acetylation of N-hydroxy-Glu-P-1, and the N-acetylation of isoniazid and 2-aminofluorene. DEJ01UG KD 2: Bacteria DEJ01UG PL 1224: Proteobacteria DEJ01UG CL 1236: Gammaproteobacteria DEJ01UG OD 91347: Enterobacterales DEJ01UG FM 543: Enterobacteriaceae DEJ01UG GE 590: Salmonella DEJ01UG SP 28901: Salmonella enterica DERQS6E ID DERQS6E DERQS6E DN Nicotinamidase (pncA) DERQS6E GN pncA DERQS6E SN Nicotinamide deamidase; Pyrazinamidase; Bifunctional protein; NAMase; PZAase; ABAYE0059; pncA DERQS6E UC B0VA03_ACIBY DERQS6E RD Pyrazinamide DERQS6E E1 3: Hydrolases DERQS6E E2 3.5: Carbon-nitrogen hydrolase DERQS6E E3 3.5.1: Linear amide hydrolase DERQS6E EC 3.5.1.19 DERQS6E KG Metabolic pathways:aby01100; Nicotinate and nicotinamide metabolism:aby00760 DERQS6E PD 2WT9; 2WTA DERQS6E SQ MKMNKQPQNSALVVVDVQNGFTPGGNLAVADADTIIPTINQLAGCFENVVLTQDWHPDNHISFAANHPGKQPFETIELDYGSQVLWPKHCIQGTHDAEFHPDLNIPTAQLIIRKGFHAHIDSYSAFMEADHTTMTGLTGYLKERGIDTVYVVGIATDFCVAWTALDAVKQGFKTLVIEDACKGIDLNGSLEQAWQTMQQQGVVRIQSTDLLNEC DERQS6E TD Primarily distributed in human lung. DERQS6E FC This enzyme acts on carbon-nitrogen bonds and takes part in nicotinate and nicotinamide metabolism. DERQS6E KD 2: Bacteria DERQS6E PL 1224: Proteobacteria DERQS6E CL 1236: Gammaproteobacteria DERQS6E OD 72274: Pseudomonadales DERQS6E FM 468: Moraxellaceae DERQS6E GE 469: Acinetobacter DERQS6E SP 470: Acinetobacter baumannii DEBGCYQ ID DEBGCYQ DEBGCYQ DN New delhi metallo-beta-lactamase NDM-1 (blaNDM) DEBGCYQ GN blaNDM DEBGCYQ SN Metallo-beta-lactamase new delhi NDM-1; Metallo-beta-lactamase new delhi NDM1; blaNDM; NDM1 DEBGCYQ UC A0A345N7K5_SALET DEBGCYQ RD Meropenem DEBGCYQ E1 3: Hydrolases DEBGCYQ E2 3.5: Carbon-nitrogen hydrolase DEBGCYQ E3 3.5.2: Cyclic amide hydrolase DEBGCYQ EC 3.5.2.6 DEBGCYQ SQ MELPNIMHPVAKLSTALAAALMLSGCMPGEIRPTIGQQMETGDQRFGDLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLVVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQEGMVAAQHSLTFAANGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKLR DEBGCYQ TD Primarily distributed in human gut. DEBGCYQ FC This enzyme hydrolyzes beta-lactam. DEBGCYQ KD 2: Bacteria DEBGCYQ PL 1224: Proteobacteria DEBGCYQ CL 1236: Gammaproteobacteria DEBGCYQ OD 91347: Enterobacterales DEBGCYQ FM 543: Enterobacteriaceae DEBGCYQ GE 590: Salmonella DEBGCYQ SP 28901: Salmonella enterica DEBGCYQ SU Salmonella enterica subsp. enterica DESRNDP ID DESRNDP DESRNDP DN Hydroxybenzoate 3-monooxygenase (pobA) DESRNDP GN pobA DESRNDP SN Hydroxybenzoate hydroxylase; 4-hydroxybenzoate 3-monooxygenase; p-hydroxybenzoate hydroxylase; PHBH; pobA DESRNDP UC PHHY_PSEFL DESRNDP RD Tetracycline DESRNDP E1 1: Oxidoreductase DESRNDP E2 1.14: Oxygen paired donor oxidoreductase DESRNDP E3 1.14.13: NADH/NADPH donor oxidoreductase DESRNDP EC 1.14.13.2 DESRNDP PD 1BF3; 1BGJ; 1BGN; 1BKW; 1CC4; 1CC6; 1CJ2; 1CJ3; 1CJ4; 1PBB; 1PBC; 1PBD; 1PBE; 1PBF; 1PDH DESRNDP SQ MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE DESRNDP TD Primarily distributed in human gut. DESRNDP FC This enzyme is a flavoprotein (FAD) and can catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). DESRNDP KD 2: Bacteria DESRNDP PL 1224: Proteobacteria DESRNDP CL 1236: Gammaproteobacteria DESRNDP OD 72274: Pseudomonadales DESRNDP FM 135621: Pseudomonadaceae DESRNDP GE 286: Pseudomonas DESRNDP SP 294: Pseudomonas fluorescens DEWPAJD ID DEWPAJD DEWPAJD DN Aminoglycoside O-phosphotransferase (aphA6) DEWPAJD GN aphA-6 DEWPAJD SN Aminoglycoside 3'-phosphotransferase; Kanamycin kinase, type VI; Neomycin-kanamycin phosphotransferase type VI; APH(3')VI; aphA-6 DEWPAJD UC KKA6_ACIBA DEWPAJD RD Kanamycin DEWPAJD GI 20472049 DEWPAJD E1 2: Transferase DEWPAJD E2 2.7: Kinase DEWPAJD E3 2.7.1: Phosphotransferase DEWPAJD EC 2.7.1.95 DEWPAJD PD 1P40 DEWPAJD SQ MELPNIIQQFIGNSVLEPNKIGQSPSDVYSFNRNNETFFLKRSSTLYTETTYSVSREAKMLSWLSEKLKVPELIMTFQDEQFEFMITKAINAKPISALFLTDQELLAIYKEALNLLNSIAIIDCPFISNIDHRLKESKFFIDNQLLDDIDQDDFDTELWGDHKTYLSLWNELTETRVEERLVFSHGDITDSNIFIDKFNEIYFLDLGRAGLADEFVDISFVERCLREDASEETAKIFLKHLKNDRPDKRNYFLKLDELN DEWPAJD TD Primarily distributed in human lung. DEWPAJD FC This enzyme acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A. DEWPAJD KD 2: Bacteria DEWPAJD PL 1224: Proteobacteria DEWPAJD CL 1236: Gammaproteobacteria DEWPAJD OD 72274: Pseudomonadales DEWPAJD FM 468: Moraxellaceae DEWPAJD GE 469: Acinetobacter DEWPAJD SP 470: Acinetobacter baumannii DEJADS9 ID DEJADS9 DEJADS9 DN Aminoglycoside N-acetyltransferase (aacC2) DEJADS9 GN aacC2 DEJADS9 SN Aminoglycoside N(6')-acetyltransferase type 1; Aminoglycoside resistance protein; AAC(6')-Ih DEJADS9 UC AAC6_ACIBA DEJADS9 RD Netilmicin DEJADS9 GI 23000000 DEJADS9 E1 2: Transferase DEJADS9 E2 2.3: Acyltransferase DEJADS9 E3 2.3.1: Acyltransferase DEJADS9 EC 2.3.1.82 DEJADS9 PD 4E8O DEJADS9 SQ MNIMPISESQLSDWLALRCLLWPDHEDVHLQEMRQLITQAHRLQLLAYTDTQQAIAMLEASIRYEYVNGTQTSPVAFLEGIFVLPEYRRSGIATGLVQQVEIWAKQFACTEFASDAALDNQISHAMHQALGFHETERVVYFKKNIG DEJADS9 TD Primarily distributed in human lung. DEJADS9 FC This enzyme catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin, kanamycin, tobramycin and netilmicin. DEJADS9 KD 2: Bacteria DEJADS9 PL 1224: Proteobacteria DEJADS9 CL 1236: Gammaproteobacteria DEJADS9 OD 72274: Pseudomonadales DEJADS9 FM 468: Moraxellaceae DEJADS9 GE 469: Acinetobacter DEJADS9 SP 470: Acinetobacter baumannii DE4OGUF ID DE4OGUF DE4OGUF DN Cytochrome P450 102A1 (cyp102) DE4OGUF GN cyp102A1 DE4OGUF SN Cytochrome P450 family 102 subfamily A member 1; Flavocytochrome P450 102A1; P450 102A1; cyp102A1 DE4OGUF UC CPXB_BACMB DE4OGUF RD Acetaminophen DE4OGUF GI 29911283 DE4OGUF E1 1: Oxidoreductase DE4OGUF E2 1.14: Oxygen paired donor oxidoreductase DE4OGUF E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE4OGUF EC 1.14.14.1 DE4OGUF KG Aminobenzoate degradation:bmeg00627; Fatty acid degradation:bmeg00071; Microbial metabolism in diverse environments:bmeg01120; Tryptophan metabolism:bmeg00380 DE4OGUF PD 1BU7; 1BVY; 1FAG; 1FAH; 1JME; 1JPZ; 1P0V; 1P0W; 1P0X; 1SMI; 1SMJ; 1YQO; 1YQP; 1ZO4; 1ZO9; 1ZOA; 2BMH; 2HPD; 2IJ2; 2IJ3; 2IJ4; 2J1M; 2J4S; 2NNB; 2UWH; 2X7Y; 2X80; 3BEN; 3CBD; 3DGI; 3EKB; 3EKD; 3EKF; 3HF2; 3KX3; 3KX4; 3KX5; 3M4V; 3NPL; 3PSX; 3WSP; 4DQK; 4DQL; 4DTW; 4DTY; 4DTZ; 4DU2; 4DUA; 4DUB; 4DUC; 4DUD; 4DUE; 4DUF; 4H23; 4H24; 4HGF; 4HGG; 4HGH; 4HGI; 4HGJ; 4KEW; 4KEY; 4KF0; 4KF2; 4KPA; 4KPB; 4O4P; 4RSN; 4WG2; 4ZF6; 4ZF8; 4ZFA; 4ZFB; 5B2U; 5B2V; 5B2W; 5B2X; 5B2Y; 5DYP; 5DYZ; 5E78; 5E7Y; 5E9Z; 5JQ2; 5JQU; 5JQV; 5JTD; 5OG9; 5UCW; 5XA3; 5XHJ; 5ZIS; 5ZLH; 6H1O; 6H1S; 6IAO DE4OGUF SQ MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGIPSPSTEQSAKKVRKKAENAHNTPLLVLYGSNMGTAEGTARDLADIAMSKGFAPQVATLDSHAGNLPREGAVLIVTASYNGHPPDNAKQFVDWLDQASADEVKGVRYSVFGCGDKNWATTYQKVPAFIDETLAAKGAENIADRGEADASDDFEGTYEEWREHMWSDVAAYFNLDIENSEDNKSTLSLQFVDSAADMPLAKMHGAFSTNVVASKELQQPGSARSTRHLEIELPKEASYQEGDHLGVIPRNYEGIVNRVTARFGLDASQQIRLEAEEEKLAHLPLAKTVSVEELLQYVELQDPVTRTQLRAMAAKTVCPPHKVELEALLEKQAYKEQVLAKRLTMLELLEKYPACEMKFSEFIALLPSIRPRYYSISSSPRVDEKQASITVSVVSGEAWSGYGEYKGIASNYLAELQEGDTITCFISTPQSEFTLPKDPETPLIMVGPGTGVAPFRGFVQARKQLKEQGQSLGEAHLYFGCRSPHEDYLYQEELENAQSEGIITLHTAFSRMPNQPKTYVQHVMEQDGKKLIELLDQGAHFYICGDGSQMAPAVEATLMKSYADVHQVSEADARLWLQQLEEKGRYAKDVWAG DE4OGUF TD Primarily distributed in human gut. DE4OGUF FC This enzyme is P-450 heme-thiolate protein, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. DE4OGUF KD 2: Bacteria DE4OGUF PL 1239: Firmicutes DE4OGUF CL 91061: Bacilli DE4OGUF OD 1385: Bacillales DE4OGUF FM 186817: Bacillaceae DE4OGUF GE 1386: Bacillus DE4OGUF SP 1404: Bacillus megaterium DE3HL9N ID DE3HL9N DE3HL9N DN Tyrosine decarboxylase (tdc) DE3HL9N GN tdc DE3HL9N SN Levodopa decarboxylase; L-dopa decarboxylase; L-tyrosine decarboxylase; TDC; tdc; tdcA; EF_0634 DE3HL9N UC TYRDC_ENTFA DE3HL9N RD Levodopa DE3HL9N GI 1199535 DE3HL9N E1 4: Lyases DE3HL9N E2 4.1: Carbon-carbon lyase DE3HL9N E3 4.1.1: Carboxy-lyase DE3HL9N EC 4.1.1.25 DE3HL9N KG Metabolic pathways:efa01100; Tyrosine metabolism:efa00350 DE3HL9N SQ MKNEKLAKGEMNLNALFIGDKAENGQLYKDLLIDLVDEHLGWRQNYMPQDMPVISSQERTSESYEKTVNHMKDVLNEISSRMRTHSVPWHTAGRYWGHMNSETLMPSLLAYNFAMLWNGNNVAYESSPATSQMEEEVGHEFAHLMSYKNGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVKPELVAGKSDWELLNMPTKEIMDLLESAEDEIDEIKAHSARSGKHLQAIGKWLVPQTKHYSWLKAADIIGIGLDQVIPVPVDHNYRMDINELEKIVRGLAEEQIPVLGVVGVVGSTEEGAVDSIDKIIALRDELMKDGIYYYVHVDAAYGGYGRAIFLDEDNNFIPYEDLQDVHEEYGVFKEKKEHISREVYDAYKAIELAESVTIDPHKMGYIPYSAGGIVIQDIRMRDVISYFATYVFEKGADIPALLGAYILEGSKAGATAASVWAAHHVLPLNVAGYGKLIGASIEGSHHFYNFLNDLTFKVGDKEIEVHTLTHPDFNMVDYVFKEKGNDDLVAMNKLNHDVYDYASYVKGNIYNNEFITSHTDFAIPDYGNSPLKFVNSLGFSDEEWNRAGKVTVLRAAVMTPYMNDKEEFDVYAPKIQAALQEKLEQIYDVK DE3HL9N TD Primarily distributed in human gut. DE3HL9N FC This enzyme catalyzes the decarboxylation of L-tyrosine to produce tyramine. DE3HL9N KD 2: Bacteria DE3HL9N PL 1239: Firmicutes DE3HL9N CL 91061: Bacilli DE3HL9N OD 186826: Lactobacillales DE3HL9N FM 81852: Enterococcaceae DE3HL9N GE 1350: Enterococcus DE3HL9N SP 1351: Enterococcus faecalis DE4AMLP ID DE4AMLP DE4AMLP DN Nicotinate dehydrogenase (nicA) DE4AMLP GN nicA DE4AMLP SN Nicotinate degradation protein A; Nicotinate dehydrogenase small subunit; PP_3947; ndhS; nicA DE4AMLP UC NICA_PSEPK DE4AMLP RD Nicotine DE4AMLP GI 1046617 DE4AMLP E1 1: Oxidoreductase DE4AMLP E2 1.17: CH/CH2 oxidoreductase DE4AMLP E3 1.17.2: MCD acceptor oxidoreductase DE4AMLP EC 1.17.2.1 DE4AMLP KG Metabolic pathways:ppu01100; Microbial metabolism in diverse environments:ppu01120; Nicotinate and nicotinamide metabolism:ppu00760 DE4AMLP SQ MQTTISLQVNGQPVEVSAMPDTPLLLILRNDLCLNGPKYGCGLGECGACTVIIDGVAARSCVIPLAGAAGRNITTLEGLGSKAAPHPVQQAFIDEQAAQCGYCMNGMIMTAKALLDRIPEPSDEQIRNELSANLCRCGTHVEILRAVRRAAETRRKP DE4AMLP TD Primarily distributed in human gut. DE4AMLP FC This enzyme is subunit of the two-component enzyme NicAB that mediates nicotinate hydroxylation, the first step in the aerobic nicotinate degradation pathway. And it mediates conversion of nicotinate into 6-hydroxynicotinate (6HNA). DE4AMLP KD 2: Bacteria DE4AMLP PL 1224: Proteobacteria DE4AMLP CL 1236: Gammaproteobacteria DE4AMLP OD 72274: Pseudomonadales DE4AMLP FM 135621: Pseudomonadaceae DE4AMLP GE 286: Pseudomonas DE4AMLP SP 303: Pseudomonas putida DE4AMLP SU Pseudomonas putida S16 DEW0GI5 ID DEW0GI5 DEW0GI5 DN Folylpolyglutamate synthetase (fpgS) DEW0GI5 GN fpgS DEW0GI5 SN Bacterial folylpoly-gamma-glutamate synthetase; Bacterial tetrahydrofolylpolyglutamate synthase; Folylpolyglutamate synthase; Bacterial FPGS; fpgS DEW0GI5 UC FPGS_LACCA DEW0GI5 RD L-glutamine DEW0GI5 E1 6: Ligase DEW0GI5 E2 6.3: Carbon-nitrogen ligase DEW0GI5 E3 6.3.2: Peptide synthase DEW0GI5 EC 6.3.2.17 DEW0GI5 PD 1FGS; 1JBV; 1JBW; 2GC5; 2GC6; 2GCA; 2GCB DEW0GI5 SQ MNYTETVAYIHSFPRLAKTGDHRRILTLLHALGNPQQQGRYIHVTGTNGKGSAANAIAHVLEASGLTVGLYTSPFIMRFNERIMIDHEPIPDAALVNAVAFVRAALERLQQQQADFNVTEFEFITALGYWYFRQRQVDVAVIEVGIGGDTDSTNVITPVVSVLTEVALDHQKLLGHTITAIAKHKAGIIKRGIPVVTGNLVPDAAAVVAAKVATTGSQWLRFDRDFSVPKAKLHGWGQRFTYEDQDGRISDLEVPLVGDYQQRNMAIAIQTAKVYAKQTEWPLTPQNIRQGLAASHWPARLEKISDTPLIVIDGAHNPDGINGLITALKQLFSQPITVIAGILADKDYAAMADRLTAAFSTVYLVPVPGTPRALPEAGYEALHEGRLKDSWQEALAASLNDVPDQPIVITGSLYLASAVRQTLLGGKS DEW0GI5 TD Primarily distributed in human gut. DEW0GI5 FC This enzyme is involved in the conversion of folates to polyglutamate derivatives, and likely functions in the retention of cellular folate pools. It catalyzes successive MgATP-dependent additions of glutamate to a pteroylmonoglutamate substrate, with a high preference for 5,10-methylenetetrahydrofolate (mTHF). Thus, it metabolizes mTHF to the tetraglutamate derivative, but longer glutamate chain length products are not observed. DEW0GI5 KD 2: Bacteria DEW0GI5 PL 1239: Firmicutes DEW0GI5 CL 91061: Bacilli DEW0GI5 OD 186826: Lactobacillales DEW0GI5 FM 33958: Lactobacillaceae DEW0GI5 GE 1578: Lactobacillus DEW0GI5 SP 1582: Lactobacillus casei DEZ1H4L ID DEZ1H4L DEZ1H4L DN Cytochrome P450 MEG (cyp106) DEZ1H4L GN cyp106A2 DEZ1H4L SN Steroid 15-beta-hydroxylase; Steroid 15-beta-monooxygenase; Cytochrome P450(MEG); P450(MEG); cyp106A2 DEZ1H4L UC CPXM_BACME DEZ1H4L RD Progesterone DEZ1H4L E1 1: Oxidoreductase DEZ1H4L E2 1.14: Oxygen paired donor oxidoreductase DEZ1H4L E3 1.14.15: Iron-sulfur protein donor oxidoreductase DEZ1H4L EC 1.14.15.8 DEZ1H4L PD 4YT3; 5IKI; 5XNT DEZ1H4L SQ MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGQTLTSLPLKASRM DEZ1H4L TD Primarily distributed in human gut. DEZ1H4L FC This enzyme has the capacity to hydroxylate certain steroids in the 15-beta position, and it also hydroxylates progesterone in the 11-alpha and 9-beta position. DEZ1H4L KD 2: Bacteria DEZ1H4L PL 1239: Firmicutes DEZ1H4L CL 91061: Bacilli DEZ1H4L OD 1385: Bacillales DEZ1H4L FM 186817: Bacillaceae DEZ1H4L GE 1386: Bacillus DEZ1H4L SP 1404: Bacillus megaterium DEZ1H4L SU Bacillus megaterium ATCC 13368 DEOFMQ7 ID DEOFMQ7 DEOFMQ7 DN VanA ligase (vanA) DEOFMQ7 GN vanA DEOFMQ7 SN Vancomycin/teicoplanin A-type resistance protein VanA; D-alanylalanine synthetase VanA; D-alanine--D-alanine ligase VanA; D-Ala-D-Ala ligase VanA; vanA DEOFMQ7 UC Q0WYK7_ENTFL DEOFMQ7 RD Vancomycin DEOFMQ7 GI 13917379 DEOFMQ7 E1 6: Ligase DEOFMQ7 E2 6.3: Carbon-nitrogen ligase DEOFMQ7 E3 6.3.2: Peptide synthase DEOFMQ7 EC 6.3.2.4 DEOFMQ7 SQ MNRIKVAILFGGCSEEHDVSVKSAIEIAANINKEKYEPLYIGITKSGVWKMCEKPCAEWENDNCYSAVLSPDKKMHGLLVKKNHEYEINHVDVAFSALHGKSGEDGSIQGLFELSGIPFVGCDIQSSAICMDKSLTYIVAKNAGIATPAFWVINKDDRPVAATFTYPVFVKPARSGSSFGVKKVNSADELDYAIESARQYDSKILIEQAVSGCEVGCAVLGNSAALVVGEVDQIRLQYGIFRIHQEVEPEKGSENAVITVPADLSAEERGRIQETAKKIYKALGCRGLARVDMFLQDNGRIVLNEVNTLPGFTSYSRYPRMMAAAGIALPELIDRLIVLALKG DEOFMQ7 TD Primarily distributed in human gut. DEOFMQ7 FC This enzyme is involved with UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase (EC 6.3.2.7) or UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase (EC 6.3.2.13), UDP-N-acetylmuramate---L-alanine ligase (EC 6.3.2.8), UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase (EC 6.3.2.9) and UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase (EC 6.3.2.10) in the synthesis of a cell-wall peptide. DEOFMQ7 KD 2: Bacteria DEOFMQ7 PL 1239: Firmicutes DEOFMQ7 CL 91061: Bacilli DEOFMQ7 OD 186826: Lactobacillales DEOFMQ7 FM 81852: Enterococcaceae DEOFMQ7 GE 1350: Enterococcus DEOFMQ7 SP 1351: Enterococcus faecalis DEL8OCP ID DEL8OCP DEL8OCP DN Glutamate racemase (MurI) DEL8OCP GN murI DEL8OCP SN D-glutamate racemase; MurI; murI; BAS0806; BAS4379; BcGR; BsGR; BsRacE; DapF; FnGR; GBAA_0847; GBAA_4717 DEL8OCP UC MURI_LACFE DEL8OCP RD L-glutamine DEL8OCP GI 6233637 DEL8OCP E1 5: Isomerase DEL8OCP E2 5.1: Racemase/epimerase DEL8OCP E3 5.1.1: Amino acid racemase/epimerase DEL8OCP EC 5.1.1.3 DEL8OCP SQ MDNRPIGVMDSGLGGLSVVRVIQQKLPNEEVIFVGDQGHFPYGTKDQAEVRQLALSIGAFLLKHDVKMMVVACNTATAAALPALQAALPIPVIGVIEPGARAALAQDKKGPIGVIATTATTTAGAYPATIERLAPGTPVIAKATQPMVEIVEHGQTGTAKAQEVVSEQLMTFKEHPVKTLIMGCTHFPFLAPEISKAVGPTVALVDPAKETVATAKSWLEQHQAMGNHAHPNYHLYSTGNLPDLRAGVNKWLLSGHFDLGTAQIEEGD DEL8OCP TD Primarily distributed in human gut. DEL8OCP FC This enzyme is a pyridoxal-phosphate protein providing the (R)-glutamate required for cell wall biosynthesis and converting L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine. DEL8OCP KD 2: Bacteria DEL8OCP PL 1239: Firmicutes DEL8OCP CL 91061: Bacilli DEL8OCP OD 186826: Lactobacillales DEL8OCP FM 33958: Lactobacillaceae DEL8OCP GE 1578: Lactobacillus DEL8OCP SP 1613: Lactobacillus fermentum DEAQBHI ID DEAQBHI DEAQBHI DN Glutamate racemase (MurI) DEAQBHI GN racE1 DEAQBHI SN D-glutamate racemase; MurI; murI; BAS0806; BAS4379; BcGR; BsGR; BsRacE; DapF; FnGR; GBAA_0847; GBAA_4717 DEAQBHI UC Q81UL8_BACAN DEAQBHI RD L-glutamine DEAQBHI E1 5: Isomerase DEAQBHI E2 5.1: Racemase/epimerase DEAQBHI E3 5.1.1: Amino acid racemase/epimerase DEAQBHI EC 5.1.1.3 DEAQBHI KG D-Glutamine and D-glutamate metabolism:bar00471; Metabolic pathways:bar01100 DEAQBHI PD 2DWU DEAQBHI SQ MSVCHKHSVIGVLDSGVGGLTVASEIIRQLPKESICYIGDNERCPYGPRSVEEVQSFVFEMVEFLKQFPLKALVVACNTAAAATLAALQEALSIPVIGVIHPGARAAIKVTKKGKIGVIGTVGTIQSNMYEKALHELDTYLKVHSHACPTLATVVENRLEDTAYVTQQVKQALLPLTKEDIDTLILGCTHYPLLESYIKKELGEDVTIISSAEETAIELSTILQHKGILADNLNPKHRFFTTGSVSSFEHIAERWLGYQISVDCVDLPVKNARICN DEAQBHI TD Primarily distributed in human gut. DEAQBHI FC This enzyme is a pyridoxal-phosphate protein providing the (R)-glutamate required for cell wall biosynthesis and converting L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine. DEAQBHI KD 2: Bacteria DEAQBHI PL 1239: Firmicutes DEAQBHI CL 91061: Bacilli DEAQBHI OD 1385: Bacillales DEAQBHI FM 186817: Bacillaceae DEAQBHI GE 1386: Bacillus DEAQBHI SP 1392: Bacillus anthracis DEU824V ID DEU824V DEU824V DN Glutamate decarboxylase (gadB) DEU824V GN gadB DEU824V SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; GAD-beta DEU824V UC A9ZM78_LACBR DEU824V RD L-glutamine DEU824V E1 4: Lyases DEU824V E2 4.1: Carbon-carbon lyase DEU824V E3 4.1.1: Carboxy-lyase DEU824V EC 4.1.1.15 DEU824V SQ MMNKNDQETQQMINNVDLEKTFLGSVEAGQSLPTYTLPDDPMAPDVAAQLVEHYRLNEAKANQNLATFCTTQMEPQADELMKNALNTNAIDKSEYPKTAAMENYCVSMIAHLWGIPDNEKIYDDFIGTSTVGSSEGCMLGGLALLHSWKHRAKAAGFDIEDLHSHKPNLVIMSGYQVVWEKFCTYWNVEMRQVPINGDQVSLDMDHVMDYVDENTIGIIGIEGITYTGSVDDIQTLDNLVTEYNKTATMPVRIHVDAAFGGLFAPFVDGFNPWDFRLKNVVSINVSGHKYGMVYPGLGWIVWRHDTADILPAEMRFQVPYLGKTVDSIAINFSHSGAHISAQYYNFIRFGLSGYKTIMQNVRKVSLKLTAALKTYGIFDILVDGSQLPINCWKLADDAPVGWTLYDLESELAKYGWQVPAYPLPKNRDDVTISRIVVRPSMTMTIADDFLDDLKLAIDGLNHTFGVTTTVDQDNKTTVRS DEU824V TD Primarily distributed in human gut. DEU824V FC This enzyme acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DEU824V KD 2: Bacteria DEU824V PL 1239: Firmicutes DEU824V CL 91061: Bacilli DEU824V OD 186826: Lactobacillales DEU824V FM 33958: Lactobacillaceae DEU824V GE 1578: Lactobacillus DEU824V SP 33959: Lactobacillus johnsonii DEWJKC0 ID DEWJKC0 DEWJKC0 DN Glutamate decarboxylase (gadB) DEWJKC0 GN gadA DEWJKC0 SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; GAD-beta; S4173; SF3594 DEWJKC0 UC DCEA_SHIFL DEWJKC0 RD L-glutamine DEWJKC0 GI 1026324 DEWJKC0 E1 4: Lyases DEWJKC0 E2 4.1: Carbon-carbon lyase DEWJKC0 E3 4.1.1: Carboxy-lyase DEWJKC0 EC 4.1.1.15 DEWJKC0 KG Alanine, aspartate and glutamate metabolism:sfl00250; Biosynthesis of secondary metabolites:sfl01110; Butanoate metabolism:sfl00650; Metabolic pathways:sfl01100; Microbial metabolism in diverse environments:sfl01120; Quorum sensing:sfl02024; Taurine and hypotaurine metabolism:sfl00430; beta-Alanine metabolism:sfl00410 DEWJKC0 SQ MDQKLLTDFRSELLDSRFGAKAISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKQGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT DEWJKC0 TD Primarily distributed in human gut. DEWJKC0 FC This enzyme converts glutamate to gamma-aminobutyrate (GABA). The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DEWJKC0 KD 2: Bacteria DEWJKC0 PL 1224: Proteobacteria DEWJKC0 CL 1236: Gammaproteobacteria DEWJKC0 OD 91347: Enterobacterales DEWJKC0 FM 543: Enterobacteriaceae DEWJKC0 GE 620: Shigella DEWJKC0 SP 623: Shigella flexneri DEJ8T0P ID DEJ8T0P DEJ8T0P DN Glutamate decarboxylase (gadB) DEJ8T0P GN gadB DEJ8T0P SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; GAD-beta; L123581; LL1290 DEJ8T0P UC DCE_LACLA DEJ8T0P RD L-glutamine DEJ8T0P GI 1114939 DEJ8T0P E1 4: Lyases DEJ8T0P E2 4.1: Carbon-carbon lyase DEJ8T0P E3 4.1.1: Carboxy-lyase DEJ8T0P EC 4.1.1.15 DEJ8T0P KG Alanine, aspartate and glutamate metabolism:lla00250; Biosynthesis of secondary metabolites:lla01110; Butanoate metabolism:lla00650; Metabolic pathways:lla01100; Microbial metabolism in diverse environments:lla01120; Quorum sensing:lla02024; Taurine and hypotaurine metabolism:lla00430 DEJ8T0P SQ MLYGKENRDEAEFLEPIFGSESEQVDLPKYKLAQQSIEPRVAYQLVQDEMLDEGNARLNLATFCQTYMEPEAVKLMSQTLEKNAIDKSEYPRTTEIENRCVNMIADLWNASEKEKFMGTSTIGSSEACMLGGMAMKFSWRKRAEKLGLDINAKKPNLVISSGYQVCWEKFCIYWDIEMREVPMDKEHMSINLDKVMDYVDEYTIGVVGIMGITYTGRYDDIKALDNLIEEYNKQTDYKVYIHVDAASGGLYAPFVEPELEWDFRLKNVISINTSGHKYGLVYPGVGWVLWRDKKYLPEELIFKVSYLGGELPTMAINFSHSASQLIGQYYNFVRYGFDGYKAIHERTHKVAMFLAKEIEKTGMFEIMNDGSQLPIVCYKLKEDSNRGWNLYDLADRLLMKGWQVPAYPLPKNLENEIIQRLVIRADFGMNMAFNYVQDMQEAIEALNKAHILYHEEPENKTYGFTH DEJ8T0P TD Primarily distributed in human gut. DEJ8T0P FC This enzyme converts internalized glutamate to GABA. The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DEJ8T0P KD 2: Bacteria DEJ8T0P PL 1239: Firmicutes DEJ8T0P CL 91061: Bacilli DEJ8T0P OD 186826: Lactobacillales DEJ8T0P FM 1300: Streptococcaceae DEJ8T0P GE 1357: Lactococcus DEJ8T0P SP 1358: Lactococcus lactis DEBIUVA ID DEBIUVA DEBIUVA DN Glutamate decarboxylase (gadB) DEBIUVA GN gadB DEBIUVA SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; AMBR_LLDLPDMO_02674; GAD-beta; LPJSA22_03059 DEBIUVA UC A0A1E3KVW8_LACPN DEBIUVA RD L-glutamine DEBIUVA E1 4: Lyases DEBIUVA E2 4.1: Carbon-carbon lyase DEBIUVA E3 4.1.1: Carboxy-lyase DEBIUVA EC 4.1.1.15 DEBIUVA SQ MAMLYGKHNHEAEEYLEPVFGAPSEQHDLPKYRLPKHSLSPREADRLVRDELLDEGNSRLNLATFCQTYMEPEAVELMKDTLAKNAIDKSEYPRTAEIENRCVNIIANLWHAPDDEHFTGTSTIGSSEACMLGGLAMKFAWRKRAQAAGLDLNAHRPNLVISAGYQVCWEKFCVYWDVDMHVVPMDEQHMALDVNHVLDYVDEYTIGIVGIMGITYTGQYDDLAALDKVVTHYNHQHPKLPVYIHVDAASGGFYTPFIEPQLIWDFRLANVVSINASGHKYGLVYPGVGWVVWRDRQFLPPELVFKVSYLGGELPTMAINFSHSAAQLIGQYYNFIRFGMDGYREIQTKTHDVARYLAAALDKVGEFKMVNNGHQLPLICYQLAPREDREWTLYDLSDRLLMNGWQVPTYPLPANLEQQVIQRIVVRADFGMNMAHDFMDDLTKAVHDLNHAHIVYHHDAAPKKYGFTH DEBIUVA TD Primarily distributed in human gut. DEBIUVA FC This enzyme acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DEBIUVA KD 2: Bacteria DEBIUVA PL 1239: Firmicutes DEBIUVA CL 91061: Bacilli DEBIUVA OD 186826: Lactobacillales DEBIUVA FM 33958: Lactobacillaceae DEBIUVA GE 1578: Lactobacillus DEBIUVA SP 1590: Lactobacillus plantarum DEC984D ID DEC984D DEC984D DN Glutamate decarboxylase (gadB) DEC984D GN gadB DEC984D SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; ERS852382_01825; GAD-beta DEC984D UC A0A174BCD4_BIFAD DEC984D RD L-glutamine DEC984D E1 4: Lyases DEC984D E2 4.1: Carbon-carbon lyase DEC984D E3 4.1.1: Carboxy-lyase DEC984D EC 4.1.1.15 DEC984D SQ MSETHSTTENNNSHCCDNTCGNADDRVVPDSVEINPLFARPKEAQAFSKFTIPQKGSLPETAYQVVHDEAMLDGNARLNLATFVSTWMDDHANRLYMEAADKNMIDKDEYPKTAEVESRCWHMLADLWHAPDPMNAIGTSTIGSSEACMLGGLALKRRWKEAREKADLPTDRPNLVMSSAVQVCWEKFCNYFDVEPRYVPISEDHKVLDGHDLDKYVDENTIGVVAIMGVTYTGMYEPVEQISEALDRIEERTGLDVRIHVDGASGGMIAPFIQPDLAWDFRVKRVYSISTSGHKYGLVYPGLGWIVWRETADLPESLIFKVSYLGGEMPTFALNFSRPGAQVLLQYYMFLRLGFDGYRRVQQTSHDMAKYLSGEIEQMDDFTLWNDGSDIPVFAWMLNDKPDRKWNLYDLQDRLRMKGWLVPAYPMPVDLTQVTVQRIVVRNGFSHDMAEAFIKDLKSCVKYLDGLRSPMPSEARASEFHH DEC984D TD Primarily distributed in human gut. DEC984D FC This enzyme acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DEC984D KD 2: Bacteria DEC984D PL 201174: Actinobacteria DEC984D CL 1760: Actinobacteria DEC984D OD 85004: Bifidobacteriales DEC984D FM 31953: Bifidobacteriaceae DEC984D GE 1678: Bifidobacterium DEC984D SP 1680: Bifidobacterium adolescentis DEPUK4S ID DEPUK4S DEPUK4S DN Cytochrome P450 142A2 (cyp142) DEPUK4S GN cyp142 DEPUK4S SN Cytochrome P450 family 142 subfamily A member 2; Cholest-4-en-3-one C26-monooxygenase 142A2; Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] 142A2; Cholesterol C26-monooxygenase 142A2; Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming] 142A2; MSMEG_5918; Steroid C26-monooxygenase 142A2; Steroid C27-monooxygenase 142A2; cyp142A2 DEPUK4S UC CP142_MYCS2 DEPUK4S RD ANW-32821 DEPUK4S GI 4533135 DEPUK4S E1 1: Oxidoreductase DEPUK4S E2 1.14: Oxygen paired donor oxidoreductase DEPUK4S E3 1.14.15: Iron-sulfur protein donor oxidoreductase DEPUK4S EC 1.14.15.28 DEPUK4S KG Microbial metabolism in diverse environments:msb01120; Steroid degradation:msb00984 DEPUK4S PD 2YOO; 3ZBY; 4TRI; 4UAX DEPUK4S SQ MTQMLTRPDVDLVNGMFYADGGAREAYRWMRANEPVFRDRNGLAAATTYQAVLDAERNPELFSSTGGIRPDQPGMPYMIDMDDPQHLLRRKLVNAGFTRKRVMDKVDSIGRLCDTLIDAVCERGECDFVRDIAAPLPMAVIGDMLGVLPTERDMLLKWSDDLVCGLSSHVDEAAIQKLMDTFAAYTEFTKDVITKRRAEPTDDLFSVLVNSEVEGQRMSDDEIVFETLLILIGGDETTRHTLSGGTEQLLRHRDQWDALVADVDLLPGAIEEMLRWTSPVKNMCRTLTADTVFHGTELRAGEKIMLMFESANFDESVFGDPDNFRIDRNPNSHVAFGFGTHFCLGNQLARLELRLMTERVLRRLPDLRLADDAPVPLRPANFVSGPESMPVVFTPSAPVLA DEPUK4S TD Primarily distributed in human lung. DEPUK4S FC This enzyme is a P-450 heme-thiolate protein, and it is involved in the utilization of cholesterol as the sole carbon and energy source by degrading the side chain. Primarily catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. Also able to sequentially oxidize cholesterol itself, not only cholest-4-en-3-one. DEPUK4S KD 2: Bacteria DEPUK4S PL 201174: Actinobacteria DEPUK4S CL 1760: Actinobacteria DEPUK4S OD 85007: Corynebacteriales DEPUK4S FM 1762: Mycobacteriaceae DEPUK4S GE 1866885: Mycolicibacterium DEPUK4S SP 1772: Mycolicibacterium smegmatis DE6ZDK4 ID DE6ZDK4 DE6ZDK4 DN Cytochrome P450 125A3 (cyp125) DE6ZDK4 GN cyp125 DE6ZDK4 SN Cytochrome P450 family 125 subfamily A member 3; Cholest-4-en-3-one 26-monooxygenase 125A3; Cholest-4-en-3-one C26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] 125A3; Cholesterol C26-monooxygenase 125A3; Cholesterol C26-monooxygenase [(25S)-3beta-hydroxycholest-5-en-26-oate forming] 125A3; MSMEG_5995; Steroid C26-monooxygenase 125A3; Steroid C27-monooxygenase 125A3; cyp125A3 DE6ZDK4 UC CP125_MYCS2 DE6ZDK4 RD ANW-32821 DE6ZDK4 GI 4531666 DE6ZDK4 E1 1: Oxidoreductase DE6ZDK4 E2 1.14: Oxygen paired donor oxidoreductase DE6ZDK4 E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE6ZDK4 EC 1.14.15.29 DE6ZDK4 KG Microbial metabolism in diverse environments:msg01120; Steroid degradation:msg00984 DE6ZDK4 PD 4APY; 5DQN DE6ZDK4 SQ MPTPNIPSDFDFLDATLNLERLPVEELAELRKSEPIHWVDVPGGTGGFGDKGYWLVTKHADVKEVSRRSDVFGSSPDGAIPVWPQDMTREAVDLQRAVLLNMDAPQHTRLRKIISRGFTPRAIGRLEDELRSRAQKIAQTAAAQGAGDFVEQVSCELPLQAIAELLGVPQDDRDKLFRWSNEMTAGEDPEYADVDPAMSSFELISYAMKMAEERAVNPTEDIVTKLIEADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITHGMIAFAQNPDQWELYKKERPETAADEIVRWATPVSAFQRTALEDVELGGVQIKKGQRVVMSYRSANFDEEVFEDPHTFNILRSPNPHVGFGGTGAHYCIGANLARMTINLIFNAIADNMPDLKPIGAPERLKSGWLNGIKHWQVDYTGAGKASVSGAPGTCPVAH DE6ZDK4 TD Primarily distributed in human lung. DE6ZDK4 FC This enzyme is a P-450 heme-thiolate protein found in several bacterial pathogens, and it is involved in degradation of the host's cholesterol. The enzyme catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol . The products are exclusively in the (25S) configuration. And it also accepts cholesterol as a substrate. DE6ZDK4 KD 2: Bacteria DE6ZDK4 PL 201174: Actinobacteria DE6ZDK4 CL 1760: Actinobacteria DE6ZDK4 OD 85007: Corynebacteriales DE6ZDK4 FM 1762: Mycobacteriaceae DE6ZDK4 GE 1866885: Mycolicibacterium DE6ZDK4 SP 1772: Mycolicibacterium smegmatis DEKGVS4 ID DEKGVS4 DEKGVS4 DN Beta-lactamase (blaB) DEKGVS4 GN penA DEKGVS4 SN Penicillinase; Cephalosporinase; Beta-lactam; Beta-lactamase TEM; IRT-4; TEM-1 DEKGVS4 UC PENA_BURM1 DEKGVS4 RD Cefotaxime DEKGVS4 E1 3: Hydrolases DEKGVS4 E2 3.5: Carbon-nitrogen hydrolase DEKGVS4 E3 3.5.2: Cyclic amide hydrolase DEKGVS4 EC 3.5.2.6 DEKGVS4 SQ MQRIGVTDYTILGTVKGAELELVRFTHPFMGFDVPAILGDHVTRMPVPVPFTPRLPRPGRLCDRSEIRPGKPLTRLARTALICRALIRRWMARTSYSDSVNCHTQPISAIFDYKDLRFEPPSNRISPAGQTSVDRLLQLSQGQAVEGQSAVARLTGEKKNHPGAQYANRLSPRIANNHPATQQTLFELGSGAKERNAINVSYLTALGTPGFTLMLPARMLCGIVSDNNFTQKQLCPSPARCTRGPAEPAKRGPWLEPGLVIRKDGLRTGKLLSSLRGLCLTVLRFQPTVPCFCRLALSSSVAISSTGLVNFSR DEKGVS4 TD Primarily distributed in human lung. DEKGVS4 FC This enzyme hydrolyzes beta-lactam with a substrate specificity for penicillin. DEKGVS4 KD 2: Bacteria DEKGVS4 PL 1224: Proteobacteria DEKGVS4 CL 28216: Betaproteobacteria DEKGVS4 OD 80840: Burkholderiales DEKGVS4 FM 119060: Burkholderiaceae DEKGVS4 GE 32008: Burkholderia DEKGVS4 SP 87883: Burkholderia multivorans DEEISQ2 ID DEEISQ2 DEEISQ2 DN Azoreductase (azoR) DEEISQ2 GN azoR DEEISQ2 SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; EF_2601; azoA DEEISQ2 UC AZOR_ENTFA DEEISQ2 RD Sulfasalazine DEEISQ2 GI 1201460 DEEISQ2 E1 1: Oxidoreductase DEEISQ2 E2 1.7: Cytochrome acceptor oxidoreductase DEEISQ2 E3 1.7.1: NAD/NADP acceptor oxidoreductase DEEISQ2 EC 1.7.1.6 DEEISQ2 PD 2HPV DEEISQ2 SQ MSKLLVVKAHPLTKEESRSVRALETFLASYRETNPSDEIEILDVYAPETNMPEIDEELLSAWGALRAGAAFETLSENQQQKVARFNELTDQFLSADKVVIANPMWNLNVPTRLKAWVDTINVAGKTFQYTAEGPKPLTSGKKALHIQSNGGFYEGKDFASQYIKAILNFIGVDQVDGLFIEGIDHFPDRAEELLNTAMTKATEYGKTF DEEISQ2 TD Primarily distributed in human gut. DEEISQ2 FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. And it requires NADH, but not NADPH, as an electron donor for its activity. And it can also reduce a wide range of sulfonated azo dyes. The substrate preference order is methyl Red > Orange II > Ponceau BS > Ponceau S > Orange G > Amaranth. DEEISQ2 KD 2: Bacteria DEEISQ2 PL 1239: Firmicutes DEEISQ2 CL 91061: Bacilli DEEISQ2 OD 186826: Lactobacillales DEEISQ2 FM 81852: Enterococcaceae DEEISQ2 GE 1350: Enterococcus DEEISQ2 SP 1351: Enterococcus faecalis DEBY951 ID DEBY951 DEBY951 DN Cytochrome P450 21A2 (cyp21) DEBY951 GN cyp158a2_1 DEBY951 SN Cytochrome P450 family 21 subfamily A member 2; Cytochrome cyp21A2; P450 21A2; cyp21A2 DEBY951 UC A0A250VKS1_STROL DEBY951 RD Progesterone DEBY951 GI 34823218 DEBY951 E1 1: Oxidoreductase DEBY951 E2 1.14: Oxygen paired donor oxidoreductase DEBY951 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEBY951 EC 1.14.14.16 DEBY951 SQ MTEKTMPGPLPPVRHWPALDLKGVDFDPVLSELMREGPVTRIQLPNGEGWAWLVTRHDDVRMVANDPRFGREAVVDQPVTRLAPHFIPARGAVGFLDPPDHTRLRRSVAAAFTARGVERVRDKARRTLDVMVDELLRIGPPADLTEAVLSPFPIAVICELMGVPADDRRGMHTWTQLILSSAHGAEVSEKAKDEMGAYFRKLIGARNDSRDEDVTSLLGAAVGRDEIDLEEAVGLAVLLQIGGEAVTNNSGQMFYLLLTRPALADRLRSDPRIRPQAIDELLRYIPHRNMVGLSRIAREDVEIRGVQIRAGDPIYVSYLAANRDPEVFPDPEHIDFGRSPNPHVAFGFGPHYCPGGMLARLESELLVEALVDRLPGLRLAVPPSQVPFRKGALIRGPEALPVTW DEBY951 TD Primarily distributed in human gut. DEBY951 FC This enzyme is a P-450 heme-thiolate protein and it responsible for the conversion of progesterone and 17alpha-hydroxyprogesterone to their respective 21-hydroxylated derivatives, 11-deoxycorticosterone and 11-deoxycortisol. Involved in the biosynthesis of the hormones aldosterone and cortisol. The electron donor is NADPH---hemoprotein reductase. DEBY951 KD 2: Bacteria DEBY951 PL 1239: Firmicutes DEBY951 CL 91061: Bacilli DEBY951 OD 1385: Bacillales DEBY951 FM 186817: Bacillaceae DEBY951 GE 1386: Bacillus DEBY951 SP 1404: Bacillus megaterium DEUW4J0 ID DEUW4J0 DEUW4J0 DN Nitroreductase (NTR) DEUW4J0 GN nfrA2 DEUW4J0 SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; NCTC12360_02994 DEUW4J0 UC A0A376H6M5_ENTGA DEUW4J0 RD Nitrofurantoin DEUW4J0 E1 1: Oxidoreductase DEUW4J0 E2 1.5: CH-NH donor oxidoreductase DEUW4J0 E3 1.5.1: NAD/NADP acceptor oxidoreductase DEUW4J0 EC 1.5.1.39 DEUW4J0 SQ MNETIDLLTNHRTYRQFDSNYQLSKEQLEAILSAARQAPSWMNGQAYSILVIDDRSLRQQLVTWNPGNPHIAESSIFLLFLADLNRTKKVAEKKQTPYLVDEGLQPLLIATTDASIALQSAAIAAESLGLGTVISGSVRKDSKAIAELLELPEYVYPVAGLSIGKPIVDMALKPRLPQEAVIHYNKYQDYSYQAIEDYDQIMTAFGEARETMPWSEKFANFWLYNLWD DEUW4J0 TD Primarily distributed in human gut. DEUW4J0 FC This enzyme contains FMN and can utilize NADH and NADPH with similar reaction rates. It also reduces riboflavin and FAD, but more slowly. DEUW4J0 KD 2: Bacteria DEUW4J0 PL 1239: Firmicutes DEUW4J0 CL 91061: Bacilli DEUW4J0 OD 186826: Lactobacillales DEUW4J0 FM 81852: Enterococcaceae DEUW4J0 GE 1350: Enterococcus DEUW4J0 SP 1353: Enterococcus gallinarum DE6CQ0I ID DE6CQ0I DE6CQ0I DN Cytochrome P450 130A1 (cyp130) DE6CQ0I GN cyp130 DE6CQ0I SN Cytochrome P450 family 130 subfamily A member 1; P450 130A1; MTCY50.26; P450 130A1; Rv1256c; cyp130A1 DE6CQ0I UC CP130_MYCTU DE6CQ0I RD Dextromethorphan hydrobromide DE6CQ0I E1 1: Oxidoreductase DE6CQ0I E2 1.14: Oxygen paired donor oxidoreductase DE6CQ0I E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE6CQ0I EC 1.14.15.29 DE6CQ0I PD 2UUQ; 2UVN; 2WGY; 2WH8; 2WHF DE6CQ0I SQ MTSVMSHEFQLATAETWPNPWPMYRALRDHDPVHHVVPPQRPEYDYYVLSRHADVWSAARDHQTFSSAQGLTVNYGELEMIGLHDTPPMVMQDPPVHTEFRKLVSRGFTPRQVETVEPTVRKFVVERLEKLRANGGGDIVTELFKPLPSMVVAHYLGVPEEDWTQFDGWTQAIVAANAVDGATTGALDAVGSMMAYFTGLIERRRTEPADDAISHLVAAGVGADGDTAGTLSILAFTFTMVTGGNDTVTGMLGGSMPLLHRRPDQRRLLLDDPEGIPDAVEELLRLTSPVQGLARTTTRDVTIGDTTIPAGRRVLLLYGSANRDERQYGPDAAELDVTRCPRNILTFSHGAHHCLGAAAARMQCRVALTELLARCPDFEVAESRIVWSGGSYVRRPLSVPFRVTS DE6CQ0I TD Primarily distributed in human gut. DE6CQ0I FC This enzyme catalyzes the N-demethylation of dextromethorphan yielding 3-methoxymorphinan. DE6CQ0I KD 2: Bacteria DE6CQ0I PL 201174: Actinobacteria DE6CQ0I CL 1760: Actinobacteria DE6CQ0I OD 85007: Corynebacteriales DE6CQ0I FM 1762: Mycobacteriaceae DE6CQ0I GE 1763: Mycobacterium DE6CQ0I SP 1773: Mycobacterium tuberculosis DEP7ECA ID DEP7ECA DEP7ECA DN Nitroreductase (NTR) DEP7ECA GN NTR DEP7ECA SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; AC1_0194 DEP7ECA UC B1R7B9_CLOPF DEP7ECA RD Metronidazole DEP7ECA GI 29572702 DEP7ECA E1 1: Oxidoreductase DEP7ECA E2 1.5: CH-NH donor oxidoreductase DEP7ECA E3 1.5.1: NAD/NADP acceptor oxidoreductase DEP7ECA EC 1.5.1.39 DEP7ECA SQ MKLDRKDIIDIFNFRFATKEFTGEIIPKEDMEMIAETARLSPSSFGLEPWKFLIVENKELIKEISEVSWGFQRQASTTSHIVIALTKAGSEVKYDSDYIRNLWINTKGVSEEFFEGIKDVLKNFQVGKLEADETNEKLLEWSKRQTYIALGNMMTAAAMREIDSCAIEGFDKEKVEEILAKKGILDKEKYELTYLIAFGYRKEDPNRKKSRLPKSEVIQWVE DEP7ECA TD Primarily distributed in human gut. DEP7ECA FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DEP7ECA KD 2: Bacteria DEP7ECA PL 1239: Firmicutes DEP7ECA CL 186801: Clostridia DEP7ECA OD 186802: Clostridiales DEP7ECA FM 31979: Clostridiaceae DEP7ECA GE 1485: Clostridium DEP7ECA SP 1502: Clostridium perfringens DEP7ECA SU Clostridium perfringens B str. ATCC 3626 DERGIEC ID DERGIEC DERGIEC DN Dihydrofolate reductase (folA) DERGIEC GN folA DERGIEC SN DHF reductase; 5,6,7,8-tetrahydrofolate: NADP+ oxidoreductase; Bifunctional TS-DHFR; BmDHFR; Bacterial DFR-TS; Bacterial DHFR; TC_0902; folA DERGIEC UC DYR_ECOLI DERGIEC RD Folic acid DERGIEC GI 944790 DERGIEC E1 1: Oxidoreductase DERGIEC E2 1.5: CH-NH donor oxidoreductase DERGIEC E3 1.5.1: NAD/NADP acceptor oxidoreductase DERGIEC EC 1.5.1.3 DERGIEC KG Folate biosynthesis:ecj00790; Metabolic pathways:ecj01100; One carbon pool by folate:ecj00670 DERGIEC PD 1DDR; 1DDS; 1DHI; 1DHJ; 1DRA; 1DRB; 1DRE; 1DRH; 1DYH; 1DYI; 1DYJ; 1JOL; 1JOM; 1RA1; 1RA2; 1RA3; 1RA8; 1RA9; 1RB2; 1RB3; 1RC4; 1RD7; 1RE7; 1RF7; 1RG7; 1RH3; 1RX1; 1RX2; 1RX3; 1RX4; 1RX5; 1RX6; 1RX7; 1RX8; 1RX9; 1TDR; 2ANO; 2ANQ; 2D0K; 2DRC; 2INQ; 3DAU; 3DRC; 3K74; 3KFY; 3OCH; 3QL3; 3QYL; 3QYO; 3R33; 4DFR; 4EIG; 4EIZ; 4EJ1; 4FHB; 4GH8; 4I13; 4I1N; 4KJJ; 4KJK; 4KJL; 4NX6; 4NX7; 4PDJ; 4X5F; 4X5G; 4X5H; 4X5I; 4X5J; 5CC9; 5CCC; 5DFR; 5E8Q; 5EAJ; 5UIH; 5UII; 5UIO; 5UIP; 5UJX; 5W3Q; 5Z6F; 5Z6J; 5Z6K; 5Z6L; 5Z6M; 6CQA; 6DFR; 6MR9; 6MT8; 6MTH; 7DFR DERGIEC SQ MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR DERGIEC TD Primarily distributed in human gut. DERGIEC FC This enzyme is key enzyme in folate metabolism and can catalyze an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. And it also slowly reduces folate to 5,6,7,8-tetrahydrofolate. DERGIEC KD 2: Bacteria DERGIEC PL 1224: Proteobacteria DERGIEC CL 1236: Gammaproteobacteria DERGIEC OD 91347: Enterobacterales DERGIEC FM 543: Enterobacteriaceae DERGIEC GE 561: Escherichia DERGIEC SP 562: Escherichia coli DERGIEC SU Escherichia coli K-12 DEEBFXM ID DEEBFXM DEEBFXM DN Dihydrofolate reductase (folA) DEEBFXM GN folA DEEBFXM SN DHF reductase; 5,6,7,8-tetrahydrofolate: NADP+ oxidoreductase; Bifunctional TS-DHFR; BmDHFR; Bacterial DFR-TS; Bacterial DHFR; TC_0902; folA DEEBFXM UC DYR_LACCA DEEBFXM RD Folic acid DEEBFXM E1 1: Oxidoreductase DEEBFXM E2 1.5: CH-NH donor oxidoreductase DEEBFXM E3 1.5.1: NAD/NADP acceptor oxidoreductase DEEBFXM EC 1.5.1.3 DEEBFXM PD 1AO8; 1BZF; 1DIS; 1DIU; 1LUD; 2HM9; 2HQP; 2L28; 2LF1; 3DFR DEEBFXM SQ MTAFLWAQDRDGLIGKDGHLPWHLPDDLHYFRAQTVGKIMVVGRRTYESFPKRPLPERTNVVLTHQEDYQAQGAVVVHDVAAVFAYAKQHPDQELVIAGGAQIFTAFKDDVDTLLVTRLAGSFEGDTKMIPLNWDDFTKVSSRTVEDTNPALTHTYEVWQKKA DEEBFXM TD Primarily distributed in human gut. DEEBFXM FC This enzyme is key enzyme in folate metabolism and can catalyze an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. And it also slowly reduces folate to 5,6,7,8-tetrahydrofolate. DEEBFXM KD 2: Bacteria DEEBFXM PL 1239: Firmicutes DEEBFXM CL 91061: Bacilli DEEBFXM OD 186826: Lactobacillales DEEBFXM FM 33958: Lactobacillaceae DEEBFXM GE 1578: Lactobacillus DEEBFXM SP 1582: Lactobacillus casei DE7IQ34 ID DE7IQ34 DE7IQ34 DN Beta-glucuronidase (uidA) DE7IQ34 GN uidA DE7IQ34 SN Beta-galactosidase/beta-glucuronidase; Beta-galactosidase BgaB; BGK71_00200; CCE29_06935; FEZ43_12625; NCTC13710_00049; PY91_01090; uidA DE7IQ34 UC A0A2A5L2J1_LACRH DE7IQ34 RD Erythromycin stearate DE7IQ34 GI 8420464 DE7IQ34 E1 3: Hydrolases DE7IQ34 E2 3.2: Glycosylase DE7IQ34 E3 3.2.1: O/S-glycosyl compound glycosidase DE7IQ34 EC 3.2.1.31 DE7IQ34 PD 6ECA DE7IQ34 SQ METSLLYPVTNDQRTDQKLDGLWQFKFDEAGEGEKSGWETGFHDGVSMPVPASFNDFFTDKASREYTGDFWYSRNFFVPSAAKGKALFLRFDAVTHRATIFVNGKEIRTHEGGFLPFAADISEAVKYGAENTVVVKGNNELSREALPAGDTITLRNGKKMVRPFFDFYNYSGLNRSVHLLSLPQERVLDYTTTFALAGNDATVNYTVETNGDAPVTVSLADADGQVVATAQGKQGALQVQNAHLWQVRNAYLYTLTIQLGDDTQTPLDTYTDRIGIRTIKISGTDILVNDKPIYLKGFGRHEDSPFAGRAFDLNVEKKDFALMKWIGANSFRTSHYPYDEQVYKIADEEGFLLTDEVPAVGFKMAAAAFLGGLNQSFFKGPWLKKLHERHIDQIRDLIKRDKNHPSVLAWSLFNEPDTIDENAVPYFKQIFDESKDLDPQGRPRTFTLSEDDTIETSKVLDFPDFYMLNRYPGWYHFGGYQISDGEAGLRDEMDKWQKAGVKKPVVFTEFGADTEAGLHKLPSVMWTEEYQVEVLKMFSRVFDDYDFIKGEQVWNLADFQTVEGNMRVNGNKKGIFTRDRQPKAAAFFYHDRWNKLPLDYKAK DE7IQ34 TD Primarily distributed in human gut. DE7IQ34 FC This enzyme takes part in glucuronoside catabolic process. It catalyzes the hydrolysis of beta-glucuronide containing substrates. DE7IQ34 KD 2: Bacteria DE7IQ34 PL 1239: Firmicutes DE7IQ34 CL 91061: Bacilli DE7IQ34 OD 186826: Lactobacillales DE7IQ34 FM 33958: Lactobacillaceae DE7IQ34 GE 1578: Lactobacillus DE7IQ34 SP 1599: Lactobacillus sakei DEAN5EW ID DEAN5EW DEAN5EW DN Nitroreductase (NTR) DEAN5EW GN nfsB DEAN5EW SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; nfsB; nfsI DEAN5EW UC NFSB_ENTCL DEAN5EW RD Metronidazole DEAN5EW E1 1: Oxidoreductase DEAN5EW E2 1.5: CH-NH donor oxidoreductase DEAN5EW E3 1.5.1: NAD/NADP acceptor oxidoreductase DEAN5EW EC 1.5.1.39 DEAN5EW PD 1KQB; 1KQC; 1KQD; 1NEC; 5J8D; 5J8G DEAN5EW SQ MDIISVALKRHSTKAFDASKKLTAEEAEKIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGTYVFNERKMLDASHVVVFCAKTAMDDAWLERVVDQEEADGRFNTPEAKAANHKGRTYFADMHRVDLKDDDQWMAKQVYLNVGNFLLGVGAMGLDAVPIEGFDAAILDEEFGLKEKGFTSLVVVPVGHHSVEDFNATLPKSRLPLSTIVTEC DEAN5EW TD Primarily distributed in human gut. DEAN5EW FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DEAN5EW KD 2: Bacteria DEAN5EW PL 1224: Proteobacteria DEAN5EW CL 1236: Gammaproteobacteria DEAN5EW OD 91347: Enterobacterales DEAN5EW FM 543: Enterobacteriaceae DEAN5EW GE 547: Enterobacter DEAN5EW SP 550: Enterobacter cloacae DERZKBP ID DERZKBP DERZKBP DN Hydroxybenzoate 3-monooxygenase (pobA) DERZKBP GN pobA DERZKBP SN Hydroxybenzoate hydroxylase; 4-hydroxybenzoate 3-monooxygenase; p-hydroxybenzoate hydroxylase; PHBH; PP_3537 DERZKBP UC Q88H28_PSEPK DERZKBP RD Tetracycline DERZKBP GI 1045564 DERZKBP E1 1: Oxidoreductase DERZKBP E2 1.14: Oxygen paired donor oxidoreductase DERZKBP E3 1.14.13: NADH/NADPH donor oxidoreductase DERZKBP EC 1.14.13.2 DERZKBP KG Benzoate degradation:ppu00362; Degradation of aromatic compounds:ppu01220; Metabolic pathways:ppu01100; Microbial metabolism in diverse environments:ppu01120 DERZKBP PD 6DLL DERZKBP SQ MKTQVAIIGAGPSGLLLGQLLHKAGIDNIIVERQTAEYVLGRIRAGVLEQGTVDLLREAGVAERMDREGLVHEGVELLVGGRRQRLDLKALTGGKTVMVYGQTEVTRDLMQAREASGAPIIYSAANVQPHELKGEKPYLTFEKDGRVQRIDCDYIAGCDGFHGISRQSIPEGVLKQYERVYPFGWLGLLSDTPPVNHELIYAHHERGFALCSQRSQTRSRYYLQVPLQDRVEEWSDERFWDELKARLPAEVAADLVTGPALEKSIAPLRSLVVEPMQYGHLFLVGDAAHIVPPTGAKGLNLAASDVNYLYRILVKVYHEGRVDLLAQYSPLALRRVWKGERFSWFMTQLLHDFGSHKDAWDQKMQEADREYFLTSPAGLVNIAENYVGLPFEEVA DERZKBP TD Primarily distributed in human gut. DERZKBP FC This enzyme is a flavoprotein (FAD) and can catalyzes the incorporation of an atom of dioxygen into p-hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). DERZKBP KD 2: Bacteria DERZKBP PL 1224: Proteobacteria DERZKBP CL 1236: Gammaproteobacteria DERZKBP OD 72274: Pseudomonadales DERZKBP FM 135621: Pseudomonadaceae DERZKBP GE 286: Pseudomonas DERZKBP SP 303: Pseudomonas putida DE7IH52 ID DE7IH52 DE7IH52 DN Beta-lactamase (blaB) DE7IH52 GN ampC DE7IH52 SN Penicillinase; Cephalosporinase; Beta-lactam; blaC DE7IH52 UC AMPC_CITFR DE7IH52 RD Avibactam DE7IH52 E1 3: Hydrolases DE7IH52 E2 3.5: Carbon-nitrogen hydrolase DE7IH52 E3 3.5.2: Cyclic amide hydrolase DE7IH52 EC 3.5.2.6 DE7IH52 PD 1RGY DE7IH52 SQ MMKKSICCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAIIYEGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDRIARGEIKLSDPVTKYWPELTGKQWRGISLLHLATYTAGGLPLQIPGDVTDKAELLRFYQNWQPQWTPGAKRLYANSSIGLFGALAVKSSGMSYEEAMTRRVLQPLKLAHTWITVPQSEQKNYAWGYLEGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIELAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPARVEAAWRILEKLQ DE7IH52 TD Primarily distributed in human gut. DE7IH52 FC This enzyme hydrolyzes beta-lactam with a substrate specificity for cephalosporins. DE7IH52 KD 2: Bacteria DE7IH52 PL 1224: Proteobacteria DE7IH52 CL 1236: Gammaproteobacteria DE7IH52 OD 91347: Enterobacterales DE7IH52 FM 543: Enterobacteriaceae DE7IH52 GE 544: Citrobacter DE7IH52 SP 546: Citrobacter freundii DE7IH52 SU Citrobacter freundii ATCC 6879 DEPI0ME ID DEPI0ME DEPI0ME DN Arylamine N-acetyltransferase (NAT) DEPI0ME GN NAT DEPI0ME SN N-hydroxyarylamine O-acetyltransferase; nhoA; BED45_23050; LR61_11020 DEPI0ME UC A0A0A2RAD0_MORMO DEPI0ME RD Asacolitin DEPI0ME E1 2: Transferase DEPI0ME E2 2.3: Acyltransferase DEPI0ME E3 2.3.1: Acyltransferase DEPI0ME EC 2.3.1.5 DEPI0ME SQ MKDISFYLTRLNIKENIKIDNYFLFRFHHAHFYSVPFENFSMKENASSCSLSQIIANKIIFNKRGGICFEFAKLLESFFSYTGFVYRTRLARVLIPLMTPATHQLFIISVKGEEWIFDVGFGARGPRAPLRMVDGYVHEHAFLSSKVSRHPAYGWVVSVKENSRLNADWEDIYAFHDTETFLPDISMAYFYTLHSPESLLNTHKVASLPTENGRISIRNNVFTEVNGLSSCSADITDNEELSQLLSGKFGISIHPQQLQ DEPI0ME TD Primarily distributed in human gut. DEPI0ME FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DEPI0ME KD 2: Bacteria DEPI0ME PL 1224: Proteobacteria DEPI0ME CL 1236: Gammaproteobacteria DEPI0ME OD 91347: Enterobacterales DEPI0ME FM 1903414: Morganellaceae DEPI0ME GE 581: Morganella DEPI0ME SP 582: Morganella morganii DE5DY7B ID DE5DY7B DE5DY7B DN Arylamine N-acetyltransferase (NAT) DE5DY7B GN nhoA DE5DY7B SN N-hydroxyarylamine O-acetyltransferase; nhoA; BEH70_05090; E6R41_12465; EVY18_22690 DE5DY7B UC A0A0D7LKP9_CITFR DE5DY7B RD Asacolitin DE5DY7B E1 2: Transferase DE5DY7B E2 2.3: Acyltransferase DE5DY7B E3 2.3.1: Acyltransferase DE5DY7B EC 2.3.1.5 DE5DY7B SQ MTPFLTAYFARIGWSDSASVDIETLKALHLLHNGAIPFENLDVLLPREMQLDDLSLEEKLVTARRGGYCFEQNGVFERALREIGFNVRSLLGRVVLANPSSLPPRTHRLLLVELQGEQWIADVGFGGQTLTAPIRLQADIEQQTPHGEYRLVQEGDDWILQFRHHDHWQSMYRFDLVVQHQSDYLMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTRYQDGRAVEQINLPDVASLYALLQEQFGLGVDDVKHGFTEDELATVMAAFDTHPEAGK DE5DY7B TD Primarily distributed in human gut. DE5DY7B FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DE5DY7B KD 2: Bacteria DE5DY7B PL 1224: Proteobacteria DE5DY7B CL 1236: Gammaproteobacteria DE5DY7B OD 91347: Enterobacterales DE5DY7B FM 543: Enterobacteriaceae DE5DY7B GE 544: Citrobacter DE5DY7B SP 546: Citrobacter freundii DEO97D6 ID DEO97D6 DEO97D6 DN VanA ligase (vanA) DEO97D6 GN vanA DEO97D6 SN Vancomycin/teicoplanin A-type resistance protein VanA; D-alanylalanine synthetase VanA; D-alanine--D-alanine ligase VanA; D-Ala-D-Ala ligase VanA; vanA DEO97D6 UC VANA_ENTFC DEO97D6 RD Vancomycin DEO97D6 GI 4670249 DEO97D6 E1 6: Ligase DEO97D6 E2 6.3: Carbon-nitrogen ligase DEO97D6 E3 6.3.2: Peptide synthase DEO97D6 EC 6.3.2.4 DEO97D6 PD 1E4E DEO97D6 SQ MNRIKVAILFGGCSEEHDVSVKSAIEIAANINKEKYEPLYIGITKSGVWKMCEKPCAEWENDNCYSAVLSPDKKMHGLLVKKNHEYEINHVDVAFSALHGKSGEDGSIQGLFELSGIPFVGCDIQSSAICMDKSLTYIVAKNAGIATPAFWVINKDDRPVAATFTYPVFVKPARSGSSFGVKKVNSADELDYAIESARQYDSKILIEQAVSGCEVGCAVLGNSAALVVGEVDQIRLQYGIFRIHQEVEPEKGSENAVITVPADLSAEERGRIQETAKKIYKALGCRGLARVDMFLQDNGRIVLNEVNTLPGFTSYSRYPRMMAAAGIALPELIDRLIVLALKG DEO97D6 TD Primarily distributed in human gut. DEO97D6 FC This enzyme is required for high-level resistance to glycopeptide antibiotics. D-Ala--D-Ala ligase of altered specificity catalyzes ester bond formation between D-Ala and various D-hydroxy acids and produces a peptidoglycan which does not terminate in D-alanine but in D-lactate, thus preventing vancomycin or teicoplanin binding. DEO97D6 KD 2: Bacteria DEO97D6 PL 1239: Firmicutes DEO97D6 CL 91061: Bacilli DEO97D6 OD 186826: Lactobacillales DEO97D6 FM 81852: Enterococcaceae DEO97D6 GE 1350: Enterococcus DEO97D6 SP 1352: Enterococcus faecium DEO97D6 SU Enterococcus faecium BM4147 DEPCQ12 ID DEPCQ12 DEPCQ12 DN Metallo-beta-lactamase (blaM) DEPCQ12 GN blaVIM-2 DEPCQ12 SN Metallo-beta-lactamase NDM-1; New Delhi metallo-beta-lactamase-1; Metallo-beta-lactamase type 2c; Metallo-beta-lactamase type IIc; B2 metallo-beta-lactamase; Beta-lactamase type IIc; NDM-1; blaNDM-1 DEPCQ12 UC Q68K11_ALCXX DEPCQ12 RD Amoxicillin DEPCQ12 E1 3: Hydrolases DEPCQ12 E2 3.5: Carbon-nitrogen hydrolase DEPCQ12 E3 3.5.2: Cyclic amide hydrolase DEPCQ12 EC 3.5.2.6 DEPCQ12 SQ MFKLLSKLLVYLTASIMAIASPLAFSVDSSGEYPTVSEIPVGEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEVEGNEIPTHSLEGLSSSGDAVRFGPVELFYPGAAHSTDNLVVYVPSASVLYGGCAIYELSRTSAGNVADADLAEWPTSIERIQQHYPEAQFVIPGHGLPGGLDLLKHTTNVVKAHTNRSVVE DEPCQ12 TD Primarily distributed in human stomach. DEPCQ12 FC This enzyme hydrolyzes beta-lactam. DEPCQ12 KD 2: Bacteria DEPCQ12 PL 1224: Proteobacteria DEPCQ12 CL 28216: Betaproteobacteria DEPCQ12 OD 80840: Burkholderiales DEPCQ12 FM 506: Alcaligenaceae DEPCQ12 GE 222: Achromobacter DEPCQ12 SP 85698: Achromobacter xylosoxidans DEKW6PB ID DEKW6PB DEKW6PB DN Gamma-glutamylcyclotransferase (GGCT) DEKW6PB GN GGCT DEKW6PB SN Gamma-glutamyl cyclotransferase; Glutamylcyclo-transferase gamma; Cytochrome c-releasing factor 21; AR466_12245 DEKW6PB UC A0A073ACX1_RALSL DEKW6PB RD ANW-43980 DEKW6PB E1 4: Lyases DEKW6PB E2 4.3: Carbon-nitrogen lyase DEKW6PB E3 4.3.2: Amidine-lyase DEKW6PB EC 4.3.2.9 DEKW6PB KG Glutathione metabolism:rsy00480; Metabolic pathways:rsy01100 DEKW6PB SQ MAVTREDLEQNRLRAALGDSPVASTLLTEAALEASLTSTLARLSAPPCDGQDAWVFGYGSLIWNPMIFHTEATCATVHGYHRGFYLYSRINRGTWDNPGLVLGLDRGGSCHGVAFRVPRAHAEREFRVLWRREMMTGAYLPRWLPTEIHGERILALAFVMNRTHEAYAGRLPDERVLGCLHKAVGLYGPAREYLQRTLIGLASNGLHDPYLDRLWQRLQAMDAANAPSQAEDATGTGPSPDPYLSA DEKW6PB TD Primarily distributed in human vagina. DEKW6PB FC This enzyme acts on derivatives of L-glutamate, L-2-aminobutanoate, L-alanine and glycine and acts as a cyclotransferase, cleaving the amide bond via transamidation using the alpha-amine of the L-glutamyl residue, releasing it as the cyclic 5-oxo-L-proline. DEKW6PB KD 2: Bacteria DEKW6PB PL 1224: Proteobacteria DEKW6PB CL 28216: Betaproteobacteria DEKW6PB OD 80840: Burkholderiales DEKW6PB FM 119060: Burkholderiaceae DEKW6PB GE 48736: Ralstonia DEKW6PB SP 305: Ralstonia solanacearum DE28NZ9 ID DE28NZ9 DE28NZ9 DN Cytochrome P450 124 (cyp124) DE28NZ9 GN cyp124 DE28NZ9 SN Cytochrome P450 family 124 subfamily A member 1; Cholest-4-en-3-one C26-monooxygenase; Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]; Cholesterol C26-monooxygenase; Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming]; MTCY339.44c; Methyl-branched lipid omega-hydroxylase; Rv2266; Steroid C26-monooxygenase; Steroid C27-monooxygenase; cyp124 DE28NZ9 UC CP124_MYCTU DE28NZ9 RD Vitamin D DE28NZ9 GI 887763 DE28NZ9 E1 1: Oxidoreductase DE28NZ9 E2 1.14: Oxygen paired donor oxidoreductase DE28NZ9 E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE28NZ9 EC 1.14.15.14 DE28NZ9 PD 2WM4; 2WM5 DE28NZ9 SQ MGLNTAIATRVNGTPPPEVPIADIELGSLDFWALDDDVRDGAFATLRREAPISFWPTIELPGFVAGNGHWALTKYDDVFYASRHPDIFSSYPNITINDQTPELAEYFGSMIVLDDPRHQRLRSIVSRAFTPKVVARIEAAVRDRAHRLVSSMIANNPDRQADLVSELAGPLPLQIICDMMGIPKADHQRIFHWTNVILGFGDPDLATDFDEFMQVSADIGAYATALAEDRRVNHHDDLTSSLVEAEVDGERLSSREIASFFILLVVAGNETTRNAITHGVLALSRYPEQRDRWWSDFDGLAPTAVEEIVRWASPVVYMRRTLTQDIELRGTKMAAGDKVSLWYCSANRDESKFADPWTFDLARNPNPHLGFGGGGAHFCLGANLARREIRVAFDELRRQMPDVVATEEPARLLSQFIHGIKTLPVTWS DE28NZ9 TD Primarily distributed in human gut. DE28NZ9 FC This enzyme is a P-450 heme-thiolate protein, and it primarily hydroxylates the omega-carbon of a number of methyl-branched lipids, including (2E,6E)-farnesol, phytanate, geranylgeraniol, 15-methylpalmitate and (2E,6E)-farnesyl diphosphate. And it also catalyzes the sequential oxidation of the terminal methyl of cholest-4-en-3-one into (25R)-26-hydroxycholest-4-en-3-one (alcohol), (25R)-26-oxocholest-4-en-3-one (aldehyde), to finally yield the carboxylic acid (25R)-3-oxocholest-4-en-26-oate. DE28NZ9 KD 2: Bacteria DE28NZ9 PL 201174: Actinobacteria DE28NZ9 CL 1760: Actinobacteria DE28NZ9 OD 85007: Corynebacteriales DE28NZ9 FM 1762: Mycobacteriaceae DE28NZ9 GE 1763: Mycobacterium DE28NZ9 SP 1773: Mycobacterium tuberculosis DEFKSVZ ID DEFKSVZ DEFKSVZ DN Catechol-2,3-dioxygenase (caD) DEFKSVZ GN DZB84_00060 DEFKSVZ SN Catechol dioxygenase; Catechol 2,3-dioxygenase; caD; cado; DZB84_00060 DEFKSVZ UC A0A371SLU3_9BACI DEFKSVZ RD Gemfibrozil DEFKSVZ E1 1: Oxidoreductase DEFKSVZ E2 1.13: Oxygen single donor oxidoreductase DEFKSVZ E3 1.13.11: Oxygen single donor oxidoreductase DEFKSVZ EC 1.13.11.2 DEFKSVZ SQ MSNFDVAQLAHVELYSPKPEETLKFFTDYLGLQISAREGQSVYLRAYEDFYHHTLKITEAKEAGMAHTAWRASSEAALYQRVQSLEKSGYGKGWIEGDLGHGAAYQFQTPDGHNMEILWNVEYYRAPEDQKTMLKSRPQKRPNIGIPARRLDHINLMCGNVTQNKQFMADELGFKLRENIIMNDGAEMGAWMSVSPLVHEIALMGDQSGEKGRFHHVAYWYGYPQHLMDLADLLVENGIEIEAGPGKHGISQAYFMYVFEPGGNRVELFGDSGYLILDPDWKTITWKEEELDKGIIWYGSPLPQEYFIYGTPDRSSVKVK DEFKSVZ TD Primarily distributed in human gut. DEFKSVZ FC This enzyme initiates the meta-cleavage pathway of catechol degradation and requires FeII. DEFKSVZ KD 2: Bacteria DEFKSVZ PL 1239: Firmicutes DEFKSVZ CL 91061: Bacilli DEFKSVZ OD 1385: Bacillales DEFKSVZ FM 186817: Bacillaceae DEFKSVZ GE 1386: Bacillus DEFKSVZ SP 1408: Bacillus pumilus DEMSNER ID DEMSNER DEMSNER DN Beta-lactamase (blaB) DEMSNER GN blaC DEMSNER SN Penicillinase; Cephalosporinase; Beta-lactam; blaC DEMSNER UC A4LA84_EDWTA DEMSNER RD Clindamycin DEMSNER E1 3: Hydrolases DEMSNER E2 3.5: Carbon-nitrogen hydrolase DEMSNER E3 3.5.2: Cyclic amide hydrolase DEMSNER EC 3.5.2.6 DEMSNER SQ MMNTRLSCTLALSALLLSSGAQASTPPSAEMRVAEAVKQTIPALMQQQQIPGMAVAVIYQGTPYYFSYGVADKATRRAVTPQTLFELGSVSKTFTGVLGGYALQRGDIRLQDTVASQWPALNGPQWRAITLQQLATYTAGGLPLQVPDAVTDTAQLLDFYQRWQPRWAPGTMRSYSNASIGLFGMLAVRPSGMDFSQAMTRWVLQPLGLKHTYFRVPPAAEGEYAWGYREGKALRVSPGMLEQEAYGIKSSAQDMATWLQANLDPAAVTQATLRQALLRAQTRYYQSGEMYQGLGWEMLSWPLQAQTLIDGSDNRVALQPQPVHLIEPPTPPQPASWVHKTGSTNGFGAYIAFIPGSRLGIVMLANKNYPNPARVQAAYTILQQLQ DEMSNER TD Primarily distributed in human gut. DEMSNER FC This enzyme hydrolyzes beta-lactam. DEMSNER KD 2: Bacteria DEMSNER PL 1224: Proteobacteria DEMSNER CL 1236: Gammaproteobacteria DEMSNER OD 91347: Enterobacterales DEMSNER FM 1903412: Hafniaceae DEMSNER GE 635: Edwardsiella DEMSNER SP 636: Edwardsiella tarda DEM1BHT ID DEM1BHT DEM1BHT DN Azoreductase (azoR) DEM1BHT GN acpH DEM1BHT SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; A5810_000531; AS238_04965; B1P95_03410; BU183_03850; BU187_02260; BU190_11865; BU192_09835; BXT96_08720; CQR37_06980; CUM68_06655; CUN04_07390; DJ550_05610; DKP91_06820; DRZ84_07550; DTPHA_1403160; DTPHA_601027; EB63_02313; EWH22_12905; F6439_02410; F6440_11520; NCTC13923_00920; acpH DEM1BHT UC A0A132Z973_ENTFC DEM1BHT RD Sulfasalazine DEM1BHT E1 1: Oxidoreductase DEM1BHT E2 1.7: Cytochrome acceptor oxidoreductase DEM1BHT E3 1.7.1: NAD/NADP acceptor oxidoreductase DEM1BHT EC 1.7.1.6 DEM1BHT SQ MASVLVVKGHPLTAEESRTVKALTSFLTSYKENHPDDEVTVLELYRDDIPEIDEELLSGWEALRAGAEFTSLSESQQQKIARFNELTDQFLAADKIVIANALWNLNIPTKLKAWFDTVNVAGKTFRYTENGPEGLVTGKKALHIQSNGGVYNGQDFASQYVKGILNFVGIDQVDQLFIEGIDYDPDRADELMQNALDKAAALGKSF DEM1BHT TD Primarily distributed in human gut. DEM1BHT FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. And it requires NADH, but not NADPH, as an electron donor for its activity. DEM1BHT KD 2: Bacteria DEM1BHT PL 1239: Firmicutes DEM1BHT CL 91061: Bacilli DEM1BHT OD 186826: Lactobacillales DEM1BHT FM 81852: Enterococcaceae DEM1BHT GE 1350: Enterococcus DEM1BHT SP 1352: Enterococcus faecium DE8UGTM ID DE8UGTM DE8UGTM DN Aldehyde oxidase (AOX) DE8UGTM GN xdhAC DE8UGTM SN Aldehyde oxidase/xanthine dehydrogenase; Xanthine dehydrogenase molybdopterin-binding; NCTC534_00123; VT96_0232590; xdhAC DE8UGTM UC A0A1V9IQJ2_CLOSG DE8UGTM RD Zonisamide DE8UGTM E1 1: Oxidoreductase DE8UGTM E2 1.17: CH/CH2 oxidoreductase DE8UGTM E3 1.17.1: NAD/NADP acceptor oxidoreductase DE8UGTM EC 1.17.1.4 DE8UGTM SQ MYEFILNGRNVSVSEDMNLLEYLRDHEDLTSVKNGCAEGACGACMILLDGKAVRACINTTAKVHGKDIKTVEGLTEFEKKVFTWAFSKAGAVQCGFCIPGMIISAKALLDKNLNPNKKEIKTAIRGNVCRCTGYVKIIKAIEMAAEAFRDGKLILNEEYKGKIGENIPRIDARDKILGIGKYVDDMKVEGMIYGSALRIKYPRALVKSIDISEALKHPDVETIITAKDIPGNRYIGHIIKDWPAMIDVGEETRYVGDSVALVAAKNKKALKEILNLIKVEYEELEPISNPDMAMDEDAPKIHPKGNVLTVEKVNRGDVDEAIANSKYVVSNHYSTPFTEHAFLELESALAMPDEDGVIIYTGSQGIYDEQREISELLGLPKEKVRTISKYVGGGFGGKEDMSVQHHAALLAWIIKKPVKVTLSRKESIKIHPKRHAMEMTITTACDEKGNLTAFKADIVADTGAYASLGGPVLQRACTHAAGPYKCPNVKIKGTAVYTNNPPGGAFRGFGVTQSVFASECNLNLLAQKVGISPWEIRFKNAVEPGDALPNGQIADKGTAIKETILAVKDIYENNKYVGIACCMKNSGVGVGLPDIGRCNLVVIKGKVHIRTSAACIGQGLGTILIQIICETTDLLPEQIILDLPDTKFAPNSGTTTASRQTVFTGEATRIASLKLKDKLLTTSLEECEGEEFYGEYQGITDPINSDKKNPVSHVAYGYATQVVILNDDGKVEKVVAAHDVGKAINSTNVEGQIEGGIVMGLGYAFTEDYPLNKSIPTAKFGTLGLFRATDIPEIQPIIIEKNTNDLAYGAKGIGEITTIPTAPAAQGAYYKFDGEFRKKLPLKDTAYRRKK DE8UGTM TD Primarily distributed in human gut. DE8UGTM FC This enzyme acts on a variety of purines and aldehydes, including hypoxanthine. DE8UGTM KD 2: Bacteria DE8UGTM PL 1239: Firmicutes DE8UGTM CL 186801: Clostridia DE8UGTM OD 186802: Clostridiales DE8UGTM FM 31979: Clostridiaceae DE8UGTM GE 1485: Clostridium DE8UGTM SP 1509: Clostridium sporogenes DEMQ20F ID DEMQ20F DEMQ20F DN Cytochrome P450 142A1 (cyp142) DEMQ20F GN cyp142 DEMQ20F SN Cytochrome P450 family 142 subfamily A member 1; Cholest-4-en-3-one C26-monooxygenase 142A1; Cholest-4-en-3-one C26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming] 142A1; Cholesterol C26-monooxygenase 142A1; Cholesterol C26-monooxygenase [(25R)-3beta-hydroxycholest-5-en-26-oate forming] 142A1; MTV023.25c; Rv3518c; Steroid C26-monooxygenase 142A1; Steroid C27-monooxygenase 142A1; cyp142A1 DEMQ20F UC CP142_MYCTU DEMQ20F RD ANW-32821 DEMQ20F GI 888282 DEMQ20F E1 1: Oxidoreductase DEMQ20F E2 1.14: Oxygen paired donor oxidoreductase DEMQ20F E3 1.14.15: Iron-sulfur protein donor oxidoreductase DEMQ20F EC 1.14.15.28 DEMQ20F KG Microbial metabolism in diverse environments:mtu01120; Steroid degradation:mtu00984 DEMQ20F PD 2XKR DEMQ20F SQ MTEAPDVDLADGNFYASREARAAYRWMRANQPVFRDRNGLAAASTYQAVIDAERQPELFSNAGGIRPDQPALPMMIDMDDPAHLLRRKLVNAGFTRKRVKDKEASIAALCDTLIDAVCERGECDFVRDLAAPLPMAVIGDMLGVRPEQRDMFLRWSDDLVTFLSSHVSQEDFQITMDAFAAYNDFTRATIAARRADPTDDLVSVLVSSEVDGERLSDDELVMETLLILIGGDETTRHTLSGGTEQLLRNRDQWDLLQRDPSLLPGAIEEMLRWTAPVKNMCRVLTADTEFHGTALCAGEKMMLLFESANFDEAVFCEPEKFDVQRNPNSHLAFGFGTHFCLGNQLARLELSLMTERVLRRLPDLRLVADDSVLPLRPANFVSGLESMPVVFTPSPPLG DEMQ20F TD Primarily distributed in human gut. DEMQ20F FC This enzyme is a P-450 heme-thiolate protein, and it is involved in degradation of the host cholesterol. The enzyme catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25R) conformation. And it also accepts cholesterol as a substrate. DEMQ20F KD 2: Bacteria DEMQ20F PL 201174: Actinobacteria DEMQ20F CL 1760: Actinobacteria DEMQ20F OD 85007: Corynebacteriales DEMQ20F FM 1762: Mycobacteriaceae DEMQ20F GE 1763: Mycobacterium DEMQ20F SP 1773: Mycobacterium tuberculosis DELIXR8 ID DELIXR8 DELIXR8 DN Cytochrome P450 125A1 (cyp125) DELIXR8 GN cyp125 DELIXR8 SN Cytochrome P450 family 125 subfamily A member 1; Cholest-4-en-3-one 26-monooxygenase 125A1; Cholest-4-en-3-one C26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] 125A1; Cholesterol C26-monooxygenase 125A1; Cholesterol C26-monooxygenase [(25S)-3beta-hydroxycholest-5-en-26-oate forming] 125A1; MTCY03C7.11; Rv3545c; Steroid C26-monooxygenase 125A1; Steroid C27-monooxygenase 125A1; cyp125A1 DELIXR8 UC CP125_MYCTU DELIXR8 RD ANW-32821 DELIXR8 GI 887782 DELIXR8 E1 1: Oxidoreductase DELIXR8 E2 1.14: Oxygen paired donor oxidoreductase DELIXR8 E3 1.14.15: Iron-sulfur protein donor oxidoreductase DELIXR8 EC 1.14.15.29 DELIXR8 KG Microbial metabolism in diverse environments:mtu01120; Steroid degradation:mtu00984 DELIXR8 PD 2X5L; 2X5W; 2XC3; 2XN8; 3IVY; 3IW0; 3IW1; 3IW2 DELIXR8 SQ MSWNHQSVEIAVRRTTVPSPNLPPGFDFTDPAIYAERLPVAEFAELRSAAPIWWNGQDPGKGGGFHDGGFWAITKLNDVKEISRHSDVFSSYENGVIPRFKNDIAREDIEVQRFVMLNMDAPHHTRLRKIISRGFTPRAVGRLHDELQERAQKIAAEAAAAGSGDFVEQVSCELPLQAIAGLLGVPQEDRGKLFHWSNEMTGNEDPEYAHIDPKASSAELIGYAMKMAEEKAKNPADDIVTQLIQADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITQGMMAFAEHPDQWELYKKVRPETAADEIVRWATPVTAFQRTALRDYELSGVQIKKGQRVVMFYRSANFDEEVFQDPFTFNILRNPNPHVGFGGTGAHYCIGANLARMTINLIFNAVADHMPDLKPISAPERLRSGWLNGIKHWQVDYTGRCPVAH DELIXR8 TD Primarily distributed in human gut. DELIXR8 FC This enzyme is a P-450 heme-thiolate protein found in several bacterial pathogens, and it is involved in degradation of the host's cholesterol. The enzyme catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol . The products are exclusively in the (25S) configuration. And it also accepts cholesterol as a substrate. DELIXR8 KD 2: Bacteria DELIXR8 PL 201174: Actinobacteria DELIXR8 CL 1760: Actinobacteria DELIXR8 OD 85007: Corynebacteriales DELIXR8 FM 1762: Mycobacteriaceae DELIXR8 GE 1763: Mycobacterium DELIXR8 SP 1773: Mycobacterium tuberculosis DEX2ZLF ID DEX2ZLF DEX2ZLF DN Tyrosine decarboxylase (tdc) DEX2ZLF GN tdc DEX2ZLF SN Levodopa decarboxylase; L-dopa decarboxylase; L-tyrosine decarboxylase; TDC; tdc; tdcA; CNR29_12740; N624_0219; TDC; UCCLBBS449_2369 DEX2ZLF UC TYRDC_LACBR DEX2ZLF RD Levodopa DEX2ZLF GI 4413406 DEX2ZLF E1 4: Lyases DEX2ZLF E2 4.1: Carbon-carbon lyase DEX2ZLF E3 4.1.1: Carboxy-lyase DEX2ZLF EC 4.1.1.25 DEX2ZLF PD 5HSI; 5HSJ DEX2ZLF SQ MEKSNRSLKDLDLNALFIGDKAENGQLYKDLLNKLVDEHLGWRKNYIPSDPNMIGPEDQNSPAFKKTVGHMKTVLDQLSERIRTESVPWHSAGRYWGHMNSETLMPALLAYNYAMLWNGNNVAYESSPATSQMEEEVGQEFARLMGYDYGWGHIVADGSLANLEGLWYARNIKSLPFAMKEVNPELVAGKSDWELLNMPTKEIMDLLENAGSQIDEVKKRSARSGKNLQRLGKWLVPQTKHYSWMKAADIIGIGLDQVVPVPIDSNYRMDIQALESIIRKYAAEKTPILGVVGVAGSTEEGAVDGIDKIVALRQKLQKEGIYFYLHVDAAYGGYARALFLDEDDQFIPYKNLQKVHAENHVFTEDKEYIKPEVYAAYKAFDQAESITIDPHKMGYVPYSAGGIVIQDIRMRDTISYFATYVFEKGADIPALLGAYILEGSKAGATAASVWAAHHTLPLNVTGYGKLEGASIEGAHRYYDFLKNLKFEVAGKRISVHPLISPDFNMVDYVLKEDGNDDLIEMNRLNHAFYEQASYVKGSLYGKEYIVSHTDFAIPDYGDSPLAFVESLGFSEVEWRHAGKVTIIRASVMTPYMNQRENFDYFAPRIKKAIQADLEKVYASVNQKENV DEX2ZLF TD Primarily distributed in human gut. DEX2ZLF FC This enzyme catalyzes the decarboxylation of L-tyrosine to produce tyramine. DEX2ZLF KD 2: Bacteria DEX2ZLF PL 1239: Firmicutes DEX2ZLF CL 91061: Bacilli DEX2ZLF OD 186826: Lactobacillales DEX2ZLF FM 33958: Lactobacillaceae DEX2ZLF GE 1578: Lactobacillus DEX2ZLF SP 1580: Lactobacillus brevis DEVSIE6 ID DEVSIE6 DEVSIE6 DN Glyceraldehyde-3-phosphate dehydrogenase (gap) DEVSIE6 GN gap DEVSIE6 SN Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase; DM298_07395; DWV49_09860; FCF10_01070; GAPDH; LAC30SC_03490 DEVSIE6 UC A0A3A9YGB0_LACAI DEVSIE6 RD AS-12141 DEVSIE6 GI 31801837 DEVSIE6 E1 1: Oxidoreductase DEVSIE6 E2 1.2: Aldehyde/oxo donor oxidoreductase DEVSIE6 E3 1.2.1: NAD/NADP acceptor oxidoreductase DEVSIE6 EC 1.2.1.- DEVSIE6 KG Biosynthesis of amino acids:lai01230; Biosynthesis of secondary metabolites:lai01110; Carbon metabolism:lai01200; Glycolysis / Gluconeogenesis:lai00010; Metabolic pathways:lai01100; Microbial metabolism in diverse environments:lai01120 DEVSIE6 SQ MTVKIGINGFGRIGRLAFRRIMDLGEKTKDIEVVAINDLTTPAMLAYLLKYDTTHGTFNHEVSSTDDSIVVDGKKYRVYAEPQAQNIPWVKNDGVDFVLECTGFYTSKAKSQAHLDAGAKRVLISAPAGNDLKTIVYSVNENTLTADDKIVSAASCTTNSLAPMANALDKEFGIEVATMTTIHAYTGTQMTLDGPSRSGKEQDARAAAENIIPHTTGSAKAIGLVLPNLNGKMNGHAQRVPVPDGSETELVSILKKKVTADEVNEAMKKYESPSFAYNGDHIVSSDVINMTAGSIFDPTQTMVTTAGDKQLVKTVAWYDNEYSFTCQMVRTLLHFATL DEVSIE6 TD Primarily distributed in human gut. DEVSIE6 FC This enzyme takes part in glucose metabolic process. DEVSIE6 KD 2: Bacteria DEVSIE6 PL 1239: Firmicutes DEVSIE6 CL 91061: Bacilli DEVSIE6 OD 186826: Lactobacillales DEVSIE6 FM 33958: Lactobacillaceae DEVSIE6 GE 1578: Lactobacillus DEVSIE6 SP 1579: Lactobacillus acidophilus DEXG57F ID DEXG57F DEXG57F DN Flavin adenine dinucleotide dehydrogenase (fadd) DEXG57F GN apbE1 DEXG57F SN FAD pyrophosphorylase; FAD synthase; FMN adenylyltransferase DEXG57F UC APBE1_KLEP3 DEXG57F RD RO-7-0207 DEXG57F E1 1: Oxidoreductase DEXG57F E2 1.5: CH-NH donor oxidoreductase DEXG57F E3 1.5.1: NAD/NADP acceptor oxidoreductase DEXG57F EC 1.5.1.37 DEXG57F SQ MDMTFFRAALLGACVLLSGCDSATTPASPASTATVLDGKTMGTFWRVSVIGVDEAKAEALRAKVQAQLDADDRLLSTWKNDSALMRFNHAADTRPWPVSEAMVDIVTLSLRIGAKTHGAMDITVGPLVNLWGFGPDKQPVTTPDAQAIAAAKARTGLQHLQVINQSGRQFLQKDIPDLFVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALVSRGMNGEGKPWRVAIQKPTDRENAVQAIVDINGHGISTSGSYRNYYELDGKRISHVIDPQTGQPITHKLVSVTVIAPTALEADGWDTGLMVLGPEKAQQVVREQGLAVYMIVKEGEGFKTWMSPQFRTFLVGEKN DEXG57F TD Primarily distributed in human gut. DEXG57F FC This enzyme can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. But it can not reduce riboflavin and does not use NADPH as acceptor. DEXG57F KD 2: Bacteria DEXG57F PL 1239: Firmicutes DEXG57F CL 186801: Clostridia DEXG57F OD 186802: Clostridiales DEXG57F FM 31979: Clostridiaceae DEXG57F GE 1485: Clostridium DEXG57F SP 1502: Clostridium perfringens DETP28W ID DETP28W DETP28W DN L-arabinose isomerase (araA) DETP28W GN araA DETP28W SN Isomerase L-arabinose; D-arabinose aldose-ketose-isomerase; araA; LCA_1856 DETP28W UC ARAA_LACSS DETP28W RD CERC-801 DETP28W GI 29637087 DETP28W E1 5: Isomerase DETP28W E2 5.3: Intramolecular oxidoreductase DETP28W E3 5.3.1: Aldose/ketose isomerase DETP28W EC 5.3.1.4 DETP28W KG Metabolic pathways:lsa01100; Pentose and glucuronate interconversions:lsa00040 DETP28W SQ MLNTENYEFWFVTGSQSLYGEETLRSVEKDAKEIVEKLNASHQLPYPIVFKLVATTADNITKVMKEANYNDHVAGVITWMHTFSPAKNWIRGTKLLQKPLLHLATQFLNKIPYDTIDFDYMNLNQSAHGDREYAFINARLRKNNKIISGYWGDEDVQKAMAKWMDVAVAYNESFKIKVVTFADKMRNVAVTDGDKVEAQIKFGWTVDYWGVGDLVAEVNAVSEADIDAKYADLQKEYDFVEGQNTPEKFEHNVKYQIREYFGLKKFMDDRGYTAFTTNFEDLVGLEQLPGLAAQLLMAEGYGFAGEGDWKTAALDRLLKIMAHNEKTVFMEDYTLDLRQGHEAILGSHMLEVDPSIASDKPRVEVHPLDIGDKDDPARLVFTGMQGDAVDVTMADYGDEFKLMSYDVRGNKPEADTPHLPVAKQLWTPKQGLREGAVGWLTVGGGHHTVLSFAVDSEQLQDLSHLFDLTYVNIK DETP28W TD Primarily distributed in human gut. DETP28W FC This enzyme catalyzes the conversion of L-arabinose to L-ribulose. It requires a divalent metal ion and binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism. It can also convert D-galactose to D-tagatose with lower efficiency. DETP28W KD 2: Bacteria DETP28W PL 1239: Firmicutes DETP28W CL 91061: Bacilli DETP28W OD 186826: Lactobacillales DETP28W FM 33958: Lactobacillaceae DETP28W GE 1578: Lactobacillus DETP28W SP 1599: Lactobacillus sakei DETP28W SU Lactobacillus sakei 23K DEQMBHW ID DEQMBHW DEQMBHW DN Dipeptidase (pepV) DEQMBHW GN pepV DEQMBHW SN Dipeptidase pepV; Glycosyl-phosphatidylinositol-anchored renal dipeptidase; F4V48_10275; RU90_GL001300; pepV DEQMBHW UC Q84BU9_LACLH DEQMBHW RD Enalapril DEQMBHW E1 3: Hydrolases DEQMBHW E2 3.4: Peptidase DEQMBHW E3 3.4.13: Dipeptidase DEQMBHW EC 3.4.13.- DEQMBHW SQ MTTIDFKAEVEKLKDALMEDLFSLLRIDSAMDMEHADAENPFGPGPRKALDAFLKIAERDGYTTKNYDNYVGHFEYENGASDDAEVLGIIGHLDVVPAGSGWDSNPFEPEIRNGNLYARGASDDKGPTVACYYALKILKELNLPLSKKIRFIVGTNEETGWADMDYYFEHCELPLPDFGFSPDAEFPIINGEKGNITEYLHFAGKNAGEVVLHSFKAGLAENMVPESATAVISGAKDLQAALEKFVAEHASKNLRFDLEETAGKATVTLYGKSAHGAMPEKGVNGATYLTLFLNQFNFADGAAAFIKVGAEKLLEDHEGEKLGTAYVDELMGNTSMNAGVWSFDENSEGKIALNFRFPQGNSPERMQEILAKLDGVVEVELSKHLHVPHYVPMSDPLVSTLIDVYEKHTGLKGYETIIGGGTFGRLLERGVAYGAMFEGEPDSMHQANEMKPVENIYKAAVIYAEAIYELTK DEQMBHW TD Primarily distributed in human gut. DEQMBHW FC This enzyme catalyzes the conversion of dipeptides into amino acids. DEQMBHW KD 2: Bacteria DEQMBHW PL 1239: Firmicutes DEQMBHW CL 91061: Bacilli DEQMBHW OD 186826: Lactobacillales DEQMBHW FM 1300: Streptococcaceae DEQMBHW GE 1357: Lactococcus DEQMBHW SP 1358: Lactococcus lactis DEQMBHW SU Lactococcus lactis subsp. hordniae (hT); Lactococcus lactis subsp. cremoris (L6); Lactococcus lactis subsp. lactis (L9) DEPR1Y7 ID DEPR1Y7 DEPR1Y7 DN Beta-galactosidase (bgaB) DEPR1Y7 GN bgaB DEPR1Y7 SN Beta-galactosidase/glucuronidase; Beta-galactosidase BgaBeta; Beta-Gal II; Beta-gal; BAD_1401; bgaB; bgaLII DEPR1Y7 UC BGAL_BIFAA DEPR1Y7 RD LS-71719 DEPR1Y7 GI 4557550 DEPR1Y7 E1 3: Hydrolases DEPR1Y7 E2 3.2: Glycosylase DEPR1Y7 E3 3.2.1: O/S-glycosyl compound glycosidase DEPR1Y7 EC 3.2.1.23 DEPR1Y7 KG Galactose metabolism:bad00052 DEPR1Y7 PD 5VYM DEPR1Y7 SQ MSARRNFEWPELLTADGRGIAFGGDYNPDQWSEDIWDDDIRLMKQAGVNTVALAIFSWDRIQPTEDRWDFGWLDRIIDKLGNAGIVVDLASATATAPLWLYESHPEVLPRDKYGHPVNAGSRQSWSPTSPVFKEYALTLCRKLAERYGTNPYVTAWHMGNEYGWNNREDYSDNALEAFRAWCRRKYGTIDALNQAWGTTFWGQEMNGFDEVLIPRFMGADSMVNPGQKLDFERFGNDMLLDFYKAERDAIAEICPDKPFTTNFMVSTDQCCMDYAAWAKEVNFVSNDHYFHEGESHLDELACSDALMDSLALGKPWYVMEHSTSAVQWKPLNTRKRKGETVRDSLAHVAMGADAINFFQWRASAFGAEAFHSAMVPHAGEDTKLFRQVCELGASLHTLADAGVQGTELAHSDTAILFSAESEWATRSQTLPSMKLNHWHDVRDWYRAFLDAGSRADIVPLAYDWSSYKTVVLPTVLILSAADTQRLADFAAAGGRVVVGYATGLIDEHFHTWLGGYPGAGDGLLRSMLGVRGEEFNILGAEAEGEPGEIRLSSADDSAALDGTTTRLWQNDVNVTGEHAQVLATYAGEEADEWELDGTAAVTRNPYGSGEAYFVGCDLDVADLTKLVRAYLAASSQENADVLHTVRASADATFDFYLPRGKKTVELQGIEGEPVILFQTDREEKPGSYTVRRNGVLVVRR DEPR1Y7 TD Primarily distributed in human gut. DEPR1Y7 FC This enzyme is involved in the hydrolysis of transgalactooligosaccharides. DEPR1Y7 KD 2: Bacteria DEPR1Y7 PL 201174: Actinobacteria DEPR1Y7 CL 1760: Actinobacteria DEPR1Y7 OD 85004: Bifidobacteriales DEPR1Y7 FM 31953: Bifidobacteriaceae DEPR1Y7 GE 1678: Bifidobacterium DEPR1Y7 SP 1680: Bifidobacterium adolescentis DEPR1Y7 SU Bifidobacterium adolescentis DSM 20083; Bifidobacterium adolescentis YIT 4011(T) DE97F4R ID DE97F4R DE97F4R DN Arylamine N-acetyltransferase (NAT) DE97F4R GN nat DE97F4R SN N-hydroxyarylamine O-acetyltransferase; nhoA; nat; PWN146_00756 DE97F4R UC A0A1C3HAL9_SERMA DE97F4R RD Asacolitin DE97F4R E1 2: Transferase DE97F4R E2 2.3: Acyltransferase DE97F4R E3 2.3.1: Acyltransferase DE97F4R EC 2.3.1.5 DE97F4R SQ MDTQRYLQHIGFIGAARPDLPTLQQLHHRHMLSVPFENLSIIYHQGIRLAPEALFSKVVERNRGGFCYELNTLFALLLREIGFKVSFISGEIRARDGHFGPPYDHLALRVDLEDQAWLVDVGFGDSFLTPLKIVVAEPQPQASGTFHLEQEGEYYLLERRNGDQRSHAKTLYRFTIQPRALHEFDEMCRFHSTSPQSHFTQRLVCSRPTDHGRVTLSDMKLIVTEDHQRHETTLHSEEERRAALWQHFAIDLDR DE97F4R TD Primarily distributed in human gut. DE97F4R FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DE97F4R KD 2: Bacteria DE97F4R PL 1224: Proteobacteria DE97F4R CL 1236: Gammaproteobacteria DE97F4R OD 91347: Enterobacterales DE97F4R FM 543: Enterobacteriaceae DE97F4R GE 620: Shigella DE97F4R SP 623: Shigella flexneri DE14FI7 ID DE14FI7 DE14FI7 DN Arylamine N-acetyltransferase (NAT) DE14FI7 GN NAT DE14FI7 SN N-hydroxyarylamine O-acetyltransferase; nhoA; B9P90_27370; KOX_19355 DE14FI7 UC A0A0H3HB23_KLEOK DE14FI7 RD Asacolitin DE14FI7 E1 2: Transferase DE14FI7 E2 2.3: Acyltransferase DE14FI7 E3 2.3.1: Acyltransferase DE14FI7 EC 2.3.1.5 DE14FI7 SQ MHSDSFDLSLYFRRIGYSGPAAADTATLHALMRHQLFAIPFENLDVQAGKIVSMEPDDIANKLLRQRRGGYCYELNGLFTMALEALGIAWRFVAARPMFYPARRPKTHMAVVAEVEGRQWLCDLGFGSYGIRAPLALDELDTDIIQDFDTFRLSRDAHGDYLLQAKVEGSWANQYGFDLSPQEWIDFAPANFLNSTHPDAVFVQKLLVIQHQPEGRFILLGNTLKSITADRVEKQRLEDDEIAHVLEQRFALSAR DE14FI7 TD Primarily distributed in human gut. DE14FI7 FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DE14FI7 KD 2: Bacteria DE14FI7 PL 1224: Proteobacteria DE14FI7 CL 1236: Gammaproteobacteria DE14FI7 OD 91347: Enterobacterales DE14FI7 FM 543: Enterobacteriaceae DE14FI7 GE 570: Klebsiella DE14FI7 SP 571: Klebsiella oxytoca DEKU5HL ID DEKU5HL DEKU5HL DN Alcohol dehydrogenase (ADH) DEKU5HL GN ADH DEKU5HL SN Alcohol dehydrogenase AdhP; Zinc-dependent alcohol dehydrogenase; Zn-dependent alcohol dehydrogenase; Iron-containing alcohol dehydrogenase; B5F04_01565; B5G22_01675; DKZ26_04195; DKZ35_01550; EGO58_03565; EW144_06055; LRLP16767_LR202_00415; lr1793 DEKU5HL UC A4L2V0_LACRE DEKU5HL RD D-glucose DEKU5HL GI 5188789 DEKU5HL E1 1: Oxidoreductase DEKU5HL E2 1.1: CH-OH donor oxidoreductase DEKU5HL E3 1.1.1: NAD/NADP oxidoreductase DEKU5HL EC 1.1.1.1 DEKU5HL SQ MNRQFDFLMPSVNFFGPGVIAKIGDRAKMLNMHKPLIVTTEGLSKIDNGPVKQTVASLEKAGVDYAVFTGAEPNPKIRNVQAGKKMYQDENCDSIITVGGGSAHDCGKGIGIVLTNGDDISKLAGIETLKNPLPPLMAVNTTAGTGSELTRHAVITNEKTHLKFVVVSWRNIPLVSFNDPMLMLDIPKDITAATGCDAFVQAIEPYVSVDHNPITDSQCKEAIQLIQTALPEVVANGHNIEARTKMVEAEMLAGMAFNNANLGYVHAMAHQLGGQYDAPHGVCCALLLTTVEEYNLIACPERFAELAKVMGFDTTGLTLYEAAQKSIDGMREMCRLVGIPSSIKEIGAKPEDFEMMAKNALKDGNAFSNPRKGTVEDIVKLYQKAYDGIY DEKU5HL TD Primarily distributed in human gut. DEKU5HL FC This enzyme uses NAD+ to oxidize ethanol and 1,3-propanediol. DEKU5HL KD 2: Bacteria DEKU5HL PL 1239: Firmicutes DEKU5HL CL 91061: Bacilli DEKU5HL OD 186826: Lactobacillales DEKU5HL FM 33958: Lactobacillaceae DEKU5HL GE 1578: Lactobacillus DEKU5HL SP 1598: Lactobacillus reuteri DEN6VO0 ID DEN6VO0 DEN6VO0 DN VanA ligase (vanA) DEN6VO0 GN vanA DEN6VO0 SN Vancomycin/teicoplanin A-type resistance protein VanA; D-alanylalanine synthetase VanA; D-alanine--D-alanine ligase VanA; D-Ala-D-Ala ligase VanA; NCTC12360_01403; vanA DEN6VO0 UC A0A376GZ73_ENTGA DEN6VO0 RD Vancomycin DEN6VO0 E1 6: Ligase DEN6VO0 E2 6.3: Carbon-nitrogen ligase DEN6VO0 E3 6.3.2: Peptide synthase DEN6VO0 EC 6.3.2.4 DEN6VO0 SQ MMKKIAVLFGGNSPEYSVSLASAASVIQAIDPLKYEVMTIGIAPTMDWYLYQGNLKNVRNDTWLEDHKNCHQLTFSSQGFMLGEKRIVPDVLFPVLHGKYGEDGCIQGLLELMNLPYVGCHVAASALCMNKWLLHQLADTMGIASAPTLLLSRYENDPATIDRFIQDHGFPIFIKPNEAGSSKGITKVTDKTALQSALTNAFAYGSTVLIQKAIAGIEIGCGILGNEQLTIGACDAISLVDGFFDFEEKYQLISATITVPAPLPLALESQIKEQAQLLYRNLGLTGLARIDFFVTDQGAIYLNEINTMPGFTGHSRYPAMMAEVGLSYEMLVEQLIALAEEDKR DEN6VO0 TD Primarily distributed in human gut. DEN6VO0 FC This enzyme is involved with UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase (EC 6.3.2.7) or UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase (EC 6.3.2.13), UDP-N-acetylmuramate---L-alanine ligase (EC 6.3.2.8), UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase (EC 6.3.2.9) and UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase (EC 6.3.2.10) in the synthesis of a cell-wall peptide. DEN6VO0 KD 2: Bacteria DEN6VO0 PL 1239: Firmicutes DEN6VO0 CL 91061: Bacilli DEN6VO0 OD 186826: Lactobacillales DEN6VO0 FM 81852: Enterococcaceae DEN6VO0 GE 1350: Enterococcus DEN6VO0 SP 1353: Enterococcus gallinarum DEN6VO0 SU Enterococcus gallinarum BM4231 DEH4O6C ID DEH4O6C DEH4O6C DN Thymidylate synthase (thyA) DEH4O6C GN thyA DEH4O6C SN Bacterial dihydrofolate reductase-thymidylate synthase; dTMP synthase; BgDHFR-TS; DHFR-TS; HTS; thyA DEH4O6C UC TYSY_LACCA DEH4O6C RD Deoxy-UMP DEH4O6C E1 2: Transferase DEH4O6C E2 2.1: Methylase DEH4O6C E3 2.1.1: Methyltransferase DEH4O6C EC 2.1.1.45 DEH4O6C PD 1BO7; 1BO8; 1BP0; 1BP6; 1BPJ; 1JMF; 1JMG; 1JMH; 1JMI; 1LCA; 1LCB; 1LCE; 1NJA; 1NJB; 1NJC; 1TDB; 1TDC; 1THY; 1TSL; 1TSM; 1TSV; 1TSW; 1TSX; 1TSY; 1TSZ; 1TVU; 1TVV; 1TVW; 1VZA; 1VZB; 1VZC; 1VZD; 1VZE; 2G86; 2G89; 2G8A; 2G8D; 2TDD; 2TDM; 3BNZ; 3BYX; 3BZ0; 3C06; 3C0A; 3IJZ; 3IK0; 3IK1; 4TMS DEH4O6C SQ MLEQPYLDLAKKVLDEGHFKPDRTHTGTYSIFGHQMRFDLSKGFPLLTTKKVPFGLIKSELLWFLHGDTNIRFLLQHRNHIWDEWAFEKWVKSDEYHGPDMTDFGHRSQKDPEFAAVYHEEMAKFDDRVLHDDAFAAKYGDLGLVYGSQWRAWHTSKGDTIDQLGDVIEQIKTHPYSRRLIVSAWNPEDVPTMALPPCHTLYQFYVNDGKLSLQLYQRSADIFLGVPFNIASYALLTHLVAHECGLEVGEFIHTFGDAHLYVNHLDQIKEQLSRTPRPAPTLQLNPDKHDIFDFDMKDIKLLNYDPYPAIKAPVAV DEH4O6C TD Primarily distributed in human gut. DEH4O6C FC This enzyme catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. DEH4O6C KD 2: Bacteria DEH4O6C PL 1239: Firmicutes DEH4O6C CL 91061: Bacilli DEH4O6C OD 186826: Lactobacillales DEH4O6C FM 33958: Lactobacillaceae DEH4O6C GE 1578: Lactobacillus DEH4O6C SP 1582: Lactobacillus casei DEDI8VX ID DEDI8VX DEDI8VX DN Propanediol dehydrogenase (dhaT) DEDI8VX GN dhaT DEDI8VX SN Dehydrogenase propanediol; 1,3-propanediol dehydrogenase; 13-propanediol dehydrogenase; AZI11_12055; CCS05_11470; CNR29_12615; LbDm2_1760; NCTC13386_00196; UCCLBBS449_2334; dhaT DEDI8VX UC A0A0C1Q6R1_LACBR DEDI8VX RD Glycerol DEDI8VX GI 4413383 DEDI8VX E1 1: Oxidoreductase DEDI8VX E2 1.1: CH-OH donor oxidoreductase DEDI8VX E3 1.1.1: NAD/NADP oxidoreductase DEDI8VX EC 1.1.1.202 DEDI8VX SQ MAERSYDFLMPSVNFFGPGVISKIGDRAKMLGMKKPVIVTDKFLEGLKDGAVEQTLDSLKAAGVDYVVYNNVEPNPKIRNIKEVKKLYEESGADSIITVGGGSAHDTGKGAGIILTNGDDITKLAGIETLDKALPPLIAVNTTAGTGSELTRHAVITNEETHLKFVVVSWRNIPLVSFNDPTLMLDVPKGLTAATGMDAFVQAVEPYVSVDHNPITDSQCVEAIKLIETSLREAVANGHNLDARTKMVEAEMLAGMAFNNANLGYVHAMAHQLGGQYDAPHGVCCALLLPYVEEYNIIACPDRFAQLAEIMGENTEGLSTRDAAELAIKAMKQLSEDVGIPHSIKEIGAKPEDFELMAENALKDGNAFSNPRKGTKEDIIKIFQAAYDAE DEDI8VX TD Primarily distributed in human gut. DEDI8VX FC This enzyme uses NAD+ to oxidize 1,3-propanediol, glycerol, ethanol and 1,2-propanediol. This enzyme required Mn2+ and are probably octamers with a molecular mass of 350 kDa. DEDI8VX KD 2: Bacteria DEDI8VX PL 1239: Firmicutes DEDI8VX CL 91061: Bacilli DEDI8VX OD 186826: Lactobacillales DEDI8VX FM 33958: Lactobacillaceae DEDI8VX GE 1578: Lactobacillus DEDI8VX SP 1580: Lactobacillus brevis DEDI8VX SU Lactobacillus brevis 6239; Lactobacillus brevis B22 DE5LYXF ID DE5LYXF DE5LYXF DN Nitroreductase (NTR) DE5LYXF GN nfrA2_4 DE5LYXF SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; NCTC13020_02816; nfrA2_4 DE5LYXF UC A0A2X3BKF5_CLOSG DE5LYXF RD Nitrofurantoin DE5LYXF E1 1: Oxidoreductase DE5LYXF E2 1.5: CH-NH donor oxidoreductase DE5LYXF E3 1.5.1: NAD/NADP acceptor oxidoreductase DE5LYXF EC 1.5.1.39 DE5LYXF SQ MNAILKRRSIRKYKDKKISDDIVEELLRAGMAAPSAVNEQPWQFIVLRDKETMKKITKVHEYSKMLLEADVAIVVCGDKSKELVDDFWVQDCSAATENILIEAQDKGLGAVWLGVYPIKERVDGIKEILNLPEGITPLSVIPIGYPDEKKEPADRSNKERVHYDKW DE5LYXF TD Primarily distributed in human gut. DE5LYXF FC This enzyme contains FMN and can utilize NADH and NADPH with similar reaction rates. It also reduces riboflavin and FAD, but more slowly. DE5LYXF KD 2: Bacteria DE5LYXF PL 1239: Firmicutes DE5LYXF CL 186801: Clostridia DE5LYXF OD 186802: Clostridiales DE5LYXF FM 31979: Clostridiaceae DE5LYXF GE 1485: Clostridium DE5LYXF SP 1509: Clostridium sporogenes DEH3KAT ID DEH3KAT DEH3KAT DN Methylenetetrahydrofolate reductase (metF) DEH3KAT GN metF DEH3KAT SN Methylene tetrahydrofolate reductase bacterial; AtMTHFR; Bacterial MTHFR; SSA_0417; metF DEH3KAT UC A3CL12_STRSV DEH3KAT RD ISO-901 DEH3KAT GI 4807150 DEH3KAT E1 1: Oxidoreductase DEH3KAT E2 1.5: CH-NH donor oxidoreductase DEH3KAT E3 1.5.1: NAD/NADP acceptor oxidoreductase DEH3KAT EC 1.5.1.20 DEH3KAT KG Carbon metabolism:ssa01200; Metabolic pathways:ssa01100; Microbial metabolism in diverse environments:ssa01120; One carbon pool by folate:ssa00670 DEH3KAT SQ MVRRHTPSLSFEVFPPNPAVGNDKIFQALREMQDLAPHFISVTASNNKFDIEETTVRLTEFIANELQIPTIAHLPAVYLTKDMVSNILQSLDRVGVHQILALRGDIFPDVAPKDDFTYATDLIEYIKTEAPHFDIIGACYPEGHPDSPNQISDIQNLKKKVDAGCSSLVTQLFFDNERFYDFQDKCILAGIEVPIHAGIMPILNRNQALRLLKTCENIKLPRKFRAILDKYEHDPESLRAAGLAYAVDQIVDLVTQDVAGIHLYTMNNAATAYHIYKATHALFNHNPSVQSF DEH3KAT TD Primarily distributed in human oral cavity. DEH3KAT FC This enzyme is a flavoprotein (FAD). And Menadione can also serve as an electron acceptor. DEH3KAT KD 2: Bacteria DEH3KAT PL 1239: Firmicutes DEH3KAT CL 91061: Bacilli DEH3KAT OD 186826: Lactobacillales DEH3KAT FM 1300: Streptococcaceae DEH3KAT GE 1301: Streptococcus DEH3KAT SP 1305: Streptococcus sanguinis DE7NXHG ID DE7NXHG DE7NXHG DN Maltose phosphorylase (malP) DE7NXHG GN malP DE7NXHG SN Glycoside hydrolase 65 protein; Glycoside hydrolase family 65; Glycoside hydrolase family 65 protein; Kojibiose phosphorylase; LBA1870 DE7NXHG UC Q5FI04_LACAC DE7NXHG RD M-7403 DE7NXHG GI 3251782 DE7NXHG E1 2: Transferase DE7NXHG E2 2.4: Glycosyltransferases DE7NXHG E3 2.4.1: Hexosyltransferase DE7NXHG EC 2.4.1.8 DE7NXHG KG Metabolic pathways:lac01100; Starch and sucrose metabolism:lac00500 DE7NXHG SQ MKRIFEIDPWKVITHKFDPKDKRLQESMTAIGNDYMGMRGNFEEGYSGDSLQGTYLAGVWFPDKTVVGWWKNGYPKYFGKTPNAPSFIGIGINVNGEKVDLAKVKFSDFELSLDMHQGLLSRSFIYEGKDVKVKLEFERFLHIVQKEAALIKVKATVLEGHAKIDFDSTLDGTVVNEDSNYGDRFWIPLGEDKDEKTIQVKTKKNPYDVPQFTVLLKEALRNNGVAVNGEVTTEDAKLSERFSVELDEGQSYELEKDVIVVTSRDVEEKDQAAVANNLMSKLQTKSFEDNLADHTEAWKKRWETSDVEISGDDAAQQGIRFNICQLFMTYYGEDKRLNVGPKGFTGEKYGGATYWDTEAFIVPMYLAVTKPSVTRALLQYRHDQLPGAYHNAKEQGLPGALFPMVTFNGIECHNEWEITFEEIHRNADIPHAIAMYTDYTGDDSYVKNEGMDVLVGTARFWAARVHWSKMRNKYVMHGVTGPNEYENNVNNNWFTNTMARWLLKYTLERLPLATKEAQERVRVTDEEKAKWQDIVDNMYLPEDEDLGIFLQQDDFLDKDIRPVTEIEDQRPINQHWSWDKILRSPFIKQADVLQGIYFFDDQYTMDQKEKNFDFYEPLTVHESSLSPCIYSIMAAELGKKEKAVELYQRTARLDLDNYNNDTVDGLHITSMSGSWLAIVQGFAGMRYDHDQLKFNPFVPDGWDHYSFKINYRGRLIEVYVDHDECKITLLSGDDLEVMVHDNKLDLKEGKTKCLKA DE7NXHG TD Primarily distributed in human gut. DE7NXHG FC This enzyme catalyzes the conversion of maltose to D-glucose and beta-D-glucose 1-phosphate. DE7NXHG KD 2: Bacteria DE7NXHG PL 1239: Firmicutes DE7NXHG CL 91061: Bacilli DE7NXHG OD 186826: Lactobacillales DE7NXHG FM 33958: Lactobacillaceae DE7NXHG GE 1578: Lactobacillus DE7NXHG SP 1579: Lactobacillus acidophilus DEFVHQU ID DEFVHQU DEFVHQU DN Glycerol-3-phosphate dehydrogenase (gpsA) DEFVHQU GN gpsA DEFVHQU SN Dihydroxyacetone-phosphate reductase; GPD-C; GPDH-C; gpsA DEFVHQU UC A0A411LCN0_ERYRH DEFVHQU RD Chloramphenicol DEFVHQU E1 1: Oxidoreductase DEFVHQU E2 1.1: CH-OH donor oxidoreductase DEFVHQU E3 1.1.1: NAD/NADP oxidoreductase DEFVHQU EC 1.1.1.94 DEFVHQU SQ GHEVMMWGRKLDQVVDVHLYHLNEEFFPGVKLNERLDATQNFEDILDSQIILLAVPTGAVEEVCIELNAHLSNPVIIINVAKGLHPTTHELLDHVIKRVIDSNKLKGVVSLIGPSHAEEVVLRKITTINAVSDNPALAEEVQVLFSNDYFRVYTNDDVIGSQYGVAIKNVIALASGIAAGLDAGDNARAALITRGLTEMQRFGVHMGGQPETYLGLCGVGDLVVTATSVHSRNFQAGMEIGQKNSAVGFLDHNTKTVEGVFAAKVVYEIAVEEGIDMPITEQIYKIIYEEKR DEFVHQU TD Primarily distributed in human gut. DEFVHQU FC This enzyme shows specificity for the B side of NADPH. DEFVHQU KD 2: Bacteria DEFVHQU PL 1239: Firmicutes DEFVHQU CL 526524: Erysipelotrichia DEFVHQU OD 526525: Erysipelotrichales DEFVHQU FM 128827: Erysipelotrichaceae DEFVHQU GE 1647: Erysipelothrix DEFVHQU SP 1648: Erysipelothrix rhusiopathiae DEMUBWL ID DEMUBWL DEMUBWL DN Chloramphenicolase (chlR) DEMUBWL GN chlR DEMUBWL SN Chloramphenicol reductase; Enzyme chloramphenicolase; Reductase chloramphenicol DEMUBWL UC A0A5M4B0P0_9BACT DEMUBWL RD Chloramphenicol DEMUBWL E1 2: Transferase DEMUBWL E2 2.3: Acyltransferase DEMUBWL E3 2.3.1: Acyltransferase DEMUBWL EC 2.3.1.28 DEMUBWL SQ MKKIDLNSWNRREHFAFFSQFDEPFFSIVAEVDCTVAYRKAKEQDIPFFIWYLYQSLLAANQVEPFRYRIIDNEVVVLDEIHASSTVAREDHTFGFTFMPYREDIKAFVAEALPEIERVQQLEGLCFDEKTSRTDVIHYSSIPWINFTALTHARHNARKDSVPKISFGQYQEKEGKLMMPVSVTVHHGLMDGYHVGLFLTKFQKLLES DEMUBWL TD Primarily distributed in human gut. DEMUBWL FC This enzyme catalyzes the hydrolysis of the amide bond in chloramphenicol. DEMUBWL KD 2: Bacteria DEMUBWL PL 1239: Firmicutes DEMUBWL CL 91061: Bacilli DEMUBWL OD 1385: Bacillales DEMUBWL FM 186817: Bacillaceae DEMUBWL GE 1386: Bacillus DEMUBWL SP 1408: Bacillus pumilus DECMT89 ID DECMT89 DECMT89 DN Chloramphenicolase (chlR) DECMT89 GN chlR DECMT89 SN Chloramphenicol reductase; Enzyme chloramphenicolase; Reductase chloramphenicol DECMT89 UC A0A5M4B0P0_9BACT DECMT89 RD Chloramphenicol DECMT89 E1 2: Transferase DECMT89 E2 2.3: Acyltransferase DECMT89 E3 2.3.1: Acyltransferase DECMT89 EC 2.3.1.28 DECMT89 SQ MKKIDLNSWNRREHFAFFSQFDEPFFSIVAEVDCTVAYRKAKEQDIPFFIWYLYQSLLAANQVEPFRYRIIDNEVVVLDEIHASSTVAREDHTFGFTFMPYREDIKAFVAEALPEIERVQQLEGLCFDEKTSRTDVIHYSSIPWINFTALTHARHNARKDSVPKISFGQYQEKEGKLMMPVSVTVHHGLMDGYHVGLFLTKFQKLLES DECMT89 TD Primarily distributed in human gut. DECMT89 FC This enzyme catalyzes the hydrolysis of the amide bond in chloramphenicol. DECMT89 KD 2: Bacteria DECMT89 PL 1224: Proteobacteria DECMT89 CL 1236: Gammaproteobacteria DECMT89 OD 91347: Enterobacterales DECMT89 FM 1903414: Morganellaceae DECMT89 GE 583: Proteus DECMT89 SP 102862: Proteus penneri DERDXAF ID DERDXAF DERDXAF DN Cellobiose 2-epimerase (CE) DERDXAF GN ce-ne1 DERDXAF SN Cellobiose epimerase; CS-HRCE; Caob-CE; B15CE; BfCE; CE; CE-NE1; CsCE; ce-ne1 DERDXAF UC CEEP_RUMAL DERDXAF RD M-7403 DERDXAF E1 5: Isomerase DERDXAF E2 5.1: Racemase/epimerase DERDXAF E3 5.1.3: Carbohydrate racemase/epimerase DERDXAF EC 5.1.3.11 DERDXAF PD 3VW5 DERDXAF SQ MMISEIRQELTDHIIPFWNKLRDDENGGFYGYLSYGLGLDKKADKGVILHSRILWFYSNAYMTLGGDELLDNAKHAYEFIKNNCIDYEYGGVYWMMDFEGKPADTMKHTYNIAFAIYALSSYYRASGDKEALALAYRPFEDIEKNTLYEYGYREAFDRQWRLVDNEALSENGLKADKTMNAILHLIEAYTELYKADGNEKVADRLKFQLGQMRDIVYTPDTNALKVFFDTAFNLVGDIHSYGHDIEATWLMDRACDVLGDEDLKKQFAEMDLKISHNIQDIALEDGALNNERDKNEIDKTRVWWVQAEAVVGFINAYQHSGDEKFLESAKSVWENIKEYIIDKREGGEWYSEVTFDHTPHDYKETVGPWKCPYHNGRMCMEVITRGVDI DERDXAF TD Primarily distributed in human gut. DERDXAF FC This enzyme catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). It can also epimerizes cellotriose to Glc-Glc-Man, cellotetraose to Glc-Glc-Glc-Man, and lactose to epilactose. DERDXAF KD 2: Bacteria DERDXAF PL 1239: Firmicutes DERDXAF CL 186801: Clostridia DERDXAF OD 186802: Clostridiales DERDXAF FM 541000: Ruminococcaceae DERDXAF GE 1263: Ruminococcus DERDXAF SP 1264: Ruminococcus albus DEC3G7M ID DEC3G7M DEC3G7M DN Beta-lactamase (blaB) DEC3G7M GN blaFRI-4 DEC3G7M SN Penicillinase; Cephalosporinase; Beta-lactam; blaFRI-4 DEC3G7M UC A0A1S7IV31_ENTAS DEC3G7M RD Doripenem DEC3G7M E1 3: Hydrolases DEC3G7M E2 3.5: Carbon-nitrogen hydrolase DEC3G7M E3 3.5.2: Cyclic amide hydrolase DEC3G7M EC 3.5.2.6 DEC3G7M SQ MFFFKKSASTFIFLLCLPLNSFASQESNGVEQMRELETSFGGRIGVYILNTKNGKEFSYRQDERFPLCSSFKAFLAASVLKRTQDKSVSLDDMMEYSGRVMEKHSPVSEKYRETGASVQTLAKAAIQYSDNGASNLLMERYIGGPEGLTAFMRSTGDTDFRLDRWELELNSAIPGDERDTSTPKAVAISLNNIAFGSVLDAKNKSLLQDWLKGNTTGNARIRAAVPDKWVVGDKTGTCGLYGTANDIAILWPDANSPAVMAVYTTRPNQNDKHDETVIKNAAKIAINAVYGSTK DEC3G7M TD Primarily distributed in human gut. DEC3G7M FC This enzyme hydrolyzes beta-lactam. DEC3G7M KD 2: Bacteria DEC3G7M PL 1224: Proteobacteria DEC3G7M CL 1236: Gammaproteobacteria DEC3G7M OD 91347: Enterobacterales DEC3G7M FM 543: Enterobacteriaceae DEC3G7M GE 547: Enterobacter DEC3G7M SP 550: Enterobacter cloacae DEV0KWQ ID DEV0KWQ DEV0KWQ DN Beta-lactamase (blaB) DEV0KWQ GN cfxa2 DEV0KWQ SN Penicillinase; Cephalosporinase; Beta-lactam; cfxa2 DEV0KWQ UC Q8KT52_9BACT DEV0KWQ RD Penicillin G DEV0KWQ E1 3: Hydrolases DEV0KWQ E2 3.5: Carbon-nitrogen hydrolase DEV0KWQ E3 3.5.2: Cyclic amide hydrolase DEV0KWQ EC 3.5.2.6 DEV0KWQ SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTFKECKTGVDRIAAPLLDKEGVVIAHKTGSGDVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEV0KWQ TD Primarily distributed in human gut. DEV0KWQ FC This enzyme hydrolyzes beta-lactam. DEV0KWQ KD 2: Bacteria DEV0KWQ PL 976: Bacteroidetes DEV0KWQ CL 200643: Bacteroidia DEV0KWQ OD 171549: Bacteroidales DEV0KWQ FM 171552: Prevotellaceae DEV0KWQ GE 838: Prevotella DEV0KWQ SP 28132: Prevotella melaninogenica DEACNTL ID DEACNTL DEACNTL DN Beta-lactamase (blaB) DEACNTL GN blaOXA-10 DEACNTL SN Penicillinase; Cephalosporinase; Beta-lactam; blaOXA-10 DEACNTL UC Q2F4C6_SHISO DEACNTL RD Amoxicillin DEACNTL GI 39724635 DEACNTL E1 3: Hydrolases DEACNTL E2 3.5: Carbon-nitrogen hydrolase DEACNTL E3 3.5.2: Cyclic amide hydrolase DEACNTL EC 3.5.2.6 DEACNTL SQ MKTFAAYVIIACLSSTALAGSITENTSWNKEFSAEAVNGVFVLCKSSSKSCATNDLARASKEYLPASTFKIPNAIIGLETGVIKNEHQVFKWDGKPRAMKQWERDLTLRGAIQVSAVPVFQQIAREVGEVRMQKYLKKFSYGNQNISGGIDKFWLEGQLRISAVNQVEFLESLYLNKLSASKENQLIVKEALVTEAAPEYLVHSKTGFSGVGTESNPGVAWWVGWVEKETEVYFFAFNMDIDNESKLPLRKSIPTKIMESEGIIGG DEACNTL TD Primarily distributed in human gut. DEACNTL FC This enzyme hydrolyzes beta-lactam. DEACNTL KD 2: Bacteria DEACNTL PL 1224: Proteobacteria DEACNTL CL 1236: Gammaproteobacteria DEACNTL OD 91347: Enterobacterales DEACNTL FM 543: Enterobacteriaceae DEACNTL GE 620: Shigella DEACNTL SP 624: Shigella sonnei DETQXR5 ID DETQXR5 DETQXR5 DN Beta-glucosidase (bglA) DETQXR5 GN bglA DETQXR5 SN Periplasmic beta-glucosidase; Glucan endo-1 3-beta-D-glucosidase; Beta-D-glucosidase; TERG_00481 DETQXR5 UC F2SBM1_TRIRC DETQXR5 RD Esculin DETQXR5 GI 10373795 DETQXR5 E1 3: Hydrolases DETQXR5 E2 3.2: Glycosylase DETQXR5 E3 3.2.1: O/S-glycosyl compound glycosidase DETQXR5 EC 3.2.1.21 DETQXR5 SQ MLFRWCPLVALAIASGTAATESWESPPYYPSPWTKGEGEWEAAYQKAVSFVSQLTLAEKVNLTTGVGWMQESCVGQVGSIPRLGFRSLCMQDGPLGIRFGDYVTAFPAGINVAATWSRELAYLRGKAMGEEFRGKGADVILGPAIGPIGRAPEGGRNWEGLGPDPVLAGKLVAETIKGMQKSGVIACAKHFIANEQERFRIAAEAQGYGFDIAESISSNVDDVTMHEIYLWPFADAVKAGVGSIMCSYNQINNSYGCGNSYTQNKLLKGELGFRGFIMSDWQAHHSGVGSAFAGLDMSMPGDTLFGTGVSYWGANLTIAVANGTIPEWRVDDMAVRIMAAYYKVGRDQVQVPINFNSWTTDVEGYQHALVKEGYGVVNQRVNVRDHHAQIARRVARDSTVLLKNEGVLPLTGTEQFTAIIGEDAGPNINGPNSCPDRGCDNGTLAMGWGSGTTNFPYLVTPDDAIQREIVGKGVGNVMSVLQNGDFKNIQSVAGQADVALVFINSDSGEGYISVDGNEGDRKNLTTWKGGDEMVKQVTSVCNNTVLVIHSSGPILAGEWHDNPNITAILWAGLPGQESGNALVDILYGKENPGGKSPFTWARTAEDYGTTILREPNNGKGAPQHLFSEGIMFEYRHFDQKNITPVYEFGYGLSYTTFSYSNLKVRPMRANKYVPATGMTKPAPRLGHSSTKYADYLFPGGFKGVTKYVYSWLTSTDPKEASGDKNYGMPLEDYVPPNANNGDAQPVLPASGVPGGNPGLFEDLYEVSAVITNDGDRVGEEVPQLYISLGGDRNAKVVLRGFDRIRLAPHQRFRWRTTITRRDVSNWDPASQDWVMTENPKIVYVGSSSRNLPLQAPLPAPNLA DETQXR5 TD Primarily distributed in human skin. DETQXR5 FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DETQXR5 KD 4751: Fungi DETQXR5 PL 4890: Ascomycota DETQXR5 CL 147545: Eurotiomycetes DETQXR5 OD 33183: Onygenales DETQXR5 FM 34384: Arthrodermataceae DETQXR5 GE 5550: Trichophyton DETQXR5 SP 5551: Trichophyton rubrum DETQXR5 SU Trichophyton rubrum NCPF 0118 DE5CAX1 ID DE5CAX1 DE5CAX1 DN Azoreductase (azoR) DE5CAX1 GN azr_2 DE5CAX1 SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; Flavin reductase; NAD(P)H-dependent oxidoreductase; NADPH azoreductase; azoR; A6J87_06095; CKU37_01320; CQA85_07565; D8867_01950; DL07_01170; DWV94_10025; DWY30_01550; DWZ07_06240; FBF48_06605; NCTC8618_04344; azr_2; azr_4 DE5CAX1 UC A0A074IU04_STRSL DE5CAX1 RD Sulfasalazine DE5CAX1 GI 29398535 DE5CAX1 E1 1: Oxidoreductase DE5CAX1 E2 1.7: Cytochrome acceptor oxidoreductase DE5CAX1 E3 1.7.1: NAD/NADP acceptor oxidoreductase DE5CAX1 EC 1.7.1.6 DE5CAX1 SQ MKFVGLVGANYDQSYNRKLLEFIRRHFKIKFELEVLEIDEVPMFNQDEKWDESFQLRLLNNKITRADGVIIATPEHNHTISAALKSVLEWLSFEVHPFENKPVMIVGASYYDQGTSRAQVHLRKILEAPGVNAYTLPGNEFLLGKAKEAFDLEGNITNEGTINFLEQCLDNFIQYVGVVSKLKKPKPIEPEDLDCNNPIATTVTEVDPDDPEWVEKVAEITGAVSGDTYVKLDHGILTVNQIDMFLKAMPFELTYADDNNQFLYYNNAHQDPDTMFAKRVPPQSGSRMSTVHGSLPPARMKNVEWVIGTLRNGNQEYVRTIVPGSPEGVINTHNYQAMYYDDGSYAGINEIVFNFKPWLDWYLETTGQRLVGGSGPFAPAAASHGGSDATSGASDAGGHGGDAAPAADATSGASSY DE5CAX1 TD Primarily distributed in human gut. DE5CAX1 FC This enzyme can reduce other azo dyes, such as Methyl Red, Rocceline, Solar Orange and Sumifix Black B. DE5CAX1 KD 2: Bacteria DE5CAX1 PL 1239: Firmicutes DE5CAX1 CL 91061: Bacilli DE5CAX1 OD 186826: Lactobacillales DE5CAX1 FM 1300: Streptococcaceae DE5CAX1 GE 1301: Streptococcus DE5CAX1 SP 1304: Streptococcus salivarius DE5CAX1 SU Streptococcus salivarius K12 DEGTKHL ID DEGTKHL DEGTKHL DN Azoreductase (azoR) DEGTKHL GN azoR DEGTKHL SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; HSIEG1_1039 DEGTKHL UC T0VG26_9ENTE DEGTKHL RD Sulfasalazine DEGTKHL E1 1: Oxidoreductase DEGTKHL E2 1.7: Cytochrome acceptor oxidoreductase DEGTKHL E3 1.7.1: NAD/NADP acceptor oxidoreductase DEGTKHL EC 1.7.1.6 DEGTKHL SQ MKNVLVVKANNRPDGVSAKMFDTFVENLDRTAVDVVTFDVYAQPMPYIGQTLFEAFGKLAQEQDLNQEEQELMTVRQDVMNKFAAADTIVFAFPMWNLTIPAALHTFIDYIFQAGFTFSYNEDGSMNQLLKDKEVVLLNARGGVYSGEMSGMESAVTFMEKVFGGMFGMTISDEVIIEGHNADPSKTEEIIAAGLEKVAEAAKKF DEGTKHL TD Primarily distributed in human gut. DEGTKHL FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. And it requires NADH, but not NADPH, as an electron donor for its activity. DEGTKHL KD 2: Bacteria DEGTKHL PL 1239: Firmicutes DEGTKHL CL 91061: Bacilli DEGTKHL OD 186826: Lactobacillales DEGTKHL FM 81852: Enterococcaceae DEGTKHL GE 1350: Enterococcus DEGTKHL SP 37734: Enterococcus casseliflavus DEI2PC5 ID DEI2PC5 DEI2PC5 DN Azoreductase (azoR) DEI2PC5 GN azoR DEI2PC5 SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; CPF_0793 DEI2PC5 UC AZOR_CLOP1 DEI2PC5 RD Sulfasalazine DEI2PC5 GI 29572085 DEI2PC5 E1 1: Oxidoreductase DEI2PC5 E2 1.7: Cytochrome acceptor oxidoreductase DEI2PC5 E3 1.7.1: NAD/NADP acceptor oxidoreductase DEI2PC5 EC 1.7.1.6 DEI2PC5 SQ MSKVLYIKANIKNEGESRTFKVSDSFVEEYKKNNPEDEIITLDLYKENIDFLRADDLGKLFGPKDEESKNNSILKYAYQFADADKYIIAAPMWNLSFPAILKAYIDYVSVSGITFKYTAEGPVGLLNNKKAVHIVSRGGGYDNSPYEMGDRYLRTILGFFGIKDIETIAIDNLDVMGVNVEEKVEEGIEKAISLAKKF DEI2PC5 TD Primarily distributed in human gut. DEI2PC5 FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. And it requires NADH, but not NADPH, as an electron donor for its activity. DEI2PC5 KD 2: Bacteria DEI2PC5 PL 1239: Firmicutes DEI2PC5 CL 186801: Clostridia DEI2PC5 OD 186802: Clostridiales DEI2PC5 FM 31979: Clostridiaceae DEI2PC5 GE 1485: Clostridium DEI2PC5 SP 1502: Clostridium perfringens DEIHK8V ID DEIHK8V DEIHK8V DN Azoreductase (azoR) DEIHK8V GN azoR DEIHK8V SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; DCW31_09905 DEIHK8V UC A0A349MYB4_9LACO DEIHK8V RD Sulfasalazine DEIHK8V E1 1: Oxidoreductase DEIHK8V E2 1.7: Cytochrome acceptor oxidoreductase DEIHK8V E3 1.7.1: NAD/NADP acceptor oxidoreductase DEIHK8V EC 1.7.1.6 DEIHK8V SQ MAKILVIKAHPLTIEHSRTLKILDAFMTQYKVSNPEDTIETRDLYAEEFPDIDRSMMTAWGQLQNGVGFPDLTTQQQQQLSAYDSTTQQYIDADKVILANPMWNLSIPAKLQAWIDTICVAGKTFQYTETAEIPLVPGKKVLHIQTAGGFYDGKDFGAKYISGIMHFLGASDVQELAVEGMDHFPEKAEAFMQDGLERATALATKF DEIHK8V TD Primarily distributed in human gut. DEIHK8V FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. DEIHK8V KD 2: Bacteria DEIHK8V PL 1239: Firmicutes DEIHK8V CL 91061: Bacilli DEIHK8V OD 186826: Lactobacillales DEIHK8V FM 33958: Lactobacillaceae DEIHK8V GE 1578: Lactobacillus DEIHK8V SP 1579: Lactobacillus acidophilus DEIHK8V SU Lactobacillus acidophilus L10 DEUP4DA ID DEUP4DA DEUP4DA DN Thioredoxin reductase TR1 (TXNRD1) DEUP4DA GN TXNRD1 DEUP4DA SN Cytoplasmic thioredoxin reductase 1; KM-102-derived reductase-like factor; Gene associated with retinoic and IFN-induced mortality 12 protein; Gene associated with retinoic and interferon-induced mortality 12 protein; GRIM-12; GRIM12; KDRF; TR; TXNRD1 DEUP4DA UC TRXR1_HUMAN DEUP4DA RD Selenium DEUP4DA GI 7296 DEUP4DA E1 1: Oxidoreductase DEUP4DA E2 1.8: Sulfur donor oxidoreductase DEUP4DA E3 1.8.1: NAD/NADP acceptor oxidoreductase DEUP4DA EC 1.8.1.9 DEUP4DA RC Detoxification of Reactive Oxygen Species:R-HSA-3299685; Interconversion of nucleotide di- and triphosphates:R-HSA-499943; Metabolism of ingested H2SeO4 and H2SeO3 into H2Se:R-HSA-2408550; Metabolism of ingested MeSeO2H into MeSeH:R-HSA-5263617; PPARA activates gene expression:R-HSA-1989781; TP53 Regulates Metabolic Genes:R-HSA-5628897; Uptake and function of diphtheria toxin:R-HSA-5336415 DEUP4DA KG Hepatocellular carcinoma:hsa05225; Pathways in cancer:hsa05200; Selenocompound metabolism:hsa00450 DEUP4DA PD 1W1C; 2CFY; 2J3N; 2ZZ0; 2ZZB; 2ZZC; 3QFA; 3QFB DEUP4DA SQ MGCAEGKAVAAAAPTELQTKGKNGDGRRRSAKDHHPGKTLPENPAGFTSTATADSRALLQAYIDGHSVVIFSRSTCTRCTEVKKLFKSLCVPYFVLELDQTEDGRALEGTLSELAAETDLPVVFVKQRKIGGHGPTLKAYQEGRLQKLLKMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSGASILQAGCUG DEUP4DA TD Primarily distributed in ovary, spleen, heart, liver, kidney and pancreas. DEUP4DA FC This enzyme possesses glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. DEUP4DA KD 33208: Metazoa DEUP4DA PL 7711: Chordata DEUP4DA CL 40674: Mammalia DEUP4DA OD 9443: Primates DEUP4DA FM 9604: Hominidae DEUP4DA GE 9605: Homo DEUP4DA SP 9606: Homo sapiens DEGDPL2 ID DEGDPL2 DEGDPL2 DN Glutathione reductase (GSR) DEGDPL2 GN GSR DEGDPL2 SN Mitochondrial glutathione reductase; GLUR; GR; GRD1; GRase; GSR DEGDPL2 UC GSHR_HUMAN DEGDPL2 RD Selenium DEGDPL2 GI 2936 DEGDPL2 E1 1: Oxidoreductase DEGDPL2 E2 1.8: Sulfur donor oxidoreductase DEGDPL2 E3 1.8.1: NAD/NADP acceptor oxidoreductase DEGDPL2 EC 1.8.1.7 DEGDPL2 RC Detoxification of Reactive Oxygen Species:R-HSA-3299685; Interconversion of nucleotide di- and triphosphates [P00390-2]:R-HSA-499943; Metabolism of ingested H2SeO4 and H2SeO3 into H2Se [P00390-2]:R-HSA-2408550; TP53 Regulates Metabolic Genes [P00390-2]:R-HSA-5628897 DEGDPL2 KG Glutathione metabolism:hsa00480; Metabolic pathways:hsa01100; Thyroid hormone synthesis:hsa04918 DEGDPL2 PD 1DNC; 1GRA; 1GRB; 1GRE; 1GRF; 1GRG; 1GRH; 1GRT; 1GSN DEGDPL2 SQ MALLPRALSAGAGPSWRRAARAFRGFLLLLPEPAALTRALSRAMACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR DEGDPL2 TD Low tissue/organ specificity. DEGDPL2 FC This enzyme catalyzes the reduction of glutathione disulfide (GSSG) to the sulfhydryl form glutathione (GSH), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell. DEGDPL2 KD 33208: Metazoa DEGDPL2 PL 7711: Chordata DEGDPL2 CL 40674: Mammalia DEGDPL2 OD 9443: Primates DEGDPL2 FM 9604: Hominidae DEGDPL2 GE 9605: Homo DEGDPL2 SP 9606: Homo sapiens DER3H9C ID DER3H9C DER3H9C DN Lipocalin-type prostaglandin-D synthase (PTGDS) DER3H9C GN PTGDS DER3H9C SN Glutathione-independent PGD synthase; Prostaglandin-D2 synthase; PGD2 synthase; Prostaglandin-H2 D-isomerase; Beta-trace protein; Cerebrin-28; PDS; PGDS; PGDS2; PTGDS DER3H9C UC PTGDS_HUMAN DER3H9C RD NSC-6292 DER3H9C GI 5730 DER3H9C E1 5: Isomerase DER3H9C E2 5.3: Intramolecular oxidoreductase DER3H9C E3 5.3.99: Intramolecular oxidoreductase DER3H9C EC 5.3.99.2 DER3H9C RC Synthesis of Prostaglandins (PG) and Thromboxanes (TX):R-HSA-2162123 DER3H9C KG Arachidonic acid metabolism:hsa00590; Metabolic pathways:hsa01100 DER3H9C PD 3O22; 3O2Y; 4IMN; 4IMO; 4ORR; 4ORS; 4ORU; 4ORW; 4ORX DER3H9C SQ MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELKEKFTAFCKAQGFTEDTIVFLPQTDKCMTEQ DER3H9C TD Primarily distributed in brain, CNS, heart muscle and retina. DER3H9C FC This enzyme catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. It binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules. DER3H9C KD 33208: Metazoa DER3H9C PL 7711: Chordata DER3H9C CL 40674: Mammalia DER3H9C OD 9443: Primates DER3H9C FM 9604: Hominidae DER3H9C GE 9605: Homo DER3H9C SP 9606: Homo sapiens DE1Z0MO ID DE1Z0MO DE1Z0MO DN Carbonic anhydrase II (CA2) DE1Z0MO GN CA2 DE1Z0MO SN Carbonate dehydratase II; Carbonic anhydrase 2; Carbonic anhydrase C; CA-II; CA2; CAC DE1Z0MO UC CAH2_HUMAN DE1Z0MO RD Nitrophenyl acetate DE1Z0MO GI 760 DE1Z0MO E1 4: Lyases DE1Z0MO E2 4.2: Carbon-oxygen lyase DE1Z0MO E3 4.2.1: Hydro-lyase DE1Z0MO EC 4.2.1.1 DE1Z0MO RC Erythrocytes take up carbon dioxide and release oxygen:R-HSA-1237044; Erythrocytes take up oxygen and release carbon dioxide:R-HSA-1247673; Reversible hydration of carbon dioxide:R-HSA-1475029 DE1Z0MO KG Bile secretion:hsa04976; Collecting duct acid secretion:hsa04966; Gastric acid secretion:hsa04971; Metabolic pathways:hsa01100; Nitrogen metabolism:hsa00910; Pancreatic secretion:hsa04972; Proximal tubule bicarbonate reclamation:hsa04964 DE1Z0MO PD 1AM6; 1AVN; 1BCD; 1BIC; 1BN1; 1BN3; 1BN4; 1BNM; 1BNN DE1Z0MO SQ MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK DE1Z0MO TD Primarily distributed in intestine and stomach. DE1Z0MO FC This enzyme can hydrate cyanamide to urea. DE1Z0MO KD 33208: Metazoa DE1Z0MO PL 7711: Chordata DE1Z0MO CL 40674: Mammalia DE1Z0MO OD 9443: Primates DE1Z0MO FM 9604: Hominidae DE1Z0MO GE 9605: Homo DE1Z0MO SP 9606: Homo sapiens DEPLH5Z ID DEPLH5Z DEPLH5Z DN Phosphoenolpyruvate carboxykinase (PCK1) DEPLH5Z GN PCK1 DEPLH5Z SN Phosphoenolpyruvate carboxykinase [GTP]; Cytosolic phosphoenolpyruvate carboxykinase [GTP]; PCK1; PEPCK-C; PEPCK1 DEPLH5Z UC PCKGC_HUMAN DEPLH5Z RD Oxaloacetate DEPLH5Z GI 5105 DEPLH5Z E1 4: Lyases DEPLH5Z E2 4.1: Carbon-carbon lyase DEPLH5Z E3 4.1.1: Carboxy-lyase DEPLH5Z EC 4.1.1.32 DEPLH5Z RC Abacavir metabolism:R-HSA-2161541; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes:R-HSA-9615017; Gluconeogenesis:R-HSA-70263; NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis:R-HSA-9632974; Transcriptional regulation of white adipocyte differentiation:R-HSA-381340 DEPLH5Z KG AMPK signaling pathway:hsa04152; Adipocytokine signaling pathway:hsa04920; Citrate cycle (TCA cycle):hsa00020; FoxO signaling pathway:hsa04068; Glucagon signaling pathway:hsa04922; Glycolysis / Gluconeogenesis:hsa00010; Insulin resistance:hsa04931; Insulin signaling pathway:hsa04910; Metabolic pathways:hsa01100; PI3K-Akt signaling pathway:hsa04151; PPAR signaling pathway:hsa03320; Proximal tubule bicarbonate reclamation:hsa04964; Pyruvate metabolism:hsa00620 DEPLH5Z PD 1KHB; 1KHE; 1KHF; 1KHG; 1M51; 1NHX; 2GMV DEPLH5Z SQ MPPQLQNGLNLSAKVVQGSLDSLPQAVREFLENNAELCQPDHIHICDGSEEENGRLLGQMEEEGILRRLKKYDNCWLALTDPRDVARIESKTVIVTQEQRDTVPIPKTGLSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGTPVLEAVGDGEFVKCLHSVGCPLPLQKPLVNNWPCNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGITNPEGEKKYLAAAFPSACGKTNLAMMNPSLPGWKVECVGDDIAWMKFDAQGHLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLASGVTITSWKNKEWSSEDGEPCAHPNSRFCTPASQCPIIDAAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPFAMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKEGKFLWPGFGENSRVLEWMFNRIDGKASTKLTPIGYIPKEDALNLKGLGHINMMELFSISKEFWEKEVEDIEKYLEDQVNADLPCEIEREILALKQRISQM DEPLH5Z TD Primarily distributed in liver kidney and adipocytes. DEPLH5Z FC This enzyme catalyzes the cataplerotic conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle and it also catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate. DEPLH5Z KD 33208: Metazoa DEPLH5Z PL 7711: Chordata DEPLH5Z CL 40674: Mammalia DEPLH5Z OD 9443: Primates DEPLH5Z FM 9604: Hominidae DEPLH5Z GE 9605: Homo DEPLH5Z SP 9606: Homo sapiens DEGF70S ID DEGF70S DEGF70S DN Cyclic ADP-ribose hydrolase 1 (CD38) DEGF70S GN CD38 DEGF70S SN ADP-ribosyl cyclase 1; ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1; 2'-phospho-ADP-ribosyl cyclase; 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase; 2'-phospho-cyclic-ADP-ribose transferase; ADPRC 1; CD38; T10; cADPr hydrolase 1 DEGF70S UC CD38_HUMAN DEGF70S RD FT-0654944 DEGF70S GI 952 DEGF70S E1 3: Hydrolases DEGF70S E2 3.2: Glycosylase DEGF70S E3 3.2.2: N-Glycosyl compound glycosidase DEGF70S EC 3.2.2.6 DEGF70S RC Nicotinate metabolism:R-HSA-196807 DEGF70S KG Calcium signaling pathway:hsa04020; Hematopoietic cell lineage:hsa04640; Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760; Oxytocin signaling pathway:hsa04921; Pancreatic secretion:hsa04972; Salivary secretion:hsa04970 DEGF70S PD 2EF1; 2HCT; 2I65; 2I66; 2I67; 2O3Q; 2O3R; 2O3S; 2O3T DEGF70S SQ MANCEFSPVSGDKPCCRLSRRAQLCLGVSILVLILVVVLAVVVPRWRQQWSGPGTTKRFPETVLARCVKYTEIHPEMRHVDCQSVWDAFKGAFISKHPCNITEEDYQPLMKLGTQTVPCNKILLWSRIKDLAHQFTQVQRDMFTLEDTLLGYLADDLTWCGEFNTSKINYQSCPDWRKDCSNNPVSVFWKTVSRRFAEAACDVVHVMLNGSRSKIFDKNSTFGSVEVHNLQPEKVQTLEAWVIHGGREDSRDLCQDPTIKELESIISKRNIQFSCKNIYRPDKFLQCVKNPEDSSCTSEI DEGF70S TD Primarily distributed in lymphoid tissue and seminal vesicle. DEGF70S FC This enzyme has cADPr hydrolase activity. DEGF70S KD 33208: Metazoa DEGF70S PL 7711: Chordata DEGF70S CL 40674: Mammalia DEGF70S OD 9443: Primates DEGF70S FM 9604: Hominidae DEGF70S GE 9605: Homo DEGF70S SP 9606: Homo sapiens DEG3S8C ID DEG3S8C DEG3S8C DN Cathepsin K (CTSK) DEG3S8C GN CTSK DEG3S8C SN Cathepsin O; Cathepsin O2; Cathepsin X; CTSK; CTSO; CTSO2 DEG3S8C UC CATK_HUMAN DEG3S8C RD BRS-640 DEG3S8C GI 1513 DEG3S8C E1 3: Hydrolases DEG3S8C E2 3.4: Peptidase DEG3S8C E3 3.4.22: Cysteine protease DEG3S8C EC 3.4.22.38 DEG3S8C RC Activation of Matrix Metalloproteinases:R-HSA-1592389; Collagen degradation:R-HSA-1442490; Degradation of the extracellular matrix:R-HSA-1474228; MHC class II antigen presentation:R-HSA-2132295; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes:R-HSA-8939242; Trafficking and processing of endosomal TLR:R-HSA-1679131 DEG3S8C KG Apoptosis:hsa04210; Lysosome:hsa04142; Osteoclast differentiation:hsa04380; Rheumatoid arthritis:hsa05323; Toll-like receptor signaling pathway:hsa04620 DEG3S8C PD 1AU2; 1AU3; 1AU4; 1AYU; 1AYV; 1AYW; 1BGO; 1BY8; 1MEM DEG3S8C SQ MWGLKVLLLPVVSFALYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGRAPDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM DEG3S8C TD Primarily distributed in adipose and osteoclasts. DEG3S8C FC This enzyme displays potent endoprotease activity against fibrinogen at acid pH and may play an important role in extracellular matrix degradation. DEG3S8C KD 33208: Metazoa DEG3S8C PL 7711: Chordata DEG3S8C CL 40674: Mammalia DEG3S8C OD 9443: Primates DEG3S8C FM 9604: Hominidae DEG3S8C GE 9605: Homo DEG3S8C SP 9606: Homo sapiens DE0LW4X ID DE0LW4X DE0LW4X DN Matrix metalloproteinase-2 (MMP-2) DE0LW4X GN MMP2 DE0LW4X SN Gelatinase A; 72 kDa gelatinase; 72 kDa type IV collagenase; CLG4A; MMP-2; MMP2; PEX; TBE-1 DE0LW4X UC MMP2_HUMAN DE0LW4X RD Amylin DE0LW4X GI 4313 DE0LW4X E1 3: Hydrolases DE0LW4X E2 3.4: Peptidase DE0LW4X E3 3.4.24: Metallopeptidase DE0LW4X EC 3.4.24.24 DE0LW4X RC Activation of Matrix Metalloproteinases:R-HSA-1592389; Collagen degradation:R-HSA-1442490; Degradation of the extracellular matrix:R-HSA-1474228; EPH-ephrin mediated repulsion of cells:R-HSA-3928665; Extra-nuclear estrogen signaling:R-HSA-9009391; Interleukin-4 and Interleukin-13 signaling:R-HSA-6785807; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs):R-HSA-381426 DE0LW4X KG AGE-RAGE signaling pathway in diabetic complications:hsa04933; Bladder cancer:hsa05219; Endocrine resistance:hsa01522; Estrogen signaling pathway:hsa04915; Fluid shear stress and atherosclerosis:hsa05418; GnRH signaling pathway:hsa04912; Leukocyte transendothelial migration:hsa04670; Pathways in cancer:hsa05200; Proteoglycans in cancer:hsa05205; Relaxin signaling pathway:hsa04926 DE0LW4X PD 1EAK; 1GEN; 1GXD; 1HOV; 1J7M; 1KS0; 1QIB; 1RTG; 3AYU DE0LW4X SQ MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC DE0LW4X TD Low tissue/organ specificity. DE0LW4X FC This enzyme is involved in diverse functions including degrading extracellular matrix proteins. It cleaves GSK3beta in vitro. Isoform 2 mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial- nuclear stress signaling with activation of the pro-inflammatory NF- kappaB, NFAT and IRF transcriptional pathways. DE0LW4X KD 33208: Metazoa DE0LW4X PL 7711: Chordata DE0LW4X CL 40674: Mammalia DE0LW4X OD 9443: Primates DE0LW4X FM 9604: Hominidae DE0LW4X GE 9605: Homo DE0LW4X SP 9606: Homo sapiens DEGPI81 ID DEGPI81 DEGPI81 DN Angiotensin-converting enzyme 2 (ACE2) DEGPI81 GN ACE2 DEGPI81 SN ACE-related carboxypeptidase; Metalloprotease MPROT15; Processed angiotensin-converting enzyme 2; ACE2; ACEH; Angiotensin-converting enzyme homolog; UNQ868/PRO1885 DEGPI81 UC ACE2_HUMAN DEGPI81 RD TXA-127 DEGPI81 GI 59272 DEGPI81 E1 3: Hydrolases DEGPI81 E2 3.4: Peptidase DEGPI81 E3 3.4.17: Metallocarboxypeptidase DEGPI81 EC 3.4.17.23 DEGPI81 RC Metabolism of Angiotensinogen to Angiotensins:R-HSA-2022377 DEGPI81 KG Protein digestion and absorption:hsa04974; Renin-angiotensin system:hsa04614 DEGPI81 PD 1XJP; 2AJF; 3D0G; 3D0H; 3D0I; 3KBH; 3SCI; 3SCJ; 3SCK DEGPI81 SQ MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF DEGPI81 TD Primarily distributed in intestine. DEGPI81 FC This enzyme converts angiotensin I to angiotensin 1-9 and angiotensin II to angiotensin 1-7. It can also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. DEGPI81 KD 33208: Metazoa DEGPI81 PL 7711: Chordata DEGPI81 CL 40674: Mammalia DEGPI81 OD 9443: Primates DEGPI81 FM 9604: Hominidae DEGPI81 GE 9605: Homo DEGPI81 SP 9606: Homo sapiens DEQ63LA ID DEQ63LA DEQ63LA DN Dinucleosidetriphosphatase (FHIT) DEQ63LA GN FHIT DEQ63LA SN AP3A hydrolase; Diadenosine 5',5'''-P1,P3-triphosphate hydrolase; Fragile histidine triad protein; Diadenosine triphosphate hydrolase; AP3Aase; FHIT DEQ63LA UC FHIT_HUMAN DEQ63LA RD Adenylylsulfate DEQ63LA GI 2272 DEQ63LA E1 3: Hydrolases DEQ63LA E2 3.6: Acid anhydride hydrolase DEQ63LA E3 3.6.1: Acid anhydride hydrolase DEQ63LA EC 3.6.1.29 DEQ63LA KG Metabolic pathways:hsa01100; Non-small cell lung cancer:hsa05223; Purine metabolism:hsa00230; Small cell lung cancer:hsa05222 DEQ63LA SQ MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKHDKEDFPASWRSEEEMAAEAAALRVYFQ DEQ63LA TD Low tissue/organ specificity. DEQ63LA FC This enzyme cleaves P1-P3-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. It can also hydrolyze P1-P4-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. DEQ63LA KD 33208: Metazoa DEQ63LA PL 7711: Chordata DEQ63LA CL 40674: Mammalia DEQ63LA OD 9443: Primates DEQ63LA FM 9604: Hominidae DEQ63LA GE 9605: Homo DEQ63LA SP 9606: Homo sapiens DESO5ZY ID DESO5ZY DESO5ZY DN Prolyl 4-hydroxylase alpha-1 (P4HA1) DESO5ZY GN P4HA1 DESO5ZY SN Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1; Prolyl 4-hydroxylase subunit alpha-1; 4-PH alpha-1; P4HA; P4HA1 DESO5ZY UC P4HA1_HUMAN DESO5ZY RD Ascorbic acid DESO5ZY GI 5033 DESO5ZY E1 1: Oxidoreductase DESO5ZY E2 1.14: Oxygen paired donor oxidoreductase DESO5ZY E3 1.14.11: 2-oxoglutarate donor oxidoreductase DESO5ZY EC 1.14.11.2 DESO5ZY RC Collagen biosynthesis and modifying enzymes:R-HSA-1650814 DESO5ZY KG Arginine and proline metabolism:hsa00330; Metabolic pathways:hsa01100 DESO5ZY PD 1TJC; 2V5F; 2YQ8; 4BT8; 4BT9; 4BTA; 4BTB DESO5ZY SQ MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE DESO5ZY TD Primarily distributed in vagina. DESO5ZY FC This enzyme catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. DESO5ZY KD 33208: Metazoa DESO5ZY PL 7711: Chordata DESO5ZY CL 40674: Mammalia DESO5ZY OD 9443: Primates DESO5ZY FM 9604: Hominidae DESO5ZY GE 9605: Homo DESO5ZY SP 9606: Homo sapiens DE5FUD0 ID DE5FUD0 DE5FUD0 DN Methylsterol monooxygenase 1 (MSMO1) DE5FUD0 GN MSMO1 DE5FUD0 SN C-4 methylsterol oxidase; DESP4; ERG25; MSMO1; SC4MOL DE5FUD0 UC MSMO1_HUMAN DE5FUD0 RD ED-71 DE5FUD0 GI 6307 DE5FUD0 E1 1: Oxidoreductase DE5FUD0 E2 1.14: Oxygen paired donor oxidoreductase DE5FUD0 E3 1.14.13: NADH/NADPH donor oxidoreductase DE5FUD0 EC 1.14.13.72 DE5FUD0 RC Cholesterol biosynthesis:R-HSA-191273 DE5FUD0 KG Metabolic pathways:hsa01100; Steroid biosynthesis:hsa00100 DE5FUD0 SQ MATNESVSIFSSASLAVEYVDSLLPENPLQEPFKNAWNYMLNNYTKFQIATWGSLIVHEALYFLFCLPGFLFQFIPYMKKYKIQKDKPETWENQWKCFKVLLFNHFCIQLPLICGTYYFTEYFNIPYDWERMPRWYFLLARCFGCAVIEDTWHYFLHRLLHHKRIYKYIHKVHHEFQAPFGMEAEYAHPLETLILGTGFFIGIVLLCDHVILLWAWVTIRLLETIDVHSGYDIPLNPLNLIPFYAGSRHHDFHHMNFIGNYASTFTWWDRIFGTDSQYNAYNEKRKKFEKKTE DE5FUD0 TD Primarily distributed in liver. DE5FUD0 FC This enzyme catalyzes the first step in the removal of the two C-4 methyl groups of 4,4-dimethylzymosterol. DE5FUD0 KD 33208: Metazoa DE5FUD0 PL 7711: Chordata DE5FUD0 CL 40674: Mammalia DE5FUD0 OD 9443: Primates DE5FUD0 FM 9604: Hominidae DE5FUD0 GE 9605: Homo DE5FUD0 SP 9606: Homo sapiens DE437BY ID DE437BY DE437BY DN Delta-aminolevulinate synthase 2 (ALAS2) DE437BY GN ALAS2 DE437BY SN Erythroid-specific mitochondrial 5-aminolevulinate synthase; Delta-ALA synthase 2; 5-aminolevulinic acid synthase 2; ALAS-E; ALAS2; ALASE DE437BY UC HEM0_HUMAN DE437BY RD Glycine DE437BY GI 212 DE437BY E1 2: Transferase DE437BY E2 2.3: Acyltransferase DE437BY E3 2.3.1: Acyltransferase DE437BY EC 2.3.1.37 DE437BY RC Heme biosynthesis:R-HSA-189451 DE437BY KG Glycine, serine and threonine metabolism:hsa00260; Metabolic pathways:hsa01100; Porphyrin and chlorophyll metabolism:hsa00860 DE437BY PD 5QQS; 5QQT; 5QQU; 5QQV; 5QQW; 5QQX; 5QQY; 5QQZ; 5QR0 DE437BY SQ MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGGDSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQEQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA DE437BY TD Primarily distributed in bone marrow and placenta. DE437BY FC This enzyme is an aminolevulinic acid synthase, and it catalyzes the first step in the heme biosynthetic pathway. DE437BY KD 33208: Metazoa DE437BY PL 7711: Chordata DE437BY CL 40674: Mammalia DE437BY OD 9443: Primates DE437BY FM 9604: Hominidae DE437BY GE 9605: Homo DE437BY SP 9606: Homo sapiens DEHKSC6 ID DEHKSC6 DEHKSC6 DN Prostaglandin dehydrogenase 1 (HPGD) DEHKSC6 GN HPGD DEHKSC6 SN Dehydrogenase/reductase family 36C member 1; Short chain dehydrogenase/reductase family 36C member 1; 15-PGDH; 15-hydroxyprostaglandin dehydrogenase [NAD(+)]; HPGD; PGDH1; SDR36C1 DEHKSC6 UC PGDH_HUMAN DEHKSC6 RD Alprostadil DEHKSC6 GI 3248 DEHKSC6 E1 1: Oxidoreductase DEHKSC6 E2 1.1: CH-OH donor oxidoreductase DEHKSC6 E3 1.1.1: NAD/NADP oxidoreductase DEHKSC6 EC 1.1.1.141 DEHKSC6 RC Biosynthesis of D-series resolvins:R-HSA-9018676; Biosynthesis of E-series 18(S)-resolvins:R-HSA-9018896; Synthesis of Lipoxins (LX):R-HSA-2142700; Synthesis of Prostaglandins (PG) and Thromboxanes (TX):R-HSA-2162123 DEHKSC6 KG Transcriptional misregulation in cancer:hsa05202 DEHKSC6 PD 2GDZ DEHKSC6 SQ MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTTPFQAKTQ DEHKSC6 TD Primarily distributed in colon epithelium and placenta. DEHKSC6 FC This enzyme catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. DEHKSC6 KD 33208: Metazoa DEHKSC6 PL 7711: Chordata DEHKSC6 CL 40674: Mammalia DEHKSC6 OD 9443: Primates DEHKSC6 FM 9604: Hominidae DEHKSC6 GE 9605: Homo DEHKSC6 SP 9606: Homo sapiens DEXL6TZ ID DEXL6TZ DEXL6TZ DN Thyroid peroxidase (TPO) DEXL6TZ GN TPO DEXL6TZ SN Iodideperoxidase; High-molecular weight-thyroid peroxidase; Iodide peroxidase-tyrosine iodinase; TPO DEXL6TZ UC PERT_HUMAN DEXL6TZ RD Guaiacol DEXL6TZ GI 7173 DEXL6TZ E1 1: Oxidoreductase DEXL6TZ E2 1.11: Peroxidase DEXL6TZ E3 1.11.1: Peroxidase DEXL6TZ EC 1.11.1.8 DEXL6TZ RC Thyroxine biosynthesis:R-HSA-209968 DEXL6TZ KG Autoimmune thyroid disease:hsa05320; Metabolic pathways:hsa01100; Thyroid hormone synthesis:hsa04918; Tyrosine metabolism:hsa00350 DEXL6TZ SQ MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQRNLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALSEDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSGRAYLPFVPPRAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAALKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPTVSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIRGLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGLPRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQMKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFESCDSITGMNLEAWRETFPQDDKCGFPESVENGDFVHCEESGRRVLVYSCRHGYELQGREQLTCTQEGWDFQPPLCKDVNECADGAHPPCHASARCRNTKGGFQCLCADPYELGDDGRTCVDSGRLPRVTWISMSLAALLIGGFAGLTSTVICRWTRTGTKSTLPISETGGGTPELRCGKHQAVGTSPQRAAAQDSEQESAGMEGRDTHRLPRAL DEXL6TZ TD Primarily distributed in thyroid. DEXL6TZ FC This enzyme iodinates and couples hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). DEXL6TZ KD 33208: Metazoa DEXL6TZ PL 7711: Chordata DEXL6TZ CL 40674: Mammalia DEXL6TZ OD 9443: Primates DEXL6TZ FM 9604: Hominidae DEXL6TZ GE 9605: Homo DEXL6TZ SP 9606: Homo sapiens DELSNWC ID DELSNWC DELSNWC DN Sphingosine kinase 1 (SPHK1) DELSNWC GN SPHK1 DELSNWC SN Acetyltransferase SPHK1; Sphingosine protein kinase 1; SK 1; SK1; SPHK1; SPK 1 DELSNWC UC SPHK1_HUMAN DELSNWC RD YP-005 DELSNWC GI 8877 DELSNWC E1 2: Transferase DELSNWC E2 2.7: Kinase DELSNWC E3 2.7.1: Phosphotransferase DELSNWC EC 2.7.1.91 DELSNWC RC Association of TriC/CCT with target proteins during biosynthesis:R-HSA-390471; Extra-nuclear estrogen signaling:R-HSA-9009391; Sphingolipid de novo biosynthesis:R-HSA-1660661; VEGFR2 mediated cell proliferation:R-HSA-5218921 DELSNWC KG Apelin signaling pathway:hsa04371; Calcium signaling pathway:hsa04020; Fc gamma R-mediated phagocytosis:hsa04666; Metabolic pathways:hsa01100; Phospholipase D signaling pathway:hsa04072; Sphingolipid metabolism:hsa00600; Sphingolipid signaling pathway:hsa04071; Tuberculosis:hsa05152; VEGF signaling pathway:hsa04370 DELSNWC PD 3VZB; 3VZC; 3VZD; 4L02; 4V24 DELSNWC SQ MDPAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAEISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSVLSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASPVVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMHLFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMVSEAVQGQVHPNYFWMVSGCVEPPPSWKPQQMPPPEEPL DELSNWC TD Low tissue/organ specificity. DELSNWC FC This enzyme catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. It also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo- dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol. DELSNWC KD 33208: Metazoa DELSNWC PL 7711: Chordata DELSNWC CL 40674: Mammalia DELSNWC OD 9443: Primates DELSNWC FM 9604: Hominidae DELSNWC GE 9605: Homo DELSNWC SP 9606: Homo sapiens DE4Q2OE ID DE4Q2OE DE4Q2OE DN Prostaglandin reductase 1 (PTGR1) DE4Q2OE GN PTGR1 DE4Q2OE SN NADP-dependent leukotriene B4 12-hydroxydehydrogenase; 15-oxoprostaglandin 13-reductase; LTB4DH; PRG-1; PTGR1 DE4Q2OE UC PTGR1_HUMAN DE4Q2OE RD MGI-114 DE4Q2OE GI 22949 DE4Q2OE E1 1: Oxidoreductase DE4Q2OE E2 1.3: CH-CH donor oxidoreductase DE4Q2OE E3 1.3.1: NAD/NADP acceptor oxidoreductase DE4Q2OE EC 1.3.1.16 DE4Q2OE RC Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691; Synthesis of Lipoxins (LX):R-HSA-2142700 DE4Q2OE PD 1ZSV; 2Y05 DE4Q2OE SQ MVRTKTWTLKKHFVGYPTNSDFELKTAELPPLKNGEVLLEALFLTVDPYMRVAAKRLKEGDTMMGQQVAKVVESKNVALPKGTIVLASPGWTTHSISDGKDLEKLLTEWPDTIPLSLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAVGSDEKVAYLQKLGFDVVFNYKTVESLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRTGPLPPGPPPEIVIYQELRMEAFVVYRWQGDARQKALKDLLKWVLEGKIQYKEYIIEGFENMPAAFMGMLKGDNLGKTIVKA DE4Q2OE TD Primarily distributed in kidney, liver and intestine. DE4Q2OE FC This enzyme functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. It catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo- leukotriene B4, which is an initial and key step of metabolic inactivation of leukotriene B4. DE4Q2OE KD 33208: Metazoa DE4Q2OE PL 7711: Chordata DE4Q2OE CL 40674: Mammalia DE4Q2OE OD 9443: Primates DE4Q2OE FM 9604: Hominidae DE4Q2OE GE 9605: Homo DE4Q2OE SP 9606: Homo sapiens DETBNY4 ID DETBNY4 DETBNY4 DN Porphobilinogen synthase (ALAD) DETBNY4 GN ALAD DETBNY4 SN Delta-aminolevulinic acid dehydratase; Porpho-bilinogensynthase; ALAD; ALADH DETBNY4 UC HEM2_HUMAN DETBNY4 RD Aminolevulinic acid DETBNY4 GI 210 DETBNY4 E1 4: Lyases DETBNY4 E2 4.2: Carbon-oxygen lyase DETBNY4 E3 4.2.1: Hydro-lyase DETBNY4 EC 4.2.1.24 DETBNY4 RC Heme biosynthesis:R-HSA-189451; Neutrophil degranulation:R-HSA-6798695 DETBNY4 KG Metabolic pathways:hsa01100; Porphyrin and chlorophyll metabolism:hsa00860 DETBNY4 PD 1E51; 1PV8; 5HMS; 5HNR DETBNY4 SQ MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKRLEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKEALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRDVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAVLEAMTAFRRAGADIIITYYTPQLLQWLKEE DETBNY4 TD Primarily distributed in liver. DETBNY4 FC This enzyme catalyzes an early step in the biosynthesis of tetrapyrroles. It binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. DETBNY4 KD 33208: Metazoa DETBNY4 PL 7711: Chordata DETBNY4 CL 40674: Mammalia DETBNY4 OD 9443: Primates DETBNY4 FM 9604: Hominidae DETBNY4 GE 9605: Homo DETBNY4 SP 9606: Homo sapiens DEIX1PO ID DEIX1PO DEIX1PO DN Phosphorylethanolamine transferase (PCYT2) DEIX1PO GN PCYT2 DEIX1PO SN CTP:phosphoethanolamine cytidylyltransferase; Ethanolamine-phosphate cytidylyltransferase; PCYT2 DEIX1PO UC PCY2_HUMAN DEIX1PO RD Lamivudine DEIX1PO GI 5833 DEIX1PO E1 2: Transferase DEIX1PO E2 2.7: Kinase DEIX1PO E3 2.7.7: Nucleotidyltransferase DEIX1PO EC 2.7.7.14 DEIX1PO RC Synthesis of PE:R-HSA-1483213 DEIX1PO KG Glycerophospholipid metabolism:hsa00564; Metabolic pathways:hsa01100; Phosphonate and phosphinate metabolism:hsa00440 DEIX1PO PD 3ELB; 4XSV DEIX1PO SQ MIRNGRGAAGGAEQPGPGGRRAVRVWCDGCYDMVHYGHSNQLRQARAMGDYLIVGVHTDEEIAKHKGPPVFTQEERYKMVQAIKWVDEVVPAAPYVTTLETLDKYNCDFCVHGNDITLTVDGRDTYEEVKQAGRYRECKRTQGVSTTDLVGRMLLVTKAHHSSQEMSSEYREYADSFGKCPGGRNPWTGVSQFLQTSQKIIQFASGKEPQPGETVIYVAGAFDLFHIGHVDFLEKVHRLAERPYIIAGLHFDQEVNHYKGKNYPIMNLHERTLSVLACRYVSEVVIGAPYAVTAELLSHFKVDLVCHGKTEIIPDRDGSDPYQEPKRRGIFRQIDSGSNLTTDLIVQRIITNRLEYEARNQKKEAKELAFLEAARQQAAQPLGERDGDF DEIX1PO TD Primarily distributed in testis, liver, heart and skeletalmuscle. DEIX1PO FC This enzyme plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. It catalyzes the formation of CDP- ethanolamine. DEIX1PO KD 33208: Metazoa DEIX1PO PL 7711: Chordata DEIX1PO CL 40674: Mammalia DEIX1PO OD 9443: Primates DEIX1PO FM 9604: Hominidae DEIX1PO GE 9605: Homo DEIX1PO SP 9606: Homo sapiens DEGI1A9 ID DEGI1A9 DEGI1A9 DN N-acetylglutamate synthase (NAGS) DEGI1A9 GN NAGS DEGI1A9 SN Amino-acid acetyltransferase; N-acetylglutamate synthase conserved domain form; N-acetylglutamate synthase long form; N-acetylglutamate synthase short form; N-acetylglutamate synthase, mitochondrial; NAGS DEGI1A9 UC NAGS_HUMAN DEGI1A9 RD L-glutamine DEGI1A9 GI 162417 DEGI1A9 E1 2: Transferase DEGI1A9 E2 2.3: Acyltransferase DEGI1A9 E3 2.3.1: Acyltransferase DEGI1A9 EC 2.3.1.1 DEGI1A9 RC Urea cycle:R-HSA-70635 DEGI1A9 KG 2-Oxocarboxylic acid metabolism:hsa01210; Arginine biosynthesis:hsa00220; Biosynthesis of amino acids:hsa01230; Metabolic pathways:hsa01100 DEGI1A9 PD 4K30 DEGI1A9 SQ MATALMAVVLRAAAVAPRLRGRGGTGGARRLSCGARRRAARGTSPGRRLSTAWSQPQPPPEEYAGADDVSQSPVAEEPSWVPSPRPPVPHESPEPPSGRSLVQRDIQAFLNQCGASPGEARHWLTQFQTCHHSADKPFAVIEVDEEVLKCQQGVSSLAFALAFLQRMDMKPLVVLGLPAPTAPSGCLSFWEAKAQLAKSCKVLVDALRHNAAAAVPFFGGGSVLRAAEPAPHASYGGIVSVETDLLQWCLESGSIPILCPIGETAARRSVLLDSLEVTASLAKALRPTKIIFLNNTGGLRDSSHKVLSNVNLPADLDLVCNAEWVSTKERQQMRLIVDVLSRLPHHSSAVITAASTLLTELFSNKGSGTLFKNAERMLRVRSLDKLDQGRLVDLVNASFGKKLRDDYLASLRPRLHSIYVSEGYNAAAILTMEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFHKPASDPGS DEGI1A9 TD Primarily distributed in liver, kidney and small intestine. DEGI1A9 FC This enzyme catalyzes the production of N-acetylglutamate (NAG) from glutamate and acetyl-CoA. DEGI1A9 KD 33208: Metazoa DEGI1A9 PL 7711: Chordata DEGI1A9 CL 40674: Mammalia DEGI1A9 OD 9443: Primates DEGI1A9 FM 9604: Hominidae DEGI1A9 GE 9605: Homo DEGI1A9 SP 9606: Homo sapiens DE7G63U ID DE7G63U DE7G63U DN Mevalonate pyrophosphate decarboxylase (MPD) DE7G63U GN MVD DE7G63U SN Diphosphomevalonate decarboxylase; Mevalonate (diphospho)decarboxylase; MDDase; MPD; MVD DE7G63U UC MVD1_HUMAN DE7G63U RD Mevalonate-PP DE7G63U GI 4597 DE7G63U E1 4: Lyases DE7G63U E2 4.1: Carbon-carbon lyase DE7G63U E3 4.1.1: Carboxy-lyase DE7G63U EC 4.1.1.33 DE7G63U RC Activation of gene expression by SREBF (SREBP):R-HSA-2426168; Cholesterol biosynthesis:R-HSA-191273; Synthesis of Dolichyl-phosphate:R-HSA-446199 DE7G63U KG Metabolic pathways:hsa01100; Terpenoid backbone biosynthesis:hsa00900 DE7G63U PD 3D4J DE7G63U SQ MASEKPLAAVTCTAPVNIAVIKYWGKRDEELVLPINSSLSVTLHQDQLKTTTTAVISKDFTEDRIWLNGREEDVGQPRLQACLREIRCLARKRRNSRDGDPLPSSLSCKVHVASVNNFPTAAGLASSAAGYACLAYTLARVYGVESDLSEVARRGSGSACRSLYGGFVEWQMGEQADGKDSIARQVAPESHWPELRVLILVVSAEKKLTGSTVGMRASVETSPLLRFRAESVVPARMAEMARCIRERDFPSFAQLTMKDSNQFHATCLDTFPPISYLNAISWRIIHLVHRFNAHHGDTKVAYTFDAGPNAVIFTLDDTVAEFVAAVWHGFPPGSNGDTFLKGLQVRPAPLSAELQAALAMEPTPGGVKYIIVTQVGPGPQILDDPCAHLLGPDGLPKPAA DE7G63U TD Primarily distributed in heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta. DE7G63U FC This enzyme converts mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP) through ATP dependent decarboxylation. DE7G63U KD 33208: Metazoa DE7G63U PL 7711: Chordata DE7G63U CL 40674: Mammalia DE7G63U OD 9443: Primates DE7G63U FM 9604: Hominidae DE7G63U GE 9605: Homo DE7G63U SP 9606: Homo sapiens DEVSTRI ID DEVSTRI DEVSTRI DN Glutaminyl-tRNA synthetase (GLNRS) DEVSTRI GN QARS1 DEVSTRI SN Glutamine-specific glutamyl-transfer ribonucleate; Aminoacyl-tRNA amidotransferase; Glutamine--tRNA ligase; AA-tRNA amidotransferase; GlnRS; QARS; QARS1 DEVSTRI UC SYQ_HUMAN DEVSTRI RD L-glutamine DEVSTRI GI 5859 DEVSTRI E1 6: Ligase DEVSTRI E2 6.1: Carbon-oxygen ligase DEVSTRI E3 6.1.1: Aminoacyl tRNA synthetase DEVSTRI EC 6.1.1.18 DEVSTRI RC Cytosolic tRNA aminoacylation:R-HSA-379716; Mitochondrial tRNA aminoacylation:R-HSA-379726; Selenoamino acid metabolism:R-HSA-2408522 DEVSTRI KG Aminoacyl-tRNA biosynthesis:hsa00970; Metabolic pathways:hsa01100 DEVSTRI PD 4R3Z; 4YE6; 4YE8; 4YE9 DEVSTRI SQ MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV DEVSTRI TD Primarily distributed in fetal cerebral cortex, particularly in the ventricular zone, inner subventricular zone, outersubventricular zone, and cortical plate. DEVSTRI FC This enzyme catalyzes the conversion of L-glutamine and tRNAGln to L-glutaminyl-tRNAGln. DEVSTRI KD 33208: Metazoa DEVSTRI PL 7711: Chordata DEVSTRI CL 40674: Mammalia DEVSTRI OD 9443: Primates DEVSTRI FM 9604: Hominidae DEVSTRI GE 9605: Homo DEVSTRI SP 9606: Homo sapiens DEEBDFT ID DEEBDFT DEEBDFT DN Glutamate-cysteine ligase regulatory (GCLM) DEEBDFT GN GCLM DEEBDFT SN Glutamate--cysteine ligase modifier subunit; Glutamate--cysteine ligase regulatory subunit; Gamma-ECS regulatory subunit; Gamma-glutamylcysteine synthetase regulatory subunit; GCLM; GCS light chain; GLCLR DEEBDFT UC GSH0_HUMAN DEEBDFT RD L-glutamine DEEBDFT GI 2730 DEEBDFT E1 6: Ligase DEEBDFT E2 6.3: Carbon-nitrogen ligase DEEBDFT E3 6.3.2: Peptide synthase DEEBDFT EC 6.3.2.2 DEEBDFT RC Defective GCLC causes Hemolytic anemia due to gamma-glutamylcysteine synthetase deficiency (HAGGSD):R-HSA-5578999; Glutathione synthesis and recycling:R-HSA-174403 DEEBDFT KG Cysteine and methionine metabolism:hsa00270; Ferroptosis:hsa04216; Glutathione metabolism:hsa00480; Metabolic pathways:hsa01100 DEEBDFT SQ MGTDSRAAKALLARARTLHLQTGNLLNWGRLRKKCPSTHSEELHDCIQKTLNEWSSQINPDLVREFPDVLECTVSHAVEKINPDEREEMKVSAKLFIVESNSSSSTRSAVDMACSVLGVAQLDSVIIASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIQAHEWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS DEEBDFT TD Primarily distributed in skeletal muscle. DEEBDFT FC This enzyme is the first rate limiting enzyme of glutathione synthesis. The enzyme consists of two subunits, a heavy catalytic subuit and a light regulatory subunit. Gamma glutamylcysteine synthetase deficiency has been implicated in some forms of hemolytic anemia. DEEBDFT KD 33208: Metazoa DEEBDFT PL 7711: Chordata DEEBDFT CL 40674: Mammalia DEEBDFT OD 9443: Primates DEEBDFT FM 9604: Hominidae DEEBDFT GE 9605: Homo DEEBDFT SP 9606: Homo sapiens DE2XQGW ID DE2XQGW DE2XQGW DN Lauric acid omega-hydroxylase (CYP4A11) DE2XQGW GN CYP4A11 DE2XQGW SN Fatty acid omega-hydroxylase; Cytochrome P-450HK-omega; Cytochrome P450 4A11; Cytochrome P450HL-omega; 20-HETE synthase; 20-hydroxyeicosatetraenoic acid synthase; CYP4A11; CYP4A2; CYP4AII; CYPIVA11 DE2XQGW UC CP4AB_HUMAN DE2XQGW RD Clofibrate DE2XQGW GI 1579 DE2XQGW E1 1: Oxidoreductase DE2XQGW E2 1.14: Oxygen paired donor oxidoreductase DE2XQGW E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE2XQGW EC 1.14.15.3 DE2XQGW RC Eicosanoids:R-HSA-211979; Fatty acids:R-HSA-211935; Miscellaneous substrates:R-HSA-211958; PPARA activates gene expression:R-HSA-1989781; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE):R-HSA-2142816; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DE2XQGW KG Arachidonic acid metabolism:hsa00590; Fatty acid degradation:hsa00071; Inflammatory mediator regulation of TRP channels:hsa04750; Metabolic pathways:hsa01100; PPAR signaling pathway:hsa03320; Retinol metabolism:hsa00830; Vascular smooth muscle contraction:hsa04270 DE2XQGW SQ MSVSVLSPSRLLGDVSGILQAASLLILLLLLIKAVQLYLHRQWLLKALQQFPCPPSHWLFGHIQELQQDQELQRIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARLVLKSKNGIHLRLRRLPNPCEDKDQL DE2XQGW TD Primarily distributed in kidney and liver. DE2XQGW FC This enzyme is involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins). It catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids, the catalytic efficiency decreasing in the following order: dodecanoic > tetradecanoic > (9Z)-octadecenoic > (9Z,12Z)-octadecadienoic > hexadecanoic acid. It acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver and participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20- hydroxyeicosatetraenoic acid (20-HETE). It can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency. Besides, it may contribute to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acid, thereby initiating chain shortening. DE2XQGW KD 33208: Metazoa DE2XQGW PL 7711: Chordata DE2XQGW CL 40674: Mammalia DE2XQGW OD 9443: Primates DE2XQGW FM 9604: Hominidae DE2XQGW GE 9605: Homo DE2XQGW SP 9606: Homo sapiens DE3PZ0I ID DE3PZ0I DE3PZ0I DN Histamine N-methyltransferase (HNMT) DE3PZ0I GN HNMT DE3PZ0I SN Histamine 1-methyltransferase; Histamine-methylating enzyme; Imidazole methyltransferase; Imidazole N-methyltransferase; Imidazolemethyltransferase; HMT; HNMT DE3PZ0I UC HNMT_HUMAN DE3PZ0I RD Histamine DE3PZ0I GI 3176 DE3PZ0I E1 2: Transferase DE3PZ0I E2 2.1: Methylase DE3PZ0I E3 2.1.1: Methyltransferase DE3PZ0I EC 2.1.1.8 DE3PZ0I RC Histidine catabolism:R-HSA-70921; Metabolism of ingested SeMet, Sec, MeSec into H2Se:R-HSA-2408508 DE3PZ0I KG Histidine metabolism:hsa00340; Metabolic pathways:hsa01100 DE3PZ0I PD 1ICZ; 1JQD; 1JQE; 2AOT; 2AOU; 2AOV; 2AOW; 2AOX DE3PZ0I SQ MASSMRSLFSDHGKYVESFRRFLNHSTEHQCMQEFMDKKLPGIIGRIGDTKSEIKILSIGGGAGEIDLQILSKVQAQYPGVCINNEVVEPSAEQIAKYKELVAKTSNLENVKFAWHKETSSEYQSRMLEKKELQKWDFIHMIQMLYYVKDIPATLKFFHSLLGTNAKMLIIVVSGSSGWDKLWKKYGSRFPQDDLCQYITSDDLTQMLDNLGLKYECYDLLSTMDISDCFIDGNENGDLLWDFLTETCNFNATAPPDLRAELGKDLQEPEFSAKKEGKVLFNNTLSFIVIEA DE3PZ0I TD Low tissue/organ specificity. DE3PZ0I FC This enzyme inactivates histamine by N-methylation and plays an important role in degrading histamine. DE3PZ0I KD 33208: Metazoa DE3PZ0I PL 7711: Chordata DE3PZ0I CL 40674: Mammalia DE3PZ0I OD 9443: Primates DE3PZ0I FM 9604: Hominidae DE3PZ0I GE 9605: Homo DE3PZ0I SP 9606: Homo sapiens DEFCMPI ID DEFCMPI DEFCMPI DN Leukotriene B4 omega-hydroxylase (CYP4F3) DEFCMPI GN CYP4F3 DEFCMPI SN Leukotriene-B(4) 20-monooxygenase 2; Docosahexaenoic acid omega-hydroxylase CYP4F3; Leukotriene-B(4) omega-hydroxylase 2; Cytochrome P450 4F3; Cytochrome P450-LTB-omega; CYP4F3; CYPIVF3; LTB4H DEFCMPI UC CP4F3_HUMAN DEFCMPI RD BML1-E04 DEFCMPI GI 4051 DEFCMPI E1 1: Oxidoreductase DEFCMPI E2 1.14: Oxygen paired donor oxidoreductase DEFCMPI E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEFCMPI EC 1.14.14.1 DEFCMPI RC Eicosanoids:R-HSA-211979; Fatty acids:R-HSA-211935; Miscellaneous substrates:R-HSA-211958; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DEFCMPI KG Arachidonic acid metabolism:hsa00590; Metabolic pathways:hsa01100 DEFCMPI SQ MPQLSLSSLGLWPMAASPWLLLLLVGASWLLARILAWTYTFYDNCCRLRCFPQPPKRNWFLGHLGLIHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYIKPVLFAPAAIVPKDKVFYSFLKPWLGDGLLLSAGEKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSARLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVTKRHQQILLYIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCIKESLRLHPPVPAVSRCCTQDIVLPDGRVIPKGIICLISVFGTHHNPAVWPDPEVYDPFRFDPKNIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLGLTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS DEFCMPI TD Primarily distributed in liver. DEFCMPI FC This enzyme is involved in the metabolism of various endogenous substrates, including fatty acids and their oxygenated derivatives (oxylipins). Isoform CYP4F3A catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of oxylipins in myeloid cells, displaying higher affinity for arachidonate metabolite leukotriene B4 (LTB4) and inactivates LTB4 via three successive oxidative transformations to 20-hydroxy-LTB4, then to 20-oxo-LTB4 and to 20- carboxy-LTB4. It exhibits omega-hydroxylase activity toward long-chain fatty acid epoxides with preference for 8,9-epoxy- (5Z,11Z,14Z)-eicosatrienoate (EET) and 9,10-epoxyoctadecanoate. It contributes to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid, by catalyzing successive omega-oxidations to the corresponding dicarboxylic acid, thereby initiating chain shortening. Isoform CYP4F3B catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of polyunsaturated fatty acids (PUFAs) and participates in the conversion of arachidonic acid to 20- hydroxyeicosatetraenoic acid (20-HETE). Besides, it exhibits high omega-hydroxylase activity toward other PUFAs, including eicosatrienoic acid (ETA), eicosapentaenoic acid (EPA) and docosahexaenoic acid. It can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of PUFAs with lower efficiency. It contributes to the degradation of saturated very long-chain fatty acids (VLCFAs) such as docosanoic acid and hexacosanoic acid, by catalyzing successive omega-oxidations and to the corresponding dicarboxylic acids, thereby initiating chain shortening. DEFCMPI KD 33208: Metazoa DEFCMPI PL 7711: Chordata DEFCMPI CL 40674: Mammalia DEFCMPI OD 9443: Primates DEFCMPI FM 9604: Hominidae DEFCMPI GE 9605: Homo DEFCMPI SP 9606: Homo sapiens DEDQHBV ID DEDQHBV DEDQHBV DN Adenosine aminohydrolase (ADA) DEDQHBV GN ADA DEDQHBV SN Adenosine deaminase; ADA; ADA1; ADA2; ADA1/ADA2; Entrez:100 DEDQHBV UC ADA_HUMAN DEDQHBV RD Nelarabine DEDQHBV GI 100 DEDQHBV E1 3: Hydrolases DEDQHBV E2 3.5: Carbon-nitrogen hydrolase DEDQHBV E3 3.5.4: Cyclic amidine hydrolase DEDQHBV EC 3.5.4.4 DEDQHBV RC Purine salvage:R-HSA-74217 DEDQHBV KG Metabolic pathways:hsa01100; Primary immunodeficiency:hsa05340; Purine metabolism:hsa00230 DEDQHBV PD 1M7M; 3IAR DEDQHBV SQ MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQNL DEDQHBV TD Primarily distributed in blood, intestine and lymphoid tissue. DEDQHBV FC This enzyme catalyzes the hydrolytic deamination of adenosine and 2- deoxyadenosine. It plays an important role in purine metabolism. DEDQHBV KD 33208: Metazoa DEDQHBV PL 7711: Chordata DEDQHBV CL 40674: Mammalia DEDQHBV OD 9443: Primates DEDQHBV FM 9604: Hominidae DEDQHBV GE 9605: Homo DEDQHBV SP 9606: Homo sapiens DENCJTA ID DENCJTA DENCJTA DN Oxaloacetate decarboxylase (FAHD1) DENCJTA GN FAHD1 DENCJTA SN OAA decarboxylase; YisK-like protein; Mitochondrial acylpyruvase FAHD1; FAH domain-containing protein 1; Fumarylacetoacetate hydrolase domain-containing protein 1; YISKL; FAHD1; C16orf36 DENCJTA UC FAHD1_HUMAN DENCJTA RD Oxaloacetate DENCJTA GI 81889 DENCJTA E1 3: Hydrolases DENCJTA E2 3.7: Carbon-carbon hydrolase DENCJTA E3 3.7.1: Carbon-carbon hydrolase DENCJTA EC 3.7.1.5 DENCJTA RC Citric acid cycle (TCA cycle):R-HSA-71403 DENCJTA KG Metabolic pathways:hsa01100; Tyrosine metabolism:hsa00350 DENCJTA PD 1SAW; 6FOG; 6FOH DENCJTA SQ MGIMAASRPLSRFWEWGKNIVCVGRNYADHVREMRSAVLSEPVLFLKPSTAYAPEGSPILMPAYTRNLHHELELGVVMGKRCRAVPEAAAMDYVGGYALCLDMTARDVQDECKKKGLPWTLAKSFTASCPVSAFVPKEKIPDPHKLKLWLKVNGELRQEGETSSMIFSIPYIISYVSKIITLEEGDIILTGTPKGVGPVKENDEIEAGIHGLVSMTFKVEKPEY DENCJTA TD Low tissue/organ specificity. DENCJTA FC This enzyme hydrolyzes acetylpyruvate and fumarylpyruvate in vitro and also has oxaloacetate decarboxylase activity. DENCJTA KD 33208: Metazoa DENCJTA PL 7711: Chordata DENCJTA CL 40674: Mammalia DENCJTA OD 9443: Primates DENCJTA FM 9604: Hominidae DENCJTA GE 9605: Homo DENCJTA SP 9606: Homo sapiens DE2ZWSM ID DE2ZWSM DE2ZWSM DN Aldehyde dehydrogenase 7 (ALDH7) DE2ZWSM GN ALDH3B1 DE2ZWSM SN Aldehyde dehydrogenase 3 family member B1; ALDH3B1; ALDH7 DE2ZWSM UC AL3B1_HUMAN DE2ZWSM RD SC-47945 DE2ZWSM GI 221 DE2ZWSM E1 1: Oxidoreductase DE2ZWSM E2 1.2: Aldehyde/oxo donor oxidoreductase DE2ZWSM E3 1.2.1: NAD/NADP acceptor oxidoreductase DE2ZWSM EC 1.2.1.5 DE2ZWSM RC Neutrophil degranulation:R-HSA-6798695; Sphingolipid de novo biosynthesis:R-HSA-1660661 DE2ZWSM KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Glycolysis / Gluconeogenesis:hsa00010; Histidine metabolism:hsa00340; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Phenylalanine metabolism:hsa00360; Tyrosine metabolism:hsa00350; beta-Alanine metabolism:hsa00410 DE2ZWSM SQ MDPLGDTLRRLREAFHAGRTRPAEFRAAQLQGLGRFLQENKQLLHDALAQDLHKSAFESEVSEVAISQGEVTLALRNLRAWMKDERVPKNLATQLDSAFIRKEPFGLVLIIAPWNYPLNLTLVPLVGALAAGNCVVLKPSEISKNVEKILAEVLPQYVDQSCFAVVLGGPQETGQLLEHRFDYIFFTGSPRVGKIVMTAAAKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGRIINQKQFQRLRALLGCGRVAIGGQSDESDRYIAPTVLVDVQEMEPVMQEEIFGPILPIVNVQSLDEAIEFINRREKPLALYAFSNSSQVVKRVLTQTSSGGFCGNDGFMHMTLASLPFGGVGASGMGRYHGKFSFDTFSHHRACLLRSPGMEKLNALRYPPQSPRRLRMLLVAMEAQGCSCTLL DE2ZWSM TD Primarily distributed in kidney and lung. DE2ZWSM FC This enzyme oxidizes medium and long chain saturated and unsaturated aldehydes. It also metabolizes benzaldehyde and it has low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde. DE2ZWSM KD 33208: Metazoa DE2ZWSM PL 7711: Chordata DE2ZWSM CL 40674: Mammalia DE2ZWSM OD 9443: Primates DE2ZWSM FM 9604: Hominidae DE2ZWSM GE 9605: Homo DE2ZWSM SP 9606: Homo sapiens DE5KEWZ ID DE5KEWZ DE5KEWZ DN Succinate-semialdehyde dehydrogenase (ALDH5A1) DE5KEWZ GN ALDH5A1 DE5KEWZ SN Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; Mitochondrial succinate-semialdehyde dehydrogenase; ALDH5A1; SSADH DE5KEWZ UC SSDH_HUMAN DE5KEWZ RD Sodium oxybate DE5KEWZ GI 7915 DE5KEWZ E1 1: Oxidoreductase DE5KEWZ E2 1.2: Aldehyde/oxo donor oxidoreductase DE5KEWZ E3 1.2.1: NAD/NADP acceptor oxidoreductase DE5KEWZ EC 1.2.1.24 DE5KEWZ RC Degradation of GABA:R-HSA-916853 DE5KEWZ KG Alanine, aspartate and glutamate metabolism:hsa00250; Butanoate metabolism:hsa00650; Metabolic pathways:hsa01100 DE5KEWZ PD 2W8N; 2W8O; 2W8P; 2W8Q; 2W8R DE5KEWZ SQ MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLRTDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKERSSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIHTPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALALAELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAFAEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFFEPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL DE5KEWZ TD Primarily distributed in liver. Also expressed in brain, pancreas, heart, skeletal muscle and kidney. DE5KEWZ FC This enzyme catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). DE5KEWZ KD 33208: Metazoa DE5KEWZ PL 7711: Chordata DE5KEWZ CL 40674: Mammalia DE5KEWZ OD 9443: Primates DE5KEWZ FM 9604: Hominidae DE5KEWZ GE 9605: Homo DE5KEWZ SP 9606: Homo sapiens DESI4OK ID DESI4OK DESI4OK DN Retinol dehydrogenase 5 (RDH5) DESI4OK GN RDH5 DESI4OK SN Dehydrogenase/reductase family 9C member 5; 11-cis RDH; 11-cis RoDH; 11-cis retinol dehydrogenase; 9-cis retinol dehydrogenase; Short chain dehydrogenase/reductase family 9C member 5; 9cRDH; HSD17B9; RDH1; RDH5; SDR9C5 DESI4OK UC RDH5_HUMAN DESI4OK RD NSC-122758 DESI4OK GI 5959 DESI4OK E1 1: Oxidoreductase DESI4OK E2 1.1: CH-OH donor oxidoreductase DESI4OK E3 1.1.1: NAD/NADP oxidoreductase DESI4OK EC 1.1.1.315 DESI4OK RC RA biosynthesis pathway:R-HSA-5365859; Retinoid cycle disease events:R-HSA-2453864; The canonical retinoid cycle in rods (twilight vision):R-HSA-2453902 DESI4OK KG Retinol metabolism:hsa00830 DESI4OK SQ MWLPLLLGALLWAVLWLLRDRQSLPASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLEKTLQACWARLPPATQAHYGGAFLTKYLKMQQRIMNLICDPDLTKVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVLTWVLPKPAQAVY DESI4OK TD Primarily distributed in adipose tissue and retina. DESI4OK FC This enzyme catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner. But it has no activity towards all-trans retinal. It plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). and also recognizes steroids (androsterone, androstanediol) as its substrates. DESI4OK KD 33208: Metazoa DESI4OK PL 7711: Chordata DESI4OK CL 40674: Mammalia DESI4OK OD 9443: Primates DESI4OK FM 9604: Hominidae DESI4OK GE 9605: Homo DESI4OK SP 9606: Homo sapiens DESWQMH ID DESWQMH DESWQMH DN Propionyl-CoA carboxylase beta (PCCB) DESWQMH GN PCCB DESWQMH SN Propanoyl-CoA:carbon dioxide ligase beta; Mitochondrial propionyl-CoA carboxylase beta; PCCase subunit beta; PCCB DESWQMH UC PCCB_HUMAN DESWQMH RD L-valine DESWQMH GI 5096 DESWQMH E1 6: Ligase DESWQMH E2 6.4: Carbon-carbon ligase DESWQMH E3 6.4.1: Carbon-carbon ligase DESWQMH EC 6.4.1.3 DESWQMH RC Biotin transport and metabolism:R-HSA-196780; Defective HLCS causes multiple carboxylase deficiency:R-HSA-3371599; Propionyl-CoA catabolism:R-HSA-71032 DESWQMH KG Carbon metabolism:hsa01200; Glyoxylate and dicarboxylate metabolism:hsa00630; Metabolic pathways:hsa01100; Propanoate metabolism:hsa00640; Valine, leucine and isoleucine degradation:hsa00280 DESWQMH SQ MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL DESWQMH TD Primarily distributed in liver. DESWQMH FC This enzyme is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl- CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA. Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate. Other alternative minor substrates include (2E)- butenoyl-CoA/crotonoyl-CoA (By similarity). DESWQMH KD 33208: Metazoa DESWQMH PL 7711: Chordata DESWQMH CL 40674: Mammalia DESWQMH OD 9443: Primates DESWQMH FM 9604: Hominidae DESWQMH GE 9605: Homo DESWQMH SP 9606: Homo sapiens DEUL532 ID DEUL532 DEUL532 DN Choline glycerophosphodiester phosphodiesterase (ENPP6) DEUL532 GN ENPP6 DEUL532 SN Glycerophosphocholine cholinephosphodiesterase ENPP6; Choline-specific glycerophosphodiester phosphodiesterase; Ectonucleotide pyrophosphatase/phosphodiesterase family member 6; GPC-Cpde; E-NPP 6; ENPP6; NPP-6; UNQ1889/PRO4334 DEUL532 UC ENPP6_HUMAN DEUL532 RD Cholini alfosceras DEUL532 GI 133121 DEUL532 E1 3: Hydrolases DEUL532 E2 3.1: Ester bond hydrolase DEUL532 E3 3.1.4: Phosphoric diester hydrolase DEUL532 EC 3.1.4.3 DEUL532 RC Glycerophospholipid catabolism:R-HSA-6814848 DEUL532 KG Ether lipid metabolism:hsa00565 DEUL532 SQ MAVKLGTLLLALALGLAQPASARRKLLVFLLDGFRSDYISDEALESLPGFKEIVSRGVKVDYLTPDFPSLSYPNYYTLMTGRHCEVHQMIGNYMWDPTTNKSFDIGVNKDSLMPLWWNGSEPLWVTLTKAKRKVYMYYWPGCEVEILGVRPTYCLEYKNVPTDINFANAVSDALDSFKSGRADLAAIYHERIDVEGHHYGPASPQRKDALKAVDTVLKYMTKWIQERGLQDRLNVIIFSDHGMTDIFWMDKVIELNKYISLNDLQQVKDRGPVVSLWPAPGKHSEIYNKLSTVEHMTVYEKEAIPSRFYYKKGKFVSPLTLVADEGWFITENREMLPFWMNSTGRREGWQRGWHGYDNELMDMRGIFLAFGPDFKSNFRAAPIRSVDVYNVMCNVVGITPLPNNGSWSRVMCMLKGRASTAPPVWPSHCALALILLFLLA DEUL532 TD Primarily distributed in brain and kidney. DEUL532 FC This enzyme hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells. It has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, it hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet- activating factor (PAF) and lysoPAF, but not other lysophospholipids. DEUL532 KD 33208: Metazoa DEUL532 PL 7711: Chordata DEUL532 CL 40674: Mammalia DEUL532 OD 9443: Primates DEUL532 FM 9604: Hominidae DEUL532 GE 9605: Homo DEUL532 SP 9606: Homo sapiens DEFNVD7 ID DEFNVD7 DEFNVD7 DN Ras proteins prenyltransferase alpha (FNTA) DEFNVD7 GN FNTA DEFNVD7 SN CAAX farnesyltransferase subunit alpha; Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha; Ras proteins prenyltransferase subunit alpha; Type I protein geranyl-geranyltransferase subunit alpha; FTase-alpha; GGTase-I-alpha; FNTA DEFNVD7 UC FNTA_HUMAN DEFNVD7 RD SQ-32709 DEFNVD7 GI 2339 DEFNVD7 E1 2: Transferase DEFNVD7 E2 2.5: Alkyl/aryl transferase DEFNVD7 E3 2.5.1: Alkyl/aryl transferase DEFNVD7 EC 2.5.1.58 DEFNVD7 RC Apoptotic cleavage of cellular proteins:R-HSA-111465; Inactivation, recovery and regulation of the phototransduction cascade:R-HSA-2514859 DEFNVD7 KG Terpenoid backbone biosynthesis:hsa00900 DEFNVD7 PD 1LD8; 1MZC; 1S63; 1SA4; 1TN6; 2F0Y; 2H6F; 2H6G; 2H6H DEFNVD7 SQ MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTENDSPTNVQQ DEFNVD7 TD Low tissue/organ specificity. DEFNVD7 FC This enzyme is essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. It contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic- aliphatic-X. DEFNVD7 KD 33208: Metazoa DEFNVD7 PL 7711: Chordata DEFNVD7 CL 40674: Mammalia DEFNVD7 OD 9443: Primates DEFNVD7 FM 9604: Hominidae DEFNVD7 GE 9605: Homo DEFNVD7 SP 9606: Homo sapiens DEBS17P ID DEBS17P DEBS17P DN Phosphoserine aminotransferase (PSAT1) DEBS17P GN PSAT1 DEBS17P SN Phosphohydroxythreonine aminotransferase; PSA; PSAT; PSAT1 DEBS17P UC SERC_HUMAN DEBS17P RD Glyoxylate DEBS17P GI 29968 DEBS17P E1 2: Transferase DEBS17P E2 2.6: Transaminase DEBS17P E3 2.6.1: Transaminase DEBS17P EC 2.6.1.52 DEBS17P RC Serine biosynthesis:R-HSA-977347 DEBS17P KG Biosynthesis of amino acids:hsa01230; Carbon metabolism:hsa01200; Cysteine and methionine metabolism:hsa00270; Glycine, serine and threonine metabolism:hsa00260; Metabolic pathways:hsa01100; Vitamin B6 metabolism:hsa00750 DEBS17P SQ MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLVRELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGTINIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSNFLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLYNTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVCPVEPQNRSKMNIPFRIGNAKGDDALEKRFLDKALELNMLSLKGHRSVGGIRASLYNAVTIEDVQKLAAFMKKFLEMHQL DEBS17P TD Primarily distributed in kidney and liver. DEBS17P FC This enzyme catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. DEBS17P KD 33208: Metazoa DEBS17P PL 7711: Chordata DEBS17P CL 40674: Mammalia DEBS17P OD 9443: Primates DEBS17P FM 9604: Hominidae DEBS17P GE 9605: Homo DEBS17P SP 9606: Homo sapiens DER5HFI ID DER5HFI DER5HFI DN Alanine aminotransferase 1 (GPT) DER5HFI GN GPT DER5HFI SN Glutamate pyruvate transaminase 1; Glutamic--alanine transaminase 1; Glutamic--pyruvic transaminase 1; AAT1; ALT1; GPT; GPT 1; GPT1 DER5HFI UC ALAT1_HUMAN DER5HFI RD Glyoxylate DER5HFI GI 2875 DER5HFI E1 2: Transferase DER5HFI E2 2.6: Transaminase DER5HFI E3 2.6.1: Transaminase DER5HFI EC 2.6.1.2 DER5HFI RC Alanine metabolism:R-HSA-8964540 DER5HFI KG 2-Oxocarboxylic acid metabolism:hsa01210; Alanine, aspartate and glutamate metabolism:hsa00250; Arginine biosynthesis:hsa00220; Biosynthesis of amino acids:hsa01230; Carbon metabolism:hsa01200; Metabolic pathways:hsa01100 DER5HFI SQ MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPFTEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSLGAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRTGVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVINPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPYAGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDLVVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQLPPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLLLEKLSRFHAKFTLEYS DER5HFI TD Primarily distributed in liver, kidney, heart and skeletal muscles. DER5HFI FC This enzyme catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. It participates in cellular nitrogen metabolism. DER5HFI KD 33208: Metazoa DER5HFI PL 7711: Chordata DER5HFI CL 40674: Mammalia DER5HFI OD 9443: Primates DER5HFI FM 9604: Hominidae DER5HFI GE 9605: Homo DER5HFI SP 9606: Homo sapiens DECVGJ3 ID DECVGJ3 DECVGJ3 DN Nicotinamide N-methyltransferase (NNMT) DECVGJ3 GN NNMT DECVGJ3 SN Nicotinamide-methyltransferase; Nicotinamide-methyl transferase; Methyl nicotinamide transferase; NNMT DECVGJ3 UC NNMT_HUMAN DECVGJ3 RD Peficitinib DECVGJ3 GI 4837 DECVGJ3 E1 2: Transferase DECVGJ3 E2 2.1: Methylase DECVGJ3 E3 2.1.1: Methyltransferase DECVGJ3 EC 2.1.1.1 DECVGJ3 RC Metabolism of ingested SeMet, Sec, MeSec into H2Se:R-HSA-2408508; Methylation:R-HSA-156581; Nicotinamide salvaging:R-HSA-197264 DECVGJ3 KG Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760 DECVGJ3 PD 2IIP; 3ROD; 5YJF; 6B1A; 6CHH DECVGJ3 SQ MESGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLSRPL DECVGJ3 TD Primarily distributed in liver. Also expressed in kidney, lung, skeletal muscle, placenta and heart. DECVGJ3 FC This enzyme catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is important for biotransformation of many drugs and xenobiotic compounds. DECVGJ3 KD 33208: Metazoa DECVGJ3 PL 7711: Chordata DECVGJ3 CL 40674: Mammalia DECVGJ3 OD 9443: Primates DECVGJ3 FM 9604: Hominidae DECVGJ3 GE 9605: Homo DECVGJ3 SP 9606: Homo sapiens DEA0BDX ID DEA0BDX DEA0BDX DN Matrix metalloproteinase-9 (MMP-9) DEA0BDX GN MMP9 DEA0BDX SN Gelatinase B; 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9; 92 kDa gelatinase; 92 kDa type IV collagenase; CLG4B; GELB; MMP-9; MMP9 DEA0BDX UC MMP9_HUMAN DEA0BDX RD Amylin DEA0BDX GI 4318 DEA0BDX E1 3: Hydrolases DEA0BDX E2 3.4: Peptidase DEA0BDX E3 3.4.24: Metallopeptidase DEA0BDX EC 3.4.24.35 DEA0BDX RC Activation of Matrix Metalloproteinases:R-HSA-1592389; Assembly of collagen fibrils and other multimeric structures:R-HSA-2022090; Collagen degradation:R-HSA-1442490; Degradation of the extracellular matrix:R-HSA-1474228; EPH-ephrin mediated repulsion of cells:R-HSA-3928665; Extra-nuclear estrogen signaling:R-HSA-9009391; Interleukin-4 and Interleukin-13 signaling:R-HSA-6785807; Neutrophil degranulation:R-HSA-6798695; Signaling by SCF-KIT:R-HSA-1433557 DEA0BDX KG Bladder cancer:hsa05219; Endocrine resistance:hsa01522; Estrogen signaling pathway:hsa04915; Fluid shear stress and atherosclerosis:hsa05418; Hepatitis B:hsa05161; IL-17 signaling pathway:hsa04657; Leukocyte transendothelial migration:hsa04670; MicroRNAs in cancer:hsa05206; Pathways in cancer:hsa05200; Prostate cancer:hsa05215; Proteoglycans in cancer:hsa05205; Relaxin signaling pathway:hsa04926; TNF signaling pathway:hsa04668; Transcriptional misregulation in cancer:hsa05202 DEA0BDX PD 1ITV; 1L6J; 1LKG; 2OVX; 2OVZ; 2OW0; 2OW1; 2OW2; 4H1Q DEA0BDX SQ MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED DEA0BDX TD Primarily distributed in adipose tissue, blood, bone marrow and lymphoid tissue. DEA0BDX FC This enzyme cleaves KiSS1 at a Gly-|-Leu bond and cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments.It also degrades fibronectin but not laminin or Pz-peptide. DEA0BDX KD 33208: Metazoa DEA0BDX PL 7711: Chordata DEA0BDX CL 40674: Mammalia DEA0BDX OD 9443: Primates DEA0BDX FM 9604: Hominidae DEA0BDX GE 9605: Homo DEA0BDX SP 9606: Homo sapiens DEA3VM1 ID DEA3VM1 DEA3VM1 DN Phosphoglucomutase 1 (PGM1) DEA3VM1 GN PGM1 DEA3VM1 SN Glucose phosphomutase 1; Phosphoglucomutase-1; PGM 1; PGM1 DEA3VM1 UC PGM1_HUMAN DEA3VM1 RD Human calcitonin DEA3VM1 GI 5236 DEA3VM1 E1 5: Isomerase DEA3VM1 E2 5.4: Mutase DEA3VM1 E3 5.4.2: Phosphomutase DEA3VM1 EC 5.4.2.2 DEA3VM1 RC Defective PGM1 causes PGM1-CDG (CDG1t):R-HSA-5609974; Glycogen synthesis:R-HSA-3322077; Neutrophil degranulation:R-HSA-6798695 DEA3VM1 KG Amino sugar and nucleotide sugar metabolism:hsa00520; Galactose metabolism:hsa00052; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100; Pentose phosphate pathway:hsa00030; Purine metabolism:hsa00230; Starch and sucrose metabolism:hsa00500 DEA3VM1 PD 5EPC; 5F9C; 5HSH; 5JN5; 5VBI; 5VEC; 5VG7; 5VIN; 6BJ0 DEA3VM1 SQ MVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAVCPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVASATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWQKYGRNFFTRYDYEEVEAEGANKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISRNQGLRLIFTDGSRIVFRLSGTGSAGATIRLYIDSYEKDVAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT DEA3VM1 TD Primarily distributed in skeletal. DEA3VM1 FC This enzyme participates in both the breakdown and synthesis of glucose. DEA3VM1 KD 33208: Metazoa DEA3VM1 PL 7711: Chordata DEA3VM1 CL 40674: Mammalia DEA3VM1 OD 9443: Primates DEA3VM1 FM 9604: Hominidae DEA3VM1 GE 9605: Homo DEA3VM1 SP 9606: Homo sapiens DEJHG19 ID DEJHG19 DEJHG19 DN Peroxisomal multifunctional enzyme 2 (HSD17B4) DEJHG19 GN HSD17B4 DEJHG19 SN Peroxisomal multifunctional enzyme type 2; (3R)-hydroxyacyl-CoA dehydrogenase; 17-beta-HSD 4; 17-beta-hydroxysteroid dehydrogenase 4; 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase; D-bifunctional protein; Enoyl-CoA hydratase 2; Multifunctional protein 2; SDR8C1; Short chain dehydrogenase/reductase family 8C member 1; DBP; EDH17B4; HSD17B4; MFE-2; MPF-2 DEJHG19 UC DHB4_HUMAN DEJHG19 RD Estrone DEJHG19 GI 3295 DEJHG19 E1 4: Lyases DEJHG19 E2 4.2: Carbon-oxygen lyase DEJHG19 E3 4.2.1: Hydro-lyase DEJHG19 EC 4.2.1.119 DEJHG19 RC Beta-oxidation of pristanoyl-CoA:R-HSA-389887; Beta-oxidation of very long chain fatty acids:R-HSA-390247; Peroxisomal protein import:R-HSA-9033241; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368; TYSND1 cleaves peroxisomal proteins:R-HSA-9033500; alpha-linolenic acid (ALA) metabolism:R-HSA-2046106 DEJHG19 KG Biosynthesis of unsaturated fatty acids:hsa01040; Fatty acid metabolism:hsa01212; Metabolic pathways:hsa01100; Peroxisome:hsa04146; Primary bile acid biosynthesis:hsa00120 DEJHG19 PD 1IKT; 1S9C; 1ZBQ DEJHG19 SQ MGSPLRFDGRVVLVTGAGAGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSLAADKVVEEIRRRGGKAVANYDSVEEGEKVVKTALDAFGRIDVVVNNAGILRDRSFARISDEDWDIIHRVHLRGSFQVTRAAWEHMKKQKYGRIIMTSSASGIYGNFGQANYSAAKLGLLGLANSLAIEGRKSNIHCNTIAPNAGSRMTQTVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRQKNHPMTPEAVKANWKKICDFENASKPQSIQESTGSIIEVLSKIDSEGGVSANHTSRATSTATSGFAGAIGQKLPPFSYAYTELEAIMYALGVGASIKDPKDLKFIYEGSSDFSCLPTFGVIIGQKSMMGGGLAEIPGLSINFAKVLHGEQYLELYKPLPRAGKLKCEAVVADVLDKGSGVVIIMDVYSYSEKELICHNQFSLFLVGSGGFGGKRTSDKVKVAVAIPNRPPDAVLTDTTSLNQAALYRLSGDWNPLHIDPNFASLAGFDKPILHGLCTFGFSARRVLQQFADNDVSRFKAIKARFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLAPTSGTSAKTPSEGGKLQSTFVFEEIGRRLKDIGPEVVKKVNAVFEWHITKGGNIGAKWTIDLKSGSGKVYQGPAKGAADTTIILSDEDFMEVVLGKLDPQKAFFSGRLKARGNIMLSQKLQMILKDYAKL DEJHG19 TD Primarily distributed in liver, heart, prostate and testis. DEJHG19 FC This enzyme acts on the peroxisomal beta-oxidation pathway for fatty acids and catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids. DEJHG19 KD 33208: Metazoa DEJHG19 PL 7711: Chordata DEJHG19 CL 40674: Mammalia DEJHG19 OD 9443: Primates DEJHG19 FM 9604: Hominidae DEJHG19 GE 9605: Homo DEJHG19 SP 9606: Homo sapiens DE5UC73 ID DE5UC73 DE5UC73 DN Glutamine synthetase (GLUL) DE5UC73 GN GLUL DE5UC73 SN Palmitoyltransferase GLUL; Glutamate--ammonia ligase; GLNS; GLUL; GS DE5UC73 UC GLNA_HUMAN DE5UC73 RD Ammonia DE5UC73 GI 2752 DE5UC73 E1 6: Ligase DE5UC73 E2 6.3: Carbon-nitrogen ligase DE5UC73 E3 6.3.1: Amide synthase DE5UC73 EC 6.3.1.2 DE5UC73 RC Astrocytic Glutamate-Glutamine Uptake And Metabolism:R-HSA-210455; Glutamate and glutamine metabolism:R-HSA-8964539 DE5UC73 KG Alanine, aspartate and glutamate metabolism:hsa00250; Arginine biosynthesis:hsa00220; Biosynthesis of amino acids:hsa01230; GABAergic synapse:hsa04727; Glutamatergic synapse:hsa04724; Glyoxylate and dicarboxylate metabolism:hsa00630; Metabolic pathways:hsa01100; Necroptosis:hsa04217; Nitrogen metabolism:hsa00910 DE5UC73 PD 2OJW; 2QC8 DE5UC73 SQ MTTSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPKCVEELPEWNFDGSSTLQSEGSNSDMYLVPAAMFRDPFRKDPNKLVLCEVFKYNRRPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADRAYGRDIVEAHYRACLYAGVKIAGTNAEVMPAQWEFQIGPCEGISMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRSASIRIPRTVGQEKKGYFEDRRPSANCDPFSVTEALIRTCLLNETGDEPFQYKN DE5UC73 TD Low tissue/organ specificity. DE5UC73 FC This enzyme catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia. DE5UC73 KD 33208: Metazoa DE5UC73 PL 7711: Chordata DE5UC73 CL 40674: Mammalia DE5UC73 OD 9443: Primates DE5UC73 FM 9604: Hominidae DE5UC73 GE 9605: Homo DE5UC73 SP 9606: Homo sapiens DE4A3BL ID DE4A3BL DE4A3BL DN Diaphorase-1 (CYB5R3) DE4A3BL GN CYB5R3 DE4A3BL SN Cytochrome b5 reductase; NADH-cytochrome b5 reductase 3; NADH-cytochrome b5 reductase 3 membrane-bound form; NADH-cytochrome b5 reductase 3 soluble form; B5R; CYB5R3; DIA1 DE4A3BL UC NB5R3_HUMAN DE4A3BL RD Dihydrocozymase DE4A3BL GI 1727 DE4A3BL E1 1: Oxidoreductase DE4A3BL E2 1.6: NADH/NADPH oxidoreductase DE4A3BL E3 1.6.2: Heme protein acceptor oxidoreductase DE4A3BL EC 1.6.2.2 DE4A3BL RC Neutrophil degranulation:R-HSA-6798695; Phase I - Functionalization of compounds:R-HSA-211945; Vitamin C (ascorbate) metabolism:R-HSA-196836 DE4A3BL KG Amino sugar and nucleotide sugar metabolism:hsa00520 DE4A3BL PD 1M91; 1UMK DE4A3BL SQ MGAQLSTLGHMVLFPVWFLYSLLMKLFQRSTPAITLESPDIKYPLRLIDREIISHDTRRFRFALPSPQHILGLPVGQHIYLSARIDGNLVVRPYTPISSDDDKGFVDLVIKVYFKDTHPKFPAGGKMSQYLESMQIGDTIEFRGPSGLLVYQGKGKFAIRPDKKSNPIIRTVKSVGMIAGGTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNKHSARFKLWYTLDRAPEAWDYGQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLDHVGHPTERCFVF DE4A3BL TD Low tissue/organ specificity. DE4A3BL FC This enzyme is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. DE4A3BL KD 33208: Metazoa DE4A3BL PL 7711: Chordata DE4A3BL CL 40674: Mammalia DE4A3BL OD 9443: Primates DE4A3BL FM 9604: Hominidae DE4A3BL GE 9605: Homo DE4A3BL SP 9606: Homo sapiens DE2WSAL ID DE2WSAL DE2WSAL DN Purine nucleoside phosphorylase (PNP) DE2WSAL GN PNP DE2WSAL SN Inosine-guanosine phosphorylase; Inosine phosphorylase; NP; PNP DE2WSAL UC PNPH_HUMAN DE2WSAL RD Ribavirin DE2WSAL GI 4860 DE2WSAL E1 2: Transferase DE2WSAL E2 2.4: Glycosyltransferases DE2WSAL E3 2.4.2: Pentosyltransferase DE2WSAL EC 2.4.2.1 DE2WSAL RC Neutrophil degranulation:R-HSA-6798695; Purine catabolism:R-HSA-74259; Purine salvage:R-HSA-74217 DE2WSAL KG Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760; Purine metabolism:hsa00230; Pyrimidine metabolism:hsa00240 DE2WSAL PD 1PWY; 1RCT; 1RFG; 1RR6; 1RSZ; 1RT9; 1ULA; 1ULB; 1V2H DE2WSAL SQ MENGYTYEDYKNTAEWLLSHTKHRPQVAIICGSGLGGLTDKLTQAQIFDYGEIPNFPRSTVPGHAGRLVFGFLNGRACVMMQGRFHMYEGYPLWKVTFPVRVFHLLGVDTLVVTNAAGGLNPKFEVGDIMLIRDHINLPGFSGQNPLRGPNDERFGDRFPAMSDAYDRTMRQRALSTWKQMGEQRELQEGTYVMVAGPSFETVAECRVLQKLGADAVGMSTVPEVIVARHCGLRVFGFSLITNKVIMDYESLEKANHEEVLAAGKQAAQKLEQFVSILMASIPLPDKAS DE2WSAL TD Primarily distributed in epididymis. DE2WSAL FC This enzyme catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. DE2WSAL KD 33208: Metazoa DE2WSAL PL 7711: Chordata DE2WSAL CL 40674: Mammalia DE2WSAL OD 9443: Primates DE2WSAL FM 9604: Hominidae DE2WSAL GE 9605: Homo DE2WSAL SP 9606: Homo sapiens DEOT0QC ID DEOT0QC DEOT0QC DN Methylarsonite methyltransferase N6AMT1 (N6AMT1) DEOT0QC GN N6AMT1 DEOT0QC SN Methyltransferase N6AMT1; N(6)-adenine-specific DNA methyltransferase 1; N(5)-glutamine methyltransferase; HemK methyltransferase family member 2; M.HsaHemK2P; C21orf127; HEMK2; N6AMT1; PRED28 DEOT0QC UC N6MT1_HUMAN DEOT0QC RD Arsenic DEOT0QC GI 29104 DEOT0QC E1 2: Transferase DEOT0QC E2 2.1: Methylase DEOT0QC E3 2.1.1: Methyltransferase DEOT0QC EC 2.1.1.72 DEOT0QC RC Eukaryotic Translation Termination:R-HSA-72764; Methylation:R-HSA-156581 DEOT0QC PD 6H1D; 6H1E; 6K0X; 6KMR; 6KMS; 6PED DEOT0QC SQ MAGENFATPFHGHVGRGAFSDVYEPAEDTFLLLDALEAAAAELAGVEICLEVGSGSGVVSAFLASMIGPQALYMCTDINPEAAACTLETARCNKVHIQPVITDLVKGLLPRLTEKVDLLVFNPPYVVTPPQEVGSHGIEAAWAGGRNGREVMDRFFPLVPDLLSPRGLFYLVTIKENNPEEILKIMKTKGLQGTTALSRQAGQETLSVLKFTKS DEOT0QC TD Primarily distributed in parathyroid and pituitary glands. DEOT0QC FC This enzyme can methylate both proteins and DNA, and to a lower extent, arsenic. Its catalytic subunit of a heterodimer with TRMT112, which catalyzes N5-methylation of Glu residue of proteins with a Gly- Gln-Xaa-Xaa-Xaa-Arg motif. It also methylates ETF1 on 'Gln-185' and acts as a N(6)-adenine-specific DNA methyltransferase by mediating methylation of DNA on the 6th position of adenine (N(6)- methyladenosine). It may also play a role in the modulation of arsenic-induced toxicity by mediating the conversion of monomethylarsonous acid (3+) into the less toxic dimethylarsonic acid. It however only plays a limited role in arsenic metabolism compared with AS3MT. DEOT0QC KD 33208: Metazoa DEOT0QC PL 7711: Chordata DEOT0QC CL 40674: Mammalia DEOT0QC OD 9443: Primates DEOT0QC FM 9604: Hominidae DEOT0QC GE 9605: Homo DEOT0QC SP 9606: Homo sapiens DEVRYQN ID DEVRYQN DEVRYQN DN Vitamin K1 2,3-epoxide reductase 1 (VKOR) DEVRYQN GN VKORC1 DEVRYQN SN Vitamin K epoxide reductase complex subunit 1; Vitamin K1 2,3-epoxide reductase subunit 1; MSTP134; MSTP576; UNQ308/PRO351; VKOR; VKORC1 DEVRYQN UC VKOR1_HUMAN DEVRYQN RD Kappadione DEVRYQN GI 79001 DEVRYQN E1 1: Oxidoreductase DEVRYQN E2 1.17: CH/CH2 oxidoreductase DEVRYQN E3 1.17.4: Disulfide acceptor oxidoreductase DEVRYQN EC 1.17.4.4 DEVRYQN RC Metabolism of vitamin K:R-HSA-6806664 DEVRYQN KG Metabolic pathways:hsa01100; Ubiquinone and other terpenoid-quinone biosynthesis:hsa00130 DEVRYQN SQ MGSTWGSPGWVRLALCLTGLVLSLYALHVKAARARDRDYRALCDVGTAISCSRVFSSRWGRGFGLVEHVLGQDSILNQSNSIFGCIFYTLQLLLGCLRTRWASVLMLLSSLVSLAGSVYLAWILFFVLYDFCIVCITTYAINVSLMWLSFRKVQEPQGKAKRH DEVRYQN TD Primarily distributed in liver. Also expressed in fetal heart, kidney, lung, adult heart and pancreas. DEVRYQN FC This enzyme is involved in vitamin K metabolism. Its catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. DEVRYQN KD 33208: Metazoa DEVRYQN PL 7711: Chordata DEVRYQN CL 40674: Mammalia DEVRYQN OD 9443: Primates DEVRYQN FM 9604: Hominidae DEVRYQN GE 9605: Homo DEVRYQN SP 9606: Homo sapiens DERBKPU ID DERBKPU DERBKPU DN Nicotinate-nucleotide adenylyltransferase 3 (NMNAT3) DERBKPU GN NMNAT3 DERBKPU SN NMN adenylyltransferase 3; NMN/NaMN adenylyltransferase 3; NMNAT3; NaMN adenylyltransferase 3; Nicotinamide-nucleotide adenylyltransferase 3; Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3; Pyridine nucleotide adenylyltransferase 3; FKSG76; PNAT-3 DERBKPU UC NMNA3_HUMAN DERBKPU RD NMN zwitterion DERBKPU GI 349565 DERBKPU E1 2: Transferase DERBKPU E2 2.7: Kinase DERBKPU E3 2.7.7: Nucleotidyltransferase DERBKPU EC 2.7.7.1 DERBKPU RC Nicotinate metabolism:R-HSA-196807 DERBKPU KG Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760 DERBKPU PD 1NUP; 1NUQ; 1NUR; 1NUS; 1NUT; 1NUU DERBKPU SQ MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWKGKSTQSTEGKTS DERBKPU TD Primarily distributed in lung and spleen. Also expressed in placenta and kidney. DERBKPU FC This enzyme catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. It can use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency and can use triazofurin monophosphate (TrMP) as substrate. It can also use GTP and ITP as nucleotide donors. It catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, it can use NAD(+), NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. DERBKPU KD 33208: Metazoa DERBKPU PL 7711: Chordata DERBKPU CL 40674: Mammalia DERBKPU OD 9443: Primates DERBKPU FM 9604: Hominidae DERBKPU GE 9605: Homo DERBKPU SP 9606: Homo sapiens DEROYHE ID DEROYHE DEROYHE DN N-acetyl-D-glucosamine 2-epimerase (AGE) DEROYHE GN RENBP DEROYHE SN GlcNAc 2-epimerase; N-acylglucosamine 2-epimerase; Renin-binding protein; RnBP; AGE; RENBP DEROYHE UC RENBP_HUMAN DEROYHE RD FT-0661285 DEROYHE GI 5973 DEROYHE E1 5: Isomerase DEROYHE E2 5.1: Racemase/epimerase DEROYHE E3 5.1.3: Carbohydrate racemase/epimerase DEROYHE EC 5.1.3.8 DEROYHE RC Synthesis of UDP-N-acetyl-glucosamine:R-HSA-446210 DEROYHE KG Amino sugar and nucleotide sugar metabolism:hsa00520; Metabolic pathways:hsa01100 DEROYHE SQ MSKGLPARQDMEKERETLQAWKERVGQELDRVVAFWMEHSHDQEHGGFFTCLGREGRVYDDLKYVWLQGRQVWMYCRLYRTFERFRHAQLLDAAKAGGEFLLRYARVAPPGKKCAFVLTRDGRPVKVQRTIFSECFYTMAMNELWRATGEVRYQTEAVEMMDQIVHWVQEDASGLGRPQLQGAPAAEPMAVPMMLLNLVEQLGEADEELAGKYAELGDWCARRILQHVQRDGQAVLENVSEGGKELPGCLGRQQNPGHTLEAGWFLLRHCIRKGDPELRAHVIDKFLLLPFHSGWDPDHGGLFYFQDADNFCPTQLEWAMKLWWPHSEAMIAFLMGYSDSGDPVLLRLFYQVAEYTFRQFRDPEYGEWFGYLSREGKVALSIKGGPFKGCFHVPRCLAMCEEMLGALLSRPAPAPSPAPTPACRGAE DEROYHE TD Primarily distributed in kidney and lymphoid tissue. DEROYHE FC This enzyme catalyzes the interconversion of N-acetylglucosamine to N- acetylmannosamine. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. DEROYHE KD 33208: Metazoa DEROYHE PL 7711: Chordata DEROYHE CL 40674: Mammalia DEROYHE OD 9443: Primates DEROYHE FM 9604: Hominidae DEROYHE GE 9605: Homo DEROYHE SP 9606: Homo sapiens DEJ73Q9 ID DEJ73Q9 DEJ73Q9 DN Dimethylaniline oxidase 1 (FMO1) DEJ73Q9 GN FMO1 DEJ73Q9 SN Dimethylaniline monooxygenase [N-oxide-forming] 1; FMO 1; FMO1; Fetal hepatic flavin-containing monooxygenase 1 DEJ73Q9 UC FMO1_HUMAN DEJ73Q9 RD Dapoxetine DEJ73Q9 GI 2326 DEJ73Q9 E1 1: Oxidoreductase DEJ73Q9 E2 1.14: Oxygen paired donor oxidoreductase DEJ73Q9 E3 1.14.13: NADH/NADPH donor oxidoreductase DEJ73Q9 EC 1.14.13.8 DEJ73Q9 RC FMO oxidises nucleophiles:R-HSA-217271 DEJ73Q9 KG Drug metabolism - cytochrome P450:hsa00982 DEJ73Q9 SQ MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYSDFPFPEDYPNYVPNSQFLEYLKMYANHFDLLKHIQFKTKVCSVTKCSDSAVSGQWEVVTMHEEKQESAIFDAVMVCTGFLTNPYLPLDSFPGINAFKGQYFHSRQYKHPDIFKDKRVLVIGMGNSGTDIAVEASHLAEKVFLSTTGGGWVISRIFDSGYPWDMVFMTRFQNMLRNSLPTPIVTWLMERKINNWLNHANYGLIPEDRTQLKEFVLNDELPGRIITGKVFIRPSIKEVKENSVIFNNTSKEEPIDIIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAIIGLIKPLGSMIPTGETQARWAVRVLKGVNKLPPPSVMIEEINARKENKPSWFGLCYCKALQSDYITYIDELLTYINAKPNLFSMLLTDPHLALTVFFGPCSPYQFRLTGPGKWEGARNAIMTQWDRTFKVIKARVVQESPSPFESFLKVFSFLALLVAIFLIFL DEJ73Q9 TD Primarily distributed in liver and kidney. DEJ73Q9 FC This enzyme is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides and form I catalyzes the N-oxygenation of secondary and tertiary amines. DEJ73Q9 KD 33208: Metazoa DEJ73Q9 PL 7711: Chordata DEJ73Q9 CL 40674: Mammalia DEJ73Q9 OD 9443: Primates DEJ73Q9 FM 9604: Hominidae DEJ73Q9 GE 9605: Homo DEJ73Q9 SP 9606: Homo sapiens DED26GV ID DED26GV DED26GV DN Cytochrome P450 4F12 (CYP4F12) DED26GV GN CYP4F12 DED26GV SN Cytochrome P450 family 4 subfamily F member 12; CYP4F12; CYPIVF12; UNQ568/PRO1129 DED26GV UC CP4FC_HUMAN DED26GV RD Fingolimod DED26GV GI 66002 DED26GV E1 1: Oxidoreductase DED26GV E2 1.14: Oxygen paired donor oxidoreductase DED26GV E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DED26GV EC 1.14.14.1 DED26GV RC Eicosanoids:R-HSA-211979; Fatty acids:R-HSA-211935 DED26GV SQ MSLLSLPWLGLRPVATSPWLLLLLVVGSWLLARILAWTYAFYNNCRRLQCFPQPPKRNWFWGHLGLITPTEEGLKNSTQMSATYSQGFTVWLGPIIPFIVLCHPDTIRSITNASAAIAPKDNLFIRFLKPWLGEGILLSGGDKWSRHRRMLTPAFHFNILKSYITIFNKSANIMLDKWQHLASEGSSRLDMFEHISLMTLDSLQKCIFSFDSHCQERPSEYIATILELSALVEKRSQHILQHMDFLYYLSHDGRRFHRACRLVHDFTDAVIRERRRTLPTQGIDDFFKDKAKSKTLDFIDVLLLSKDEDGKALSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDRDPKEIEWDDLAQLPFLTMCVKESLRLHPPAPFISRCCTQDIVLPDGRVIPKGITCLIDIIGVHHNPTVWPDPEVYDPFRFDPENSKGRSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALMLLHFRFLPDHTEPRRKLELIMRAEGGLWLRVEPLNVSLQ DED26GV TD Primarily distributed in small intestine, liver, colon and heart. DED26GV FC This enzyme is involved in the metabolism of endogenous polyunsaturated fatty acids (PUFAs). It catalyzes the hydroxylation of carbon hydrogen bonds, with preference for omega-2 position and Metabolizes (5Z,8Z,11Z,14Z)- eicosatetraenoic acid (arachidonate) toward 18-hydroxy arachidonate. Besides, it catalyzes the epoxidation of double bonds of PUFAs such as docosapentaenoic and docosahexaenoic acids. It is also involved in the metabolism of xenobiotics and catalyzes the hydroxylation of the antihistamine drug ebastine. DED26GV KD 33208: Metazoa DED26GV PL 7711: Chordata DED26GV CL 40674: Mammalia DED26GV OD 9443: Primates DED26GV FM 9604: Hominidae DED26GV GE 9605: Homo DED26GV SP 9606: Homo sapiens DE6NMGO ID DE6NMGO DE6NMGO DN Cytochrome P450 2S1 (CYP2S1) DE6NMGO GN CYP2S1 DE6NMGO SN Cytochrome P450 family 2 subfamily S member 1; Thromboxane-A synthase; CYP2S1; CYPIIS1; UNQ891/PRO1906 DE6NMGO UC CP2S1_HUMAN DE6NMGO RD NSC-122758 DE6NMGO GI 29785 DE6NMGO E1 1: Oxidoreductase DE6NMGO E2 1.14: Oxygen paired donor oxidoreductase DE6NMGO E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE6NMGO EC 1.14.14.1 DE6NMGO RC CYP2E1 reactions:R-HSA-211999; Miscellaneous substrates:R-HSA-211958; Xenobiotics:R-HSA-211981 DE6NMGO KG Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Retinol metabolism:hsa00830 DE6NMGO SQ MEATGTWALLLALALLLLLTLALSGTRARGHLPPGPTPLPLLGNLLQLRPGALYSGLMRLSKKYGPVFTIYLGPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVSGLFNIPPAFQLQVRPTDLHSTTQTR DE6NMGO TD Primarily distributed in blood, gallbladder, intestine and stomach. DE6NMGO FC This enzyme is involved in the metabolism of retinoids and eicosanoids. In epidermis, it may contribute to the oxidative metabolism of all-trans- retinoic acid. Additionally, it displays peroxidase and isomerase activities toward various oxygenated eicosanoids such as prostaglandin H2 (PGH2) and hydroperoxyeicosatetraenoates (HPETEs). DE6NMGO KD 33208: Metazoa DE6NMGO PL 7711: Chordata DE6NMGO CL 40674: Mammalia DE6NMGO OD 9443: Primates DE6NMGO FM 9604: Hominidae DE6NMGO GE 9605: Homo DE6NMGO SP 9606: Homo sapiens DEXI4UQ ID DEXI4UQ DEXI4UQ DN Aldehyde dehydrogenase 5 (ALDHX) DEXI4UQ GN ALDH1B1 DEXI4UQ SN Aldehyde dehydrogenase 1 family member B1; Mitochondrial aldehyde dehydrogenase X; ALDH1B1; ALDH5; ALDHX DEXI4UQ UC AL1B1_HUMAN DEXI4UQ RD SC-47945 DEXI4UQ GI 219 DEXI4UQ E1 1: Oxidoreductase DEXI4UQ E2 1.2: Aldehyde/oxo donor oxidoreductase DEXI4UQ E3 1.2.1: NAD/NADP acceptor oxidoreductase DEXI4UQ EC 1.2.1.3 DEXI4UQ RC Ethanol oxidation:R-HSA-71384 DEXI4UQ KG Arginine and proline metabolism:hsa00330; Ascorbate and aldarate metabolism:hsa00053; Fatty acid degradation:hsa00071; Glycerolipid metabolism:hsa00561; Glycolysis / Gluconeogenesis:hsa00010; Histidine metabolism:hsa00340; Lysine degradation:hsa00310; Metabolic pathways:hsa01100; Pyruvate metabolism:hsa00620; Tryptophan metabolism:hsa00380; Valine, leucine and isoleucine degradation:hsa00280; beta-Alanine metabolism:hsa00410 DEXI4UQ SQ MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPTTGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLASLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCGQIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITGYGPTAGAAIAQHVDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADMEHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGPQVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGPVQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHTPFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS DEXI4UQ TD Primarily distributed in liver, testis and smooth. DEXI4UQ FC This enzyme plays a major role in the detoxification of alcohol-derived acetaldehyde and is involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. DEXI4UQ KD 33208: Metazoa DEXI4UQ PL 7711: Chordata DEXI4UQ CL 40674: Mammalia DEXI4UQ OD 9443: Primates DEXI4UQ FM 9604: Hominidae DEXI4UQ GE 9605: Homo DEXI4UQ SP 9606: Homo sapiens DEZBN53 ID DEZBN53 DEZBN53 DN Sulfotransferase 2B1 (SULT2B1) DEZBN53 GN SULT2B1 DEZBN53 SN Sulfotransferase family cytosolic 2B member 1; Alcohol sulfotransferase; Hydroxysteroid sulfotransferase 2; Sulfotransferase family 2B member 1; HSST2; ST2B1; SULT2B1 DEZBN53 UC ST2B1_HUMAN DEZBN53 RD Dehydroepiandrosterone DEZBN53 GI 6820 DEZBN53 E1 2: Transferase DEZBN53 E2 2.8: Sulfotransferase DEZBN53 E3 2.8.2: Sulfotransferase DEZBN53 EC 2.8.2.2 DEZBN53 RC Cytosolic sulfonation of small molecules:R-HSA-156584 DEZBN53 KG Steroid hormone biosynthesis:hsa00140 DEZBN53 PD 1Q1Q; 1Q1Z; 1Q20; 1Q22 DEZBN53 SQ MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS DEZBN53 TD Primarily distributed in placenta, prostate, trachea, esophagus, lymphoid tissue and tongue. DEZBN53 FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. It is also responsible for the sulfation of cholesterol. It can catalyze sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA). And it preferentially sulfonates cholesterol, while it has also significant activity with pregnenolone and DHEA. Besides, it plays a role in epidermal cholesterol metabolism. DEZBN53 KD 33208: Metazoa DEZBN53 PL 7711: Chordata DEZBN53 CL 40674: Mammalia DEZBN53 OD 9443: Primates DEZBN53 FM 9604: Hominidae DEZBN53 GE 9605: Homo DEZBN53 SP 9606: Homo sapiens DERZQ2Y ID DERZQ2Y DERZQ2Y DN D-amino-acid oxidase (DAO) DERZQ2Y GN DAO DERZQ2Y SN D-aminoacid oxidase; D-amino acid oxidase; D-AAO; chDAO; DAO1; DAAO; DAMOX; DAO DERZQ2Y UC OXDA_HUMAN DERZQ2Y RD D-Serine DERZQ2Y GI 1610 DERZQ2Y E1 1: Oxidoreductase DERZQ2Y E2 1.4: CH-NH2 donor oxidoreductase DERZQ2Y E3 1.4.3: Oxygen acceptor oxidoreductase DERZQ2Y EC 1.4.3.3 DERZQ2Y RC Glyoxylate metabolism and glycine degradation:R-HSA-389661; Peroxisomal protein import:R-HSA-9033241 DERZQ2Y KG Arginine and proline metabolism:hsa00330; D-Arginine and D-ornithine metabolism:hsa00472; Glycine, serine and threonine metabolism:hsa00260; Metabolic pathways:hsa01100; Peroxisome:hsa04146 DERZQ2Y PD 2E49; 2E4A; 2E82; 2GNZ; 3CUK; 3G3E; 3W4I; 3W4J; 3W4K DERZQ2Y SQ MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPNNPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPRELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVNCTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGGIFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGPSNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL DERZQ2Y TD Primarily distributed in brain, kidney and liver. DERZQ2Y FC This enzyme can act as a detoxifying agent which removes D-amino acids accumulated during aging and acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups and does not act on acidic amino acids. DERZQ2Y KD 33208: Metazoa DERZQ2Y PL 7711: Chordata DERZQ2Y CL 40674: Mammalia DERZQ2Y OD 9443: Primates DERZQ2Y FM 9604: Hominidae DERZQ2Y GE 9605: Homo DERZQ2Y SP 9606: Homo sapiens DE9KJP3 ID DE9KJP3 DE9KJP3 DN Arsenite methyltransferase (AS3MT) DE9KJP3 GN AS3MT DE9KJP3 SN Methylarsonite methyltransferase; S-adenosyl-L-methionine:arsenic(III) methyltransferase; AS3MT; CYT19 DE9KJP3 UC AS3MT_HUMAN DE9KJP3 RD Arsenic DE9KJP3 GI 57412 DE9KJP3 E1 2: Transferase DE9KJP3 E2 2.1: Methylase DE9KJP3 E3 2.1.1: Methyltransferase DE9KJP3 EC 2.1.1.137 DE9KJP3 RC Methylation:R-HSA-156581 DE9KJP3 SQ MAALRDAEIQKDVQTYYGQVLKRSADLQTNGCVTTARPVPKHIREALQNVHEEVALRYYGCGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHMEKYGFQASNVTFIHGYIEKLGEAGIKNESHDIVVSNCVINLVPDKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFCPPRLVTANLITIQNKELERVIGDCRFVSATFRLFKHSKTGPTKRCQVIYNGGITGHEKELMFDANFTFKEGEIVEVDEETAAILKNSRFAQDFLIRPIGEKLPTSGGCSALELKDIITDPFKLAEESDSMKSRCVPDAAGGCCGTKKSC DE9KJP3 TD Primarily distributed in adrenal gland and parathyroid gland. DE9KJP3 FC This enzyme catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH. DE9KJP3 KD 33208: Metazoa DE9KJP3 PL 7711: Chordata DE9KJP3 CL 40674: Mammalia DE9KJP3 OD 9443: Primates DE9KJP3 FM 9604: Hominidae DE9KJP3 GE 9605: Homo DE9KJP3 SP 9606: Homo sapiens DEPWYLT ID DEPWYLT DEPWYLT DN Arginine carboxypeptidase (CPN1) DEPWYLT GN CPN1 DEPWYLT SN Lysine carboxypeptidase; Plasma carboxypeptidase B; ACBP; Anaphylatoxin inactivator; CPN; CPN1; Carboxypeptidase N catalytic chain; Carboxypeptidase N polypeptide 1; Carboxypeptidase N small subunit; Kininase-1; SCPN; Serum carboxypeptidase N DEPWYLT UC CBPN_HUMAN DEPWYLT RD BRS-640 DEPWYLT GI 1369 DEPWYLT E1 3: Hydrolases DEPWYLT E2 3.4: Peptidase DEPWYLT E3 3.4.17: Metallocarboxypeptidase DEPWYLT EC 3.4.17.3 DEPWYLT RC Regulation of Complement cascade:R-HSA-977606 DEPWYLT PD 2NSM DEPWYLT SQ MSDLLSVFLHLLLLFKLVAPVTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLPLPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGWMFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQVHQGIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGPAEPTLVNFHLKRSIPQVSPVRRAPSRRHGVRAKVQPQARKKEMEMRQLQRGPA DEPWYLT TD Primarily distributed in liver. Synthesized in the liver and secreted in plasma. DEPWYLT FC This enzyme protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. DEPWYLT KD 33208: Metazoa DEPWYLT PL 7711: Chordata DEPWYLT CL 40674: Mammalia DEPWYLT OD 9443: Primates DEPWYLT FM 9604: Hominidae DEPWYLT GE 9605: Homo DEPWYLT SP 9606: Homo sapiens DET89OV ID DET89OV DET89OV DN Thyroxine 5-deiodinase (DIO3) DET89OV GN DIO3 DET89OV SN Iodothyronine deiodinase III; Type III iodothyronine deiodinase; Type 3 DI; 5DIII; DIO3; DIOIII; ITDI3; TXDI3 DET89OV UC IOD3_HUMAN DET89OV RD L-thyroxine DET89OV GI 1735 DET89OV E1 1: Oxidoreductase DET89OV E2 1.21: X-H/Y-H oxidoreductase DET89OV E3 1.21.99: X-H/Y-H oxidoreductase DET89OV EC 1.21.99.3 DET89OV RC Regulation of thyroid hormone activity:R-HSA-350864 DET89OV KG Thyroid hormone signaling pathway:hsa04919 DET89OV SQ MPRQATSRLVVGEGEGSQGASGPAATMLRSLLLHSLRLCAQTASCLVLFPRFLGTAFMLWLLDFLCIRKHFLGRRRRGQPEPEVELNSEGEEVPPDDPPICVSDDNRLCTLASLKAVWHGQKLDFFKQAHEGGPAPNSEVVLPDGFQSQHILDYAQGNRPLVLNFGSCTUPPFMARMSAFQRLVTKYQRDVDFLIIYIEEAHPSDGWVTTDSPYIIPQHRSLEDRVSAARVLQQGAPGCALVLDTMANSSSSAYGAYFERLYVIQSGTIMYQGGRGPDGYQVSELRTWLERYDEQLHGARPRRV DET89OV TD Primarily distributed in cervix, uterine and placenta. DET89OV FC This enzyme is responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. DET89OV KD 33208: Metazoa DET89OV PL 7711: Chordata DET89OV CL 40674: Mammalia DET89OV OD 9443: Primates DET89OV FM 9604: Hominidae DET89OV GE 9605: Homo DET89OV SP 9606: Homo sapiens DEX8J7E ID DEX8J7E DEX8J7E DN Testicular 17-beta-hydroxysteroid dehydrogenase (HSD17B3) DEX8J7E GN HSD17B3 DEX8J7E SN Testosterone 17-beta-dehydrogenase 3; 17-beta-HSD 3; 17-beta-hydroxysteroid dehydrogenase type 3; Short chain dehydrogenase/reductase family 12C member 2; EDH17B3; HSD17B3; SDR12C2 DEX8J7E UC DHB3_HUMAN DEX8J7E RD Androstenedione DEX8J7E GI 3293 DEX8J7E E1 1: Oxidoreductase DEX8J7E E2 1.1: CH-OH donor oxidoreductase DEX8J7E E3 1.1.1: NAD/NADP oxidoreductase DEX8J7E EC 1.1.1.64 DEX8J7E RC Androgen biosynthesis:R-HSA-193048; Synthesis of very long-chain fatty acyl-CoAs:R-HSA-75876 DEX8J7E KG Metabolic pathways:hsa01100; Steroid hormone biosynthesis:hsa00140 DEX8J7E SQ MGDVLEQFFILTGLLVCLACLAKCVRFSRCVLLNYWKVLPKSFLRSMGQWAVITGAGDGIGKAYSFELAKRGLNVVLISRTLEKLEAIATEIERTTGRSVKIIQADFTKDDIYEHIKEKLAGLEIGILVNNVGMLPNLLPSHFLNAPDEIQSLIHCNITSVVKMTQLILKHMESRQKGLILNISSGIALFPWPLYSMYSASKAFVCAFSKALQEEYKAKEVIIQVLTPYAVSTAMTKYLNTNVITKTADEFVKESLNYVTIGGETCGCLAHEILAGFLSLIPAWAFYSGAFQRLLLTHYVAYLKLNTKVR DEX8J7E TD Primarily distributed in testis. DEX8J7E FC This enzyme favors the reduction of androstenedione to testosterone. DEX8J7E KD 33208: Metazoa DEX8J7E PL 7711: Chordata DEX8J7E CL 40674: Mammalia DEX8J7E OD 9443: Primates DEX8J7E FM 9604: Hominidae DEX8J7E GE 9605: Homo DEX8J7E SP 9606: Homo sapiens DEZT8FM ID DEZT8FM DEZT8FM DN Retinoic acid 4-hydroxylase 26B1 (CYP26B1) DEZT8FM GN CYP26B1 DEZT8FM SN Cytochrome P450 26A2; Cytochrome P450 26B1; Cytochrome P450 retinoic acid-inactivating 2; Cytochrome P450RAI-2; CYP26A2; CYP26B1; P450RAI2 DEZT8FM UC CP26B_HUMAN DEZT8FM RD Etretinate DEZT8FM GI 56603 DEZT8FM E1 1: Oxidoreductase DEZT8FM E2 1.14: Oxygen paired donor oxidoreductase DEZT8FM E3 1.14.13: NADH/NADPH donor oxidoreductase DEZT8FM EC 1.14.13.- DEZT8FM RC Defective CYP26B1 causes Radiohumeral fusions with other skeletal and craniofacial anomalies (RHFCA):R-HSA-5579015; RA biosynthesis pathway:R-HSA-5365859; Vitamins:R-HSA-211916 DEZT8FM KG Metabolic pathways:hsa01100; Retinol metabolism:hsa00830 DEZT8FM SQ MLFEGLDLVSALATLAACLVSVTLLLAVSQQLWQLRWAATRDKSCKLPIPKGSMGFPLIGETGHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILMGEHHLVSTEWPRSTRMLLGPNTVSNSIGDIHRNKRKVFSKIFSHEALESYLPKIQLVIQDTLRAWSSHPEAINVYQEAQKLTFRMAIRVLLGFSIPEEDLGHLFEVYQQFVDNVFSLPVDLPFSGYRRGIQARQILQKGLEKAIREKLQCTQGKDYLDALDLLIESSKEHGKEMTMQELKDGTLELIFAAYATTASASTSLIMQLLKHPTVLEKLRDELRAHGILHSGGCPCEGTLRLDTLSGLRYLDCVIKEVMRLFTPISGGYRTVLQTFELDGFQIPKGWSVMYSIRDTHDTAPVFKDVNVFDPDRFSQARSEDKDGRFHYLPFGGGVRTCLGKHLAKLFLKVLAVELASTSRFELATRTFPRITLVPVLHPVDGLSVKFFGLDSNQNEILPETEAMLSATV DEZT8FM TD Primarily distributed in brain, particularly in thecerebellum and pons. DEZT8FM FC This enzyme is involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation. It is also involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates: all-trans-RA > 9-cis-RA > 13- cis-RA. It generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH-RA. It catalyzes the hydroxylation of carbon hydrogen bonds of atRA primarily at C-4. It also has a significant activity in oxidation of tazarotenic acid and may therefore metabolize that xenobiotic in vivo. DEZT8FM KD 33208: Metazoa DEZT8FM PL 7711: Chordata DEZT8FM CL 40674: Mammalia DEZT8FM OD 9443: Primates DEZT8FM FM 9604: Hominidae DEZT8FM GE 9605: Homo DEZT8FM SP 9606: Homo sapiens DE915QP ID DE915QP DE915QP DN Ketoacyl-CoA reductase (HSD17B12) DE915QP GN HSD17B12 DE915QP SN Very-long-chain 3-oxoacyl-CoA reductase; Short chain dehydrogenase/reductase family 12C member 1; 17-beta-HSD 12; 17-beta-hydroxysteroid dehydrogenase 12; 3-ketoacyl-CoA reductase; Estradiol 17-beta-dehydrogenase 12; HSD17B12; KAR; SDR12C1 DE915QP UC DHB12_HUMAN DE915QP RD Estrone DE915QP GI 51144 DE915QP E1 1: Oxidoreductase DE915QP E2 1.1: CH-OH donor oxidoreductase DE915QP E3 1.1.1: NAD/NADP oxidoreductase DE915QP EC 1.1.1.330 DE915QP RC Androgen biosynthesis:R-HSA-193048; Synthesis of very long-chain fatty acyl-CoAs:R-HSA-75876 DE915QP KG Biosynthesis of unsaturated fatty acids:hsa01040; Fatty acid elongation:hsa00062; Fatty acid metabolism:hsa01212; Metabolic pathways:hsa01100; Steroid hormone biosynthesis:hsa00140 DE915QP SQ MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGSTDGIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKTGLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERSKGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLAKIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWIYLKIVMNMNKSTRAHYLKKTKKN DE915QP TD Primarily distributed in ovary and mammary. DE915QP FC This enzyme catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3- hydroxyacyl-CoA, within each cycle of fatty acid elongation. It may also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation. DE915QP KD 33208: Metazoa DE915QP PL 7711: Chordata DE915QP CL 40674: Mammalia DE915QP OD 9443: Primates DE915QP FM 9604: Hominidae DE915QP GE 9605: Homo DE915QP SP 9606: Homo sapiens DEGSPC9 ID DEGSPC9 DEGSPC9 DN Hydroxyacyl-CoA dehydrogenase 2 (HSD17B10) DEGSPC9 GN HSD17B10 DEGSPC9 SN Endoplasmic reticulum-associated amyloid beta-peptide-binding protein; 17-beta-hydroxysteroid dehydrogenase 10; 2-methyl-3-hydroxybutyryl-CoA dehydrogenase; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 3-hydroxyacyl-CoA dehydrogenase type II; 3-hydroxyacyl-CoA dehydrogenase type-2; Mitochondrial RNase P protein 2; Mitochondrial ribonuclease P protein 2; Short chain dehydrogenase/reductase family 5C member 1; Short-chain type dehydrogenase/reductase XH98G2; Type II HADH; 17-beta-HSD 10; XH98G2; ERAB; HADH2; HSD17B10; MHBD; MRPP2; SCHAD; SDR5C1 DEGSPC9 UC HCD2_HUMAN DEGSPC9 RD Dihydrocozymase DEGSPC9 GI 3028 DEGSPC9 E1 1: Oxidoreductase DEGSPC9 E2 1.1: CH-OH donor oxidoreductase DEGSPC9 E3 1.1.1: NAD/NADP oxidoreductase DEGSPC9 EC 1.1.1.35 DEGSPC9 RC Branched-chain amino acid catabolism:R-HSA-70895; rRNA processing in the mitochondrion:R-HSA-8868766; tRNA modification in the mitochondrion:R-HSA-6787450; tRNA processing in the mitochondrion:R-HSA-6785470 DEGSPC9 KG Alzheimer's disease:hsa05010; Metabolic pathways:hsa01100; Valine, leucine and isoleucine degradation:hsa00280 DEGSPC9 PD 1F67; 1SO8; 1U7T; 2O23 DEGSPC9 SQ MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVIRLDGAIRMQP DEGSPC9 TD Low tissue/organ specificity. DEGSPC9 FC This enzyme catalyzes the beta-oxidation at position 17 of androgens and estrogens and has 3-alpha- hydroxysteroid dehydrogenase activity with androsterone. It catalyzes the third step in the beta-oxidation of fatty acids and carries out oxidative conversions of 7-alpha-OH and 7-beta-OH bile acids. It also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. DEGSPC9 KD 33208: Metazoa DEGSPC9 PL 7711: Chordata DEGSPC9 CL 40674: Mammalia DEGSPC9 OD 9443: Primates DEGSPC9 FM 9604: Hominidae DEGSPC9 GE 9605: Homo DEGSPC9 SP 9606: Homo sapiens DE4E31Z ID DE4E31Z DE4E31Z DN Deoxy-5'-nucleotidase 1 (NT5C) DE4E31Z GN NT5C DE4E31Z SN Cytosolic 5'(3')-deoxyribonucleotidase; Cytosolic 5',3'-pyrimidine nucleotidase; DNT1; NT5C; UMPH2; dNT-1 DE4E31Z UC NT5C_HUMAN DE4E31Z RD Lamivudine DE4E31Z GI 30833 DE4E31Z E1 3: Hydrolases DE4E31Z E2 3.1: Ester bond hydrolase DE4E31Z E3 3.1.3: Phosphoric monoester hydrolase DE4E31Z EC 3.1.3.5 DE4E31Z RC Purine catabolism:R-HSA-74259; Pyrimidine catabolism:R-HSA-73621 DE4E31Z KG Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760; Purine metabolism:hsa00230; Pyrimidine metabolism:hsa00240 DE4E31Z PD 2I7D; 4L57; 4YIH; 6G2N DE4E31Z SQ MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADKVASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRLLSWSDNWREILDSKRGAAQRE DE4E31Z TD Low tissue/organ specificity. DE4E31Z FC This enzyme dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP. DE4E31Z KD 33208: Metazoa DE4E31Z PL 7711: Chordata DE4E31Z CL 40674: Mammalia DE4E31Z OD 9443: Primates DE4E31Z FM 9604: Hominidae DE4E31Z GE 9605: Homo DE4E31Z SP 9606: Homo sapiens DEQIZP2 ID DEQIZP2 DEQIZP2 DN Chondroitin 6-sulfotransferase (CHST3) DEQIZP2 GN CHST3 DEQIZP2 SN Carbohydrate sulfotransferase 3; Chondroitin 6-O-sulfotransferase 1; Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0; C6ST-1; CHST3; GST-0 DEQIZP2 UC CHST3_HUMAN DEQIZP2 RD Chondroitin sulfate DEQIZP2 GI 9469 DEQIZP2 E1 2: Transferase DEQIZP2 E2 2.8: Sulfotransferase DEQIZP2 E3 2.8.2: Sulfotransferase DEQIZP2 EC 2.8.2.17 DEQIZP2 RC Chondroitin sulfate biosynthesis:R-HSA-2022870; Defective CHST3 causes SEDCJD:R-HSA-3595172 DEQIZP2 KG Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate:hsa00532 DEQIZP2 SQ MEKGLTLPQDCRDFVHSLKMRSKYALFLVFVVIVFVFIEKENKIISRVSDKLKQIPQALADANSTDPALILAENASLLSLSELDSAFSQLQSRLRNLSLQLGVEPAMEAAGEEEEEQRKEEEPPRPAVAGPRRHVLLMATTRTGSSFVGEFFNQQGNIFYLFEPLWHIERTVSFEPGGANAAGSALVYRDVLKQLFLCDLYVLEHFITPLPEDHLTQFMFRRGSSRSLCEDPVCTPFVKKVFEKYHCKNRRCGPLNVTLAAEACRRKEHMALKAVRIRQLEFLQPLAEDPRLDLRVIQLVRDPRAVLASRMVAFAGKYKTWKKWLDDEGQDGLREEEVQRLRGNCESIRLSAELGLRQPAWLRGRYMLVRYEDVARGPLQKAREMYRFAGIPLTPQVEDWIQKNTQAAHDGSGIYSTQKNSSEQFEKWRFSMPFKLAQVVQAACGPAMRLFGYKLARDAAALTNRSVSLLEERGTFWVT DEQIZP2 TD Low tissue/organ specificity. DEQIZP2 FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. DEQIZP2 KD 33208: Metazoa DEQIZP2 PL 7711: Chordata DEQIZP2 CL 40674: Mammalia DEQIZP2 OD 9443: Primates DEQIZP2 FM 9604: Hominidae DEQIZP2 GE 9605: Homo DEQIZP2 SP 9606: Homo sapiens DE8DP90 ID DE8DP90 DE8DP90 DN Semicarbazide-sensitive amine oxidase (AOC2) DE8DP90 GN AOC2 DE8DP90 SN Amine oxidase [copper-containing]; Retina-specific copper amine oxidase; SSAO; AOC2; RAO DE8DP90 UC AOC2_HUMAN DE8DP90 RD Phenylethylamine DE8DP90 GI 314 DE8DP90 E1 1: Oxidoreductase DE8DP90 E2 1.4: CH-NH2 donor oxidoreductase DE8DP90 E3 1.4.3: Oxygen acceptor oxidoreductase DE8DP90 EC 1.4.3.21 DE8DP90 RC Phase I - Functionalization of compounds:R-HSA-211945 DE8DP90 KG Glycine, serine and threonine metabolism:hsa00260; Metabolic pathways:hsa01100; Phenylalanine metabolism:hsa00360; Tyrosine metabolism:hsa00350; beta-Alanine metabolism:hsa00410 DE8DP90 SQ MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLELLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRNSPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALEGRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYRIQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFINNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVYFEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF DE8DP90 TD Primarily distributed in retina. DE8DP90 FC This enzyme has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. DE8DP90 KD 33208: Metazoa DE8DP90 PL 7711: Chordata DE8DP90 CL 40674: Mammalia DE8DP90 OD 9443: Primates DE8DP90 FM 9604: Hominidae DE8DP90 GE 9605: Homo DE8DP90 SP 9606: Homo sapiens DE0WGR8 ID DE0WGR8 DE0WGR8 DN Phenylalanine--tRNA ligase mitochondrial (FARS2) DE0WGR8 GN FARS2 DE0WGR8 SN Phenylalanyl-tRNA synthetase; Mitochondrial phenylalanine--tRNA ligase; FARS1; FARS2; HSPC320; PheRS DE0WGR8 UC SYFM_HUMAN DE0WGR8 RD L-phenylalanine DE0WGR8 GI 10667 DE0WGR8 E1 6: Ligase DE0WGR8 E2 6.1: Carbon-oxygen ligase DE0WGR8 E3 6.1.1: Aminoacyl tRNA synthetase DE0WGR8 EC 6.1.1.20 DE0WGR8 RC Mitochondrial tRNA aminoacylation:R-HSA-379726 DE0WGR8 KG Aminoacyl-tRNA biosynthesis:hsa00970 DE0WGR8 PD 3CMQ; 3HFV; 3TEG; 3TUP; 5MGH; 5MGU; 5MGV; 5MGW DE0WGR8 SQ MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQDDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVEFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQLLGVEGRF DE0WGR8 TD Low tissue/organ specificity. DE0WGR8 FC This enzyme is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, it also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins. DE0WGR8 KD 33208: Metazoa DE0WGR8 PL 7711: Chordata DE0WGR8 CL 40674: Mammalia DE0WGR8 OD 9443: Primates DE0WGR8 FM 9604: Hominidae DE0WGR8 GE 9605: Homo DE0WGR8 SP 9606: Homo sapiens DEQG7F9 ID DEQG7F9 DEQG7F9 DN Lactate dehydrogenase C (LDHC) DEQG7F9 GN LDHC DEQG7F9 SN L-lactate dehydrogenase C chain; LDH testis subunit; Cancer/testis antigen 32; LDH-C; LDH-X; LDH3; LDHC; LDHX; CT32 DEQG7F9 UC LDHC_HUMAN DEQG7F9 RD Lactate DEQG7F9 GI 3948 DEQG7F9 E1 1: Oxidoreductase DEQG7F9 E2 1.1: CH-OH donor oxidoreductase DEQG7F9 E3 1.1.1: NAD/NADP oxidoreductase DEQG7F9 EC 1.1.1.27 DEQG7F9 RC Pyruvate metabolism:R-HSA-70268 DEQG7F9 KG Central carbon metabolism in cancer:hsa05230; Cysteine and methionine metabolism:hsa00270; Glucagon signaling pathway:hsa04922; Glycolysis / Gluconeogenesis:hsa00010; HIF-1 signaling pathway:hsa04066; Metabolic pathways:hsa01100; Propanoate metabolism:hsa00640; Pyruvate metabolism:hsa00620 DEQG7F9 SQ MSTVKEQLIEKLIEDDENSQCKITIVGTGAVGMACAISILLKDLADELALVDVALDKLKGEMMDLQHGSLFFSTSKITSGKDYSVSANSRIVIVTAGARQQEGETRLALVQRNVAIMKSIIPAIVHYSPDCKILVVSNPVDILTYIVWKISGLPVTRVIGSGCNLDSARFRYLIGEKLGVHPTSCHGWIIGEHGDSSVPLWSGVNVAGVALKTLDPKLGTDSDKEHWKNIHKQVIQSAYEIIKLKGYTSWAIGLSVMDLVGSILKNLRRVHPVSTMVKGLYGIKEELFLSIPCVLGRNGVSDVVKINLNSEEEALFKKSAETLWNIQKDLIF DEQG7F9 TD Primarily distributed in testis. DEQG7F9 FC This enzyme catalyzes the conversion of lactate to pyruvate and back, as it converts NAD+ to NADH and back. DEQG7F9 KD 33208: Metazoa DEQG7F9 PL 7711: Chordata DEQG7F9 CL 40674: Mammalia DEQG7F9 OD 9443: Primates DEQG7F9 FM 9604: Hominidae DEQG7F9 GE 9605: Homo DEQG7F9 SP 9606: Homo sapiens DEMJ7R2 ID DEMJ7R2 DEMJ7R2 DN Amidophosphoribosyltransferase (GPAT) DEMJ7R2 GN PPAT DEMJ7R2 SN Glutamine phosphoribosylpyrophosphate amidotransferase; ATase; GPAT; PPAT DEMJ7R2 UC PUR1_HUMAN DEMJ7R2 RD Fluorouracilo DEMJ7R2 GI 5471 DEMJ7R2 E1 2: Transferase DEMJ7R2 E2 2.4: Glycosyltransferases DEMJ7R2 E3 2.4.2: Pentosyltransferase DEMJ7R2 EC 2.4.2.14 DEMJ7R2 RC Purine ribonucleoside monophosphate biosynthesis:R-HSA-73817 DEMJ7R2 KG Alanine, aspartate and glutamate metabolism:hsa00250; Metabolic pathways:hsa01100; Purine metabolism:hsa00230 DEMJ7R2 SQ MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFLSIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKEKKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW DEMJ7R2 TD Low tissue/organ specificity. DEMJ7R2 FC This enzyme is responsible for catalyzing the conversion of 5-phosphoribosyl-1-pyrophosphate (PRPP) into 5-phosphoribosyl-1-amine (PRA), using the amine group from a glutamine side-chain. DEMJ7R2 KD 33208: Metazoa DEMJ7R2 PL 7711: Chordata DEMJ7R2 CL 40674: Mammalia DEMJ7R2 OD 9443: Primates DEMJ7R2 FM 9604: Hominidae DEMJ7R2 GE 9605: Homo DEMJ7R2 SP 9606: Homo sapiens DEYCUQ2 ID DEYCUQ2 DEYCUQ2 DN Metallo-endopeptidase-like 1 (MMEL1) DEYCUQ2 GN MMEL1 DEYCUQ2 SN Neprilysin II; Soluble form membrane metallo-endopeptidase-like 1; Neprilysin-2; Neprilysin-2 secreted; Membrane metallo-endopeptidase-like 1; Membrane metallo-endopeptidase-like 2; MELL1; MMEL1; MMEL2; NEP2; NEP2(m); NEP2(s); NEPII; NL2 DEYCUQ2 UC MMEL1_HUMAN DEYCUQ2 RD Gonadorelin DEYCUQ2 GI 79258 DEYCUQ2 E1 3: Hydrolases DEYCUQ2 E2 3.4: Peptidase DEYCUQ2 E3 3.4.24: Metallopeptidase DEYCUQ2 EC 3.4.24.11 DEYCUQ2 SQ MGKSEGPVGMVESAGRAGQKRPGFLEGGLLLLLLLVTAALVALGVLYADRRGKQLPRLASRLCFLQEERTFVKRKPRGIPEAQEVSEVCTTPGCVIAAARILQNMDPTTEPCDDFYQFACGGWLRRHVIPETNSRYSIFDVLRDELEVILKAVLENSTAKDRPAVEKARTLYRSCMNQSVIEKRGSQPLLDILEVVGGWPVAMDRWNETVGLEWELERQLALMNSQFNRRVLIDLFIWNDDQNSSRHIIYIDQPTLGMPSREYYFNGGSNRKVREAYLQFMVSVATLLREDANLPRDSCLVQEDMVQVLELETQLAKATVPQEERHDVIALYHRMGLEELQSQFGLKGFNWTLFIQTVLSSVKIKLLPDEEVVVYGIPYLQNLENIIDTYSARTIQNYLVWRLVLDRIGSLSQRFKDTRVNYRKALFGTMVEEVRWRECVGYVNSNMENAVGSLYVREAFPGDSKSMVRELIDKVRTVFVETLDELGWMDEESKKKAQEKAMSIREQIGHPDYILEEMNRRLDEEYSNLNFSEDLYFENSLQNLKVGAQRSLRKLREKVDPNLWIIGAAVVNAFYSPNRNQIVFPAGILQPPFFSKEQPQALNFGGIGMVIGHEITHGFDDNGRNFDKNGNMMDWWSNFSTQHFREQSECMIYQYGNYSWDLADEQNVNGFNTLGENIADNGGVRQAYKAYLKWMAEGGKDQQLPGLDLTHEQLFFINYAQVWCGSYRPEFAIQSIKTDVHSPLKYRVLGSLQNLAAFADTFHCARGTPMHPKERCRVW DEYCUQ2 TD Primarily distributed in testis. DEYCUQ2 FC This enzyme degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. It shares the same substrate specificity with MME and cleaves peptides at the same amide bond. DEYCUQ2 KD 33208: Metazoa DEYCUQ2 PL 7711: Chordata DEYCUQ2 CL 40674: Mammalia DEYCUQ2 OD 9443: Primates DEYCUQ2 FM 9604: Hominidae DEYCUQ2 GE 9605: Homo DEYCUQ2 SP 9606: Homo sapiens DEPT1ME ID DEPT1ME DEPT1ME DN Gamma-glutamyltranspeptidase 1 (GGT1) DEPT1ME GN GGT1 DEPT1ME SN Glutathione hydrolase 1 proenzyme; Leukotriene-C4 hydrolase; Gamma-glutamyltransferase 1; Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain; CD224; GGT; GGT 1; GGT1 DEPT1ME UC GGT1_HUMAN DEPT1ME RD Glutathiol DEPT1ME GI 2678 DEPT1ME E1 3: Hydrolases DEPT1ME E2 3.4: Peptidase DEPT1ME E3 3.4.19: Omega peptidase DEPT1ME EC 3.4.19.13 DEPT1ME RC Aflatoxin activation and detoxification:R-HSA-5423646; Defective GGT1 causes Glutathionuria (GLUTH):R-HSA-5579022; Defective GGT1 causes Glutathionuria (GLUTH):R-HSA-9035968; Glutathione synthesis and recycling:R-HSA-174403; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DEPT1ME KG Arachidonic acid metabolism:hsa00590; Glutathione metabolism:hsa00480; Metabolic pathways:hsa01100; Taurine and hypotaurine metabolism:hsa00430 DEPT1ME PD 4GDX; 4GG2; 4Z9O; 4ZBK; 4ZC6; 4ZCG; 5V4Q DEPT1ME SQ MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY DEPT1ME TD Primarily distributed in kidney, liver and seminal vesicle. DEPT1ME FC This enzyme cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, it can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. DEPT1ME KD 33208: Metazoa DEPT1ME PL 7711: Chordata DEPT1ME CL 40674: Mammalia DEPT1ME OD 9443: Primates DEPT1ME FM 9604: Hominidae DEPT1ME GE 9605: Homo DEPT1ME SP 9606: Homo sapiens DE1DOKJ ID DE1DOKJ DE1DOKJ DN Cytosolic 5'-nucleotidase II (NT5C2) DE1DOKJ GN NT5C2 DE1DOKJ SN Cytosolic purine 5'-nucleotidase; NT5B; NT5C2; NT5CP; PNT5 DE1DOKJ UC 5NTC_HUMAN DE1DOKJ RD Ribavirin DE1DOKJ GI 22978 DE1DOKJ E1 3: Hydrolases DE1DOKJ E2 3.1: Ester bond hydrolase DE1DOKJ E3 3.1.3: Phosphoric monoester hydrolase DE1DOKJ EC 3.1.3.5 DE1DOKJ RC Abacavir metabolism:R-HSA-2161541; Purine catabolism:R-HSA-74259 DE1DOKJ KG Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760; Purine metabolism:hsa00230; Pyrimidine metabolism:hsa00240 DE1DOKJ PD 2JCM; 2XCV; 2XCW; 2XCX; 2XJB; 2XJC; 2XJD; 2XJE; 2XJF DE1DOKJ SQ MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEEE DE1DOKJ TD Low tissue/organ specificity. DE1DOKJ FC This enzyme preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides. DE1DOKJ KD 33208: Metazoa DE1DOKJ PL 7711: Chordata DE1DOKJ CL 40674: Mammalia DE1DOKJ OD 9443: Primates DE1DOKJ FM 9604: Hominidae DE1DOKJ GE 9605: Homo DE1DOKJ SP 9606: Homo sapiens DEBH7ND ID DEBH7ND DEBH7ND DN Chondroitin sulfate glucuronyltransferase (CHPF2) DEBH7ND GN CHPF2 DEBH7ND SN Chondroitin glucuronyltransferase; Chondroitin polymerizing factor 2; Chondroitin synthase 3; N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase; UNQ299/PRO339; CHPF2; CHSY3; CSGLCAT; CSGlcA-T; ChPF-2; ChSy-3; KIAA1402 DEBH7ND UC CHPF2_HUMAN DEBH7ND RD UDP-glucuronate DEBH7ND GI 54480 DEBH7ND E1 2: Transferase DEBH7ND E2 2.4: Glycosyltransferases DEBH7ND E3 2.4.1: Hexosyltransferase DEBH7ND EC 2.4.1.226 DEBH7ND RC Chondroitin sulfate biosynthesis:R-HSA-2022870 DEBH7ND KG Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate:hsa00532; Metabolic pathways:hsa01100 DEBH7ND SQ MRLSSLLALLRPALPLILGLSLGCSLSLLRVSWIQGEGEDPCVEAVGERGGPQNPDSRARLDQSDEDFKPRIVPYYRDPNKPYKKVLRTRYIQTELGSRERLLVAVLTSRATLSTLAVAVNRTVAHHFPRLLYFTGQRGARAPAGMQVVSHGDERPAWLMSETLRHLHTHFGADYDWFFIMQDDTYVQAPRLAALAGHLSINQDLYLGRAEEFIGAGEQARYCHGGFGYLLSRSLLLRLRPHLDGCRGDILSARPDEWLGRCLIDSLGVGCVSQHQGQQYRSFELAKNRDPEKEGSSAFLSAFAVHPVSEGTLMYRLHKRFSALELERAYSEIEQLQAQIRNLTVLTPEGEAGLSWPVGLPAPFTPHSRFEVLGWDYFTEQHTFSCADGAPKCPLQGASRADVGDALETALEQLNRRYQPRLRFQKQRLLNGYRRFDPARGMEYTLDLLLECVTQRGHRRALARRVSLLRPLSRVEILPMPYVTEATRVQLVLPLLVAEAAAAPAFLEAFAANVLEPREHALLTLLLVYGPREGGRGAPDPFLGVKAAAAELERRYPGTRLAWLAVRAEAPSQVRLMDVVSKKHPVDTLFFLTTVWTRPGPEVLNRCRMNAISGWQAFFPVHFQEFNPALSPQRSPPGPPGAGPDPPSPPGADPSRGAPIGGRFDRQASAEGCFYNADYLAARARLAGELAGQEEEEALEGLEVMDVFLRFSGLHLFRAVEPGLVQKFSLRDCSPRLSEELYHRCRLSNLEGLGGRAQLAMALFEQEQANST DEBH7ND TD Primarily distributed in placenta, small intestine and pancreas. DEBH7ND FC This enzyme transfers glucuronic acid (GlcUA) from UDP-GlcUA to N- acetylgalactosamine residues on the non-reducing end of the elongating chondroitin polymer. DEBH7ND KD 33208: Metazoa DEBH7ND PL 7711: Chordata DEBH7ND CL 40674: Mammalia DEBH7ND OD 9443: Primates DEBH7ND FM 9604: Hominidae DEBH7ND GE 9605: Homo DEBH7ND SP 9606: Homo sapiens DEE1B8O ID DEE1B8O DEE1B8O DN Glucose-6-phosphatase beta (G6PC3) DEE1B8O GN G6PC3 DEE1B8O SN G6Pase-beta; Glucose-6-phosphatase 3; Ubiquitous glucose-6-phosphatase catalytic subunit-related protein; G-6-Pase 3; G6PC3; G6Pase 3; UGRP DEE1B8O UC G6PC3_HUMAN DEE1B8O RD D-glucose 6-phosphate DEE1B8O GI 92579 DEE1B8O E1 3: Hydrolases DEE1B8O E2 3.1: Ester bond hydrolase DEE1B8O E3 3.1.3: Phosphoric monoester hydrolase DEE1B8O EC 3.1.3.9 DEE1B8O RC Gluconeogenesis:R-HSA-70263; Severe congenital neutropenia type 4 (G6PC3):R-HSA-3282872 DEE1B8O KG AMPK signaling pathway:hsa04152; Adipocytokine signaling pathway:hsa04920; Carbohydrate digestion and absorption:hsa04973; FoxO signaling pathway:hsa04068; Galactose metabolism:hsa00052; Glucagon signaling pathway:hsa04922; Glycolysis / Gluconeogenesis:hsa00010; Insulin resistance:hsa04931; Insulin signaling pathway:hsa04910; Metabolic pathways:hsa01100; PI3K-Akt signaling pathway:hsa04151; Starch and sucrose metabolism:hsa00500 DEE1B8O SQ MESTLGAGIVIAEALQNQLAWLENVWLWITFLGDPKILFLFYFPAAYYASRRVGIAVLWISLITEWLNLIFKWFLFGDRPFWWVHESGYYSQAPAQVHQFPSSCETGPGSPSGHCMITGAALWPIMTALSSQVATRARSRWVRVMPSLAYCTFLLAVGLSRIFILAHFPHQVLAGLITGAVLGWLMTPRVPMERELSFYGLTALALMLGTSLIYWTLFTLGLDLSWSISLAFKWCERPEWIHVDSRPFASLSRDSGAALGLGIALHSPCYAQVRRAQLGNGQKIACLVLAMGLLGPLDWLGHPPQISLFYIFNFLKYTLWPCLVLALVPWAVHMFSAQEAPPIHSS DEE1B8O TD Primarily distributed in skeletal muscle. Also expressed in heart, brain, placenta, kidney, colon, thymus, spleen, pancreas, testis, prostate, ovary, liver, lung, small intestine and peripheral bloodlymphocytes. DEE1B8O FC This enzyme hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. DEE1B8O KD 33208: Metazoa DEE1B8O PL 7711: Chordata DEE1B8O CL 40674: Mammalia DEE1B8O OD 9443: Primates DEE1B8O FM 9604: Hominidae DEE1B8O GE 9605: Homo DEE1B8O SP 9606: Homo sapiens DE3GT9C ID DE3GT9C DE3GT9C DN Cytochrome P450 4F2 (CYP4F2) DE3GT9C GN CYP4F2 DE3GT9C SN Cytochrome P450 family 4 subfamily F member 2; Arachidonic acid omega-hydroxylase; CYP4F2; CYPIVF2; Leukotriene-B(4) 20-monooxygenase 1; Leukotriene-B(4) omega-hydroxylase 1; Phylloquinone omega-hydroxylase CYP4F2 DE3GT9C UC CP4F2_HUMAN DE3GT9C RD Dinoprostone DE3GT9C GI 8529 DE3GT9C E1 1: Oxidoreductase DE3GT9C E2 1.14: Oxygen paired donor oxidoreductase DE3GT9C E3 1.14.13: NADH/NADPH donor oxidoreductase DE3GT9C EC 1.14.13.30 DE3GT9C RC Eicosanoids:R-HSA-211979; Fatty acids:R-HSA-211935; Miscellaneous substrates:R-HSA-211958; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE):R-HSA-2142816; Synthesis of Leukotrienes (LT) and Eoxins (EX):R-HSA-2142691 DE3GT9C KG Arachidonic acid metabolism:hsa00590; Metabolic pathways:hsa01100 DE3GT9C SQ MSQLSLSWLGLWPVAASPWLLLLLVGASWLLAHVLAWTYAFYDNCRRLRCFPQPPRRNWFWGHQGMVNPTEEGMRVLTQLVATYPQGFKVWMGPISPLLSLCHPDIIRSVINASAAIAPKDKFFYSFLEPWLGDGLLLSAGDKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSACLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVSKRHHEILLHIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQELLKDREPKEIEWDDLAHLPFLTMCMKESLRLHPPVPVISRHVTQDIVLPDGRVIPKGIICLISVFGTHHNPAVWPDPEVYDPFRFDPENIKERSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS DE3GT9C TD Primarily distributed in intestine and liver. DE3GT9C FC This enzyme is involved in the metabolism of various endogenous substrates, including fatty acids, eicosanoids and vitamins. It catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long- and very long-chain fatty acids and displays high omega-hydroxylase activity toward polyunsaturated fatty acids (PUFAs). It participates in the conversion of arachidonic acid to omega-hydroxyeicosatetraenoic acid (20-HETE) and plays a role in the oxidative inactivation of eicosanoids. In addition, it catalyzes omega-hydroxylation of 3-hydroxy fatty acids and converts monoepoxides of linoleic acid leukotoxin and isoleukotoxin to omega-hydroxylated metabolites. It also contributes to the degradation of very long-chain fatty acids (VLCFAs) by catalyzing successive omega-oxidations and chain shortening. It plays an important role in vitamin metabolism by chain shortening and catalyzes omega- hydroxylation of the phytyl chain of tocopherols (forms of vitamin E), with preference for gamma-tocopherols over alpha-tocopherols. It also can Omega-hydroxylates and inactivates phylloquinone (vitamin K1), and menaquinone-4 (MK-4, a form of vitamin K2), both acting as cofactors in blood coagulation. DE3GT9C KD 33208: Metazoa DE3GT9C PL 7711: Chordata DE3GT9C CL 40674: Mammalia DE3GT9C OD 9443: Primates DE3GT9C FM 9604: Hominidae DE3GT9C GE 9605: Homo DE3GT9C SP 9606: Homo sapiens DE8E6X9 ID DE8E6X9 DE8E6X9 DN Soluble aminopeptidase P (sAmp) DE8E6X9 GN XPNPEP1 DE8E6X9 SN Aminoacylproline aminopeptidase; Cytosolic aminopeptidase P; X-Pro aminopeptidase 1; Soluble X-prolyl aminopeptidase 1; Xaa-Pro aminopeptidase 1; sAmp; XPNPEP1; XPNPEPL; XPNPEPL1 DE8E6X9 UC XPP1_HUMAN DE8E6X9 RD BRS-640 DE8E6X9 GI 7511 DE8E6X9 E1 3: Hydrolases DE8E6X9 E2 3.4: Peptidase DE8E6X9 E3 3.4.11: Aminopeptidase DE8E6X9 EC 3.4.11.9 DE8E6X9 PD 3CTZ DE8E6X9 SQ MPPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHLLLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSETIPKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKEVPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPVPETNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGHIAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGPCGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPVKTKYNFNNRGSLTFEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKELQKQGRQEALEWLIRETQPISKQH DE8E6X9 TD Primarily distributed in pancreas, heart, muscle, kidney, liver, lung and brain. DE8E6X9 FC This enzyme contributes to the degradation of bradykinin. It catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. DE8E6X9 KD 33208: Metazoa DE8E6X9 PL 7711: Chordata DE8E6X9 CL 40674: Mammalia DE8E6X9 OD 9443: Primates DE8E6X9 FM 9604: Hominidae DE8E6X9 GE 9605: Homo DE8E6X9 SP 9606: Homo sapiens DE5EGK0 ID DE5EGK0 DE5EGK0 DN Prolyl 4-hydroxylase alpha-2 (P4HA2) DE5EGK0 GN P4HA2 DE5EGK0 SN Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2; Prolyl 4-hydroxylase subunit alpha-2; 4-PH alpha-2; P4HA2; UNQ290/PRO330 DE5EGK0 UC P4HA2_HUMAN DE5EGK0 RD Ascorbic acid DE5EGK0 GI 8974 DE5EGK0 E1 1: Oxidoreductase DE5EGK0 E2 1.14: Oxygen paired donor oxidoreductase DE5EGK0 E3 1.14.11: 2-oxoglutarate donor oxidoreductase DE5EGK0 EC 1.14.11.2 DE5EGK0 RC Collagen biosynthesis and modifying enzymes:R-HSA-1650814 DE5EGK0 KG Arginine and proline metabolism:hsa00330; Metabolic pathways:hsa01100 DE5EGK0 PD 6EVL; 6EVM; 6EVN; 6EVO; 6EVP DE5EGK0 SQ MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSHERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVKLTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPKLARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVANYGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKKGTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD DE5EGK0 TD Low tissue/organ specificity. DE5EGK0 FC This enzyme catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. DE5EGK0 KD 33208: Metazoa DE5EGK0 PL 7711: Chordata DE5EGK0 CL 40674: Mammalia DE5EGK0 OD 9443: Primates DE5EGK0 FM 9604: Hominidae DE5EGK0 GE 9605: Homo DE5EGK0 SP 9606: Homo sapiens DER8LQ6 ID DER8LQ6 DER8LQ6 DN Phenylethanolamine N-methyltransferase (PNMT) DER8LQ6 GN PNMT DER8LQ6 SN Noradrenaline N-methyltransferase; PNMTase; PENT; PNMT DER8LQ6 UC PNMT_HUMAN DER8LQ6 RD Phenylethanolamine DER8LQ6 GI 5409 DER8LQ6 E1 2: Transferase DER8LQ6 E2 2.1: Methylase DER8LQ6 E3 2.1.1: Methyltransferase DER8LQ6 EC 2.1.1.28 DER8LQ6 RC Catecholamine biosynthesis:R-HSA-209905 DER8LQ6 KG Metabolic pathways:hsa01100; Tyrosine metabolism:hsa00350 DER8LQ6 PD 1N7J; 1YZ3; 2AN3; 2AN4; 2AN5; 2G70; 2G71; 2G72; 2G8N DER8LQ6 SQ MSGADRSPNAGAAPDSAPGQAAVASAYQRFEPRAYLRNNYAPPRGDLCNPNGVGPWKLRCLAQTFATGEVSGRTLIDIGSGPTVYQLLSACSHFEDITMTDFLEVNRQELGRWLQEEPGAFNWSMYSQHACLIEGKGECWQDKERQLRARVKRVLPIDVHQPQPLGAGSPAPLPADALVSAFCLEAVSPDLASFQRALDHITTLLRPGGHLLLIGALEESWYLAGEARLTVVPVSEEEVREALVRSGYKVRDLRTYIMPAHLQTGVDDVKGVFFAWAQKVGL DER8LQ6 TD Primarily distributed in adrenal gland, ductus deferens and seminal vesicle. DER8LQ6 FC This enzyme converts noradrenaline to adrenaline. DER8LQ6 KD 33208: Metazoa DER8LQ6 PL 7711: Chordata DER8LQ6 CL 40674: Mammalia DER8LQ6 OD 9443: Primates DER8LQ6 FM 9604: Hominidae DER8LQ6 GE 9605: Homo DER8LQ6 SP 9606: Homo sapiens DEPOVCH ID DEPOVCH DEPOVCH DN Maillard deglycase (PARK7) DEPOVCH GN PARK7 DEPOVCH SN Oncogene DJ1; Parkinson disease protein 7; Protein/nucleic acid deglycase DJ-1; Parkinsonism-associated deglycase; Protein DJ-1; DJ-1; PARK7 DEPOVCH UC PARK7_HUMAN DEPOVCH RD Phenylglyoxal DEPOVCH GI 11315 DEPOVCH E1 3: Hydrolases DEPOVCH E2 3.5: Carbon-nitrogen hydrolase DEPOVCH E3 3.5.1: Linear amide hydrolase DEPOVCH EC 3.5.1.124 DEPOVCH RC Chaperone Mediated Autophagy:R-HSA-9613829; Microautophagy:R-HSA-9615710; SUMOylation of transcription cofactors:R-HSA-3899300 DEPOVCH KG Parkinson's disease:hsa05012 DEPOVCH PD 1PDV; 1PDW; 1PE0; 1Q2U; 1SOA; 1UCF; 2OR3; 2R1T; 2R1U DEPOVCH SQ MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEALNGKEVAAQVKAPLVLKD DEPOVCH TD Primarily distributed in pancreas, kidney, skeletalmuscle, liver, testis and heart. DEPOVCH FC This enzyme catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. DEPOVCH KD 33208: Metazoa DEPOVCH PL 7711: Chordata DEPOVCH CL 40674: Mammalia DEPOVCH OD 9443: Primates DEPOVCH FM 9604: Hominidae DEPOVCH GE 9605: Homo DEPOVCH SP 9606: Homo sapiens DEY0TQC ID DEY0TQC DEY0TQC DN Dimethylarginine dimethylaminohydrolase 1 (DDAH1) DEY0TQC GN DDAH1 DEY0TQC SN Dimethylargininase-1; N(G),N(G)-dimethylarginine dimethylaminohydrolase 1; DDAH; DDAH-1; DDAH1; DDAHI DEY0TQC UC DDAH1_HUMAN DEY0TQC RD S-MTC DEY0TQC GI 23576 DEY0TQC E1 3: Hydrolases DEY0TQC E2 3.5: Carbon-nitrogen hydrolase DEY0TQC E3 3.5.3: Linear amidine hydrolase DEY0TQC EC 3.5.3.18 DEY0TQC RC eNOS activation:R-HSA-203615 DEY0TQC PD 2JAI; 2JAJ; 3I2E; 3I4A; 3P8E; 3P8P; 6DGE DEY0TQC SQ MAGLGHPAAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQHQLYVGVLGSKLGLQVVELPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS DEY0TQC TD Primarily distributed in brain, liver, kidney and pancreas. DEY0TQC FC This enzyme hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)- monomethyl-L-arginine (MMA). DEY0TQC KD 33208: Metazoa DEY0TQC PL 7711: Chordata DEY0TQC CL 40674: Mammalia DEY0TQC OD 9443: Primates DEY0TQC FM 9604: Hominidae DEY0TQC GE 9605: Homo DEY0TQC SP 9606: Homo sapiens DE3FEV8 ID DE3FEV8 DE3FEV8 DN Dicarbonyl/L-xylulose reductase (DCXR) DE3FEV8 GN DCXR DE3FEV8 SN Carbonyl reductase II; Kidney dicarbonyl reductase; L-xylulose reductase; Short chain dehydrogenase/reductase family 20C member 1; Sperm surface protein P34H; XR; kiDCR; DCXR; SDR20C1 DE3FEV8 UC DCXR_HUMAN DE3FEV8 RD Naphthoquinone beta DE3FEV8 GI 51181 DE3FEV8 E1 1: Oxidoreductase DE3FEV8 E2 1.1: CH-OH donor oxidoreductase DE3FEV8 E3 1.1.1: NAD/NADP oxidoreductase DE3FEV8 EC 1.1.1.10 DE3FEV8 RC Essential pentosuria:R-HSA-5662853; Formation of xylulose-5-phosphate:R-HSA-5661270 DE3FEV8 KG Metabolic pathways:hsa01100; Pentose and glucuronate interconversions:hsa00040 DE3FEV8 PD 1PR9; 1WNT; 3D3W DE3FEV8 SQ MELFLAGRRVLVTGAGKGIGRGTVQALHATGARVVAVSRTQADLDSLVRECPGIEPVCVDLGDWEATERALGSVGPVDLLVNNAAVALLQPFLEVTKEAFDRSFEVNLRAVIQVSQIVARGLIARGVPGAIVNVSSQCSQRAVTNHSVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTSMGQATWSDPHKAKTMLNRIPLGKFAEVEHVVNAILFLLSDRSGMTTGSTLPVEGGFWAC DE3FEV8 TD Primarily distributed in kidney, liver and epididymis. DE3FEV8 FC This enzyme catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose and participates in the uronate cycle of glucose metabolism. DE3FEV8 KD 33208: Metazoa DE3FEV8 PL 7711: Chordata DE3FEV8 CL 40674: Mammalia DE3FEV8 OD 9443: Primates DE3FEV8 FM 9604: Hominidae DE3FEV8 GE 9605: Homo DE3FEV8 SP 9606: Homo sapiens DERQV72 ID DERQV72 DERQV72 DN VKORC1-like protein 1 (VKORC1L1) DERQV72 GN VKORC1L1 DERQV72 SN Vitamin K epoxide reductase complex subunit 1-like protein 1; VKORC1L1 DERQV72 UC VKORL_HUMAN DERQV72 RD Vitamin K DERQV72 GI 154807 DERQV72 E1 1: Oxidoreductase DERQV72 E2 1.17: CH/CH2 oxidoreductase DERQV72 E3 1.17.4: Disulfide acceptor oxidoreductase DERQV72 EC 1.17.4.4 DERQV72 RC Metabolism of vitamin K:R-HSA-6806664 DERQV72 KG Metabolic pathways:hsa01100; Ubiquinone and other terpenoid-quinone biosynthesis:hsa00130 DERQV72 SQ MAAPVLLRVSVPRWERVARYAVCAAGILLSIYAYHVEREKERDPEHRALCDLGPWVKCSAALASRWGRGFGLLGSIFGKDGVLNQPNSVFGLIFYILQLLLGMTASAVAALILMTSSIMSVVGSLYLAYILYFVLKEFCIICIVTYVLNFLLLIINYKRLVYLNEAWKRQLQPKQD DERQV72 TD Low tissue/organ specificity. DERQV72 FC This enzyme is involved in vitamin K metabolism. It can reduce inactive vitamin K 2,3-epoxide to active vitamin K (in vitro), and may contribute to vitamin K-mediated protection against oxidative stress. DERQV72 KD 33208: Metazoa DERQV72 PL 7711: Chordata DERQV72 CL 40674: Mammalia DERQV72 OD 9443: Primates DERQV72 FM 9604: Hominidae DERQV72 GE 9605: Homo DERQV72 SP 9606: Homo sapiens DE478BP ID DE478BP DE478BP DN Uridine-cytidine kinase 1 (UCK1) DE478BP GN UCK1 DE478BP SN Cytidine monophosphokinase 1; Uridine monophosphokinase 1; UCK 1; UCK1; URK1 DE478BP UC UCK1_HUMAN DE478BP RD Uridine DE478BP GI 83549 DE478BP E1 2: Transferase DE478BP E2 2.7: Kinase DE478BP E3 2.7.1: Phosphotransferase DE478BP EC 2.7.1.48 DE478BP RC Pyrimidine salvage:R-HSA-73614 DE478BP KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DE478BP PD 2JEO; 2UVQ DE478BP SQ MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVVILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRRGRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGDICKWHRGGSNGRSYKRTFSEPGDHPGMLTSGKRSHLESSSRPH DE478BP TD Low tissue/organ specificity. DE478BP FC This enzyme phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate but does not phosphorylate deoxyribonucleosides or purine ribonucleosides. It can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)- acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine. DE478BP KD 33208: Metazoa DE478BP PL 7711: Chordata DE478BP CL 40674: Mammalia DE478BP OD 9443: Primates DE478BP FM 9604: Hominidae DE478BP GE 9605: Homo DE478BP SP 9606: Homo sapiens DEMPH4I ID DEMPH4I DEMPH4I DN Uridine/cytidine monophosphate kinase (UMPK) DEMPH4I GN CMPK1 DEMPH4I SN Deoxycytidylate kinase; Nucleoside-diphosphate kinase; UMP-CMP kinase; UMP/CMP kinase; UMP/CMPK; Uridine monophosphate/cytidine monophosphate kinase; dCMP kinase; CMK; CMPK; CMPK1; UCK; UMK; UMPK DEMPH4I UC KCY_HUMAN DEMPH4I RD Gemcitabine DEMPH4I GI 51727 DEMPH4I E1 2: Transferase DEMPH4I E2 2.7: Kinase DEMPH4I E3 2.7.4: Phosphotransferase DEMPH4I EC 2.7.4.14 DEMPH4I RC Interconversion of nucleotide di- and triphosphates:R-HSA-499943 DEMPH4I KG Drug metabolism - other enzymes:hsa00983; Metabolic pathways:hsa01100; Pyrimidine metabolism:hsa00240 DEMPH4I PD 1TEV DEMPH4I SQ MKPLVVFVLGGPGAGKGTQCARIVEKYGYTHLSAGELLRDERKNPDSQYGELIEKYIKEGKIVPVEITISLLKREMDQTMAANAQKNKFLIDGFPRNQDNLQGWNKTMDGKADVSFVLFFDCNNEICIERCLERGKSSGRSDDNRESLEKRIQTYLQSTKPIIDLYEEMGKVKKIDASKSVDEVFDEVVQIFDKEG DEMPH4I TD Low tissue/organ specificity. DEMPH4I FC This enzyme catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. It plays an important role in de novo pyrimidine nucleotide biosynthesis and it has preference for UMP and CMP as phosphate acceptors. DEMPH4I KD 33208: Metazoa DEMPH4I PL 7711: Chordata DEMPH4I CL 40674: Mammalia DEMPH4I OD 9443: Primates DEMPH4I FM 9604: Hominidae DEMPH4I GE 9605: Homo DEMPH4I SP 9606: Homo sapiens DE4U39Y ID DE4U39Y DE4U39Y DN UDP-glucose pyrophosphorylase (UGPase) DE4U39Y GN UGP2 DE4U39Y SN UTP--glucose-1-phosphate uridylyltransferase; UDPGP; UGP1; UGP2; UGPase DE4U39Y UC UGPA_HUMAN DE4U39Y RD D-glucose 1-phosphate DE4U39Y GI 7360 DE4U39Y E1 2: Transferase DE4U39Y E2 2.7: Kinase DE4U39Y E3 2.7.7: Nucleotidyltransferase DE4U39Y EC 2.7.7.9 DE4U39Y RC Formation of the active cofactor, UDP-glucuronate:R-HSA-173599; Glycogen synthesis:R-HSA-3322077 DE4U39Y KG Amino sugar and nucleotide sugar metabolism:hsa00520; Galactose metabolism:hsa00052; Metabolic pathways:hsa01100; Pentose and glucuronate interconversions:hsa00040; Starch and sucrose metabolism:hsa00500 DE4U39Y PD 3R2W; 3R3I; 4R7P DE4U39Y SQ MSRFVQDLSKAMSQDGASQFQEVIRQELELSVKKELEKILTTASSHEFEHTKKDLDGFRKLFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGLPDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPVAKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNPPNGKRCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLDGGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSGNLRILDH DE4U39Y TD Primarily distributed in liver. DE4U39Y FC This enzyme plays a central role as a glucosyl donor in cellular metabolic pathways. DE4U39Y KD 33208: Metazoa DE4U39Y PL 7711: Chordata DE4U39Y CL 40674: Mammalia DE4U39Y OD 9443: Primates DE4U39Y FM 9604: Hominidae DE4U39Y GE 9605: Homo DE4U39Y SP 9606: Homo sapiens DE48Q2Z ID DE48Q2Z DE48Q2Z DN UDP-glucose 6-dehydrogenase (UGDH) DE48Q2Z GN UGDH DE48Q2Z SN UDP-Glc dehydrogenase; UDP-glucose dehydrogenase; UDP-GlcDH; UDPGDH; UGDH DE48Q2Z UC UGDH_HUMAN DE48Q2Z RD UDP-glucose DE48Q2Z GI 7358 DE48Q2Z E1 1: Oxidoreductase DE48Q2Z E2 1.1: CH-OH donor oxidoreductase DE48Q2Z E3 1.1.1: NAD/NADP oxidoreductase DE48Q2Z EC 1.1.1.22 DE48Q2Z RC Formation of the active cofactor, UDP-glucuronate:R-HSA-173599 DE48Q2Z KG Amino sugar and nucleotide sugar metabolism:hsa00520; Ascorbate and aldarate metabolism:hsa00053; Metabolic pathways:hsa01100; Pentose and glucuronate interconversions:hsa00040 DE48Q2Z PD 2Q3E; 2QG4; 3ITK; 3KHU; 3PRJ; 4EDF; 5VR8; 6C58; 6C5A DE48Q2Z SQ MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV DE48Q2Z TD Primarily distributed in liver. Also expressed in heart, placenta, pancreas, spleen, thymus, prostate, ovary, small intestine and colon. DE48Q2Z FC This enzyme catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans. It is required for the biosynthesis of chondroitin sulfate and heparan sulfate. DE48Q2Z KD 33208: Metazoa DE48Q2Z PL 7711: Chordata DE48Q2Z CL 40674: Mammalia DE48Q2Z OD 9443: Primates DE48Q2Z FM 9604: Hominidae DE48Q2Z GE 9605: Homo DE48Q2Z SP 9606: Homo sapiens DE3OZT4 ID DE3OZT4 DE3OZT4 DN Testicular acid phosphatase (ACP4) DE3OZT4 GN ACP4 DE3OZT4 SN Acid monophosphatase 4; Acid nucleoside diphosphate phosphatase 4; Acid phosphatase 4; ACP4; ACPT DE3OZT4 UC PPAT_HUMAN DE3OZT4 RD Riboflavin DE3OZT4 GI 93650 DE3OZT4 E1 3: Hydrolases DE3OZT4 E2 3.1: Ester bond hydrolase DE3OZT4 E3 3.1.3: Phosphoric monoester hydrolase DE3OZT4 EC 3.1.3.2 DE3OZT4 SQ MAGLGFWGHPAGPLLLLLLLVLPPRALPEGPLVFVALVFRHGDRAPLASYPMDPHKEVASTLWPRGLGQLTTEGVRQQLELGRFLRSRYEAFLSPEYRREEVYIRSTDFDRTLESAQANLAGLFPEAAPGSPEARWRPIPVHTVPVAEDKLLRFPMRSCPRYHELLREATEAAEYQEALEGWTGFLSRLENFTGLSLVGEPLRRAWKVLDTLMCQQAHGLPLPAWASPDVLRTLAQISALDIGAHVGPPRAAEKAQLTGGILLNAILANFSRVQRLGLPLKMVMYSAHDSTLLALQGALGLYDGHTPPYAACLGFEFRKHLGNPAKDGGNVTVSLFYRNDSAHLPLPLSLPGCPAPCPLGRFYQLTAPARPPAHGVSCHGPYEAAIPPAPVVPLLAGAVAVLVALSLGLGLLAWRPGCLRALGGPV DE3OZT4 TD Primarily distributed in skin and testis. DE3OZT4 FC This enzyme dephosphorylates receptor tyrosine-protein kinase ERBB4 and inhibits its ligand-induced proteolytic cleavage. And it may play a role in odontogenesis. DE3OZT4 KD 33208: Metazoa DE3OZT4 PL 7711: Chordata DE3OZT4 CL 40674: Mammalia DE3OZT4 OD 9443: Primates DE3OZT4 FM 9604: Hominidae DE3OZT4 GE 9605: Homo DE3OZT4 SP 9606: Homo sapiens DESICUZ ID DESICUZ DESICUZ DN Retinol dehydrogenase 13 (RDH13) DESICUZ GN RDH13 DESICUZ SN Dehydrogenase/reductase family 7C member 3; Short chain dehydrogenase/reductase family 7C member 3; PSEC0082; RDH13; SDR7C3; UNQ736/PRO1430 DESICUZ UC RDH13_HUMAN DESICUZ RD Dihydrocozymase DESICUZ GI 112724 DESICUZ E1 1: Oxidoreductase DESICUZ E2 1.1: CH-OH donor oxidoreductase DESICUZ E3 1.1.1: NAD/NADP oxidoreductase DESICUZ EC 1.1.1.300 DESICUZ RC RA biosynthesis pathway:R-HSA-5365859 DESICUZ SQ MSRYLLPLSALGTVAGAAVLLKDYVTGGACPSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEAEDEEVARRLWAESARLVGLEAPSVREQPLPR DESICUZ TD Low tissue/organ specificity. DESICUZ FC This enzyme has a clear preference for NADP. It oxidizes all-trans-retinol, but seems to reduce all-trans-retinal with much higher efficiency. DESICUZ KD 33208: Metazoa DESICUZ PL 7711: Chordata DESICUZ CL 40674: Mammalia DESICUZ OD 9443: Primates DESICUZ FM 9604: Hominidae DESICUZ GE 9605: Homo DESICUZ SP 9606: Homo sapiens DEUATVX ID DEUATVX DEUATVX DN Quinone reductase 2 (NQO2) DEUATVX GN NQO2 DEUATVX SN NRH:quinone oxidoreductase 2; NRH dehydrogenase [quinone] 2; Ribosyldihydronicotinamide dehydrogenase [quinone]; NMOR2; NQO2; QR2 DEUATVX UC NQO2_HUMAN DEUATVX RD SRT-647 DEUATVX GI 4835 DEUATVX E1 1: Oxidoreductase DEUATVX E2 1.1: Diphenol donor oxidoreductase DEUATVX E3 1.10.5: Quinone oxidoreductase DEUATVX EC 1.10.5.1 DEUATVX RC Phase I - Functionalization of compounds:R-HSA-211945 DEUATVX PD 1XI2; 1ZX1; 2BZS; 2QMY; 2QMZ; 2QR2; 2QWX; 2QX4; 2QX6 DEUATVX SQ MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRATDKDITGTLSNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ DEUATVX TD Low tissue/organ specificity. DEUATVX FC This enzyme serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways. DEUATVX KD 33208: Metazoa DEUATVX PL 7711: Chordata DEUATVX CL 40674: Mammalia DEUATVX OD 9443: Primates DEUATVX FM 9604: Hominidae DEUATVX GE 9605: Homo DEUATVX SP 9606: Homo sapiens DEMQTKH ID DEMQTKH DEMQTKH DN HIF-prolyl hydroxylase 3 (EGLN3) DEMQTKH GN EGLN3 DEMQTKH SN Hypoxia-inducible factor prolyl hydroxylase 3; Egl nine homolog 3; Prolyl hydroxylase domain-containing protein 3; EGLN3; HIF-PH3; HPH-1; HPH-3; PHD3 DEMQTKH UC EGLN3_HUMAN DEMQTKH RD Oxoglutarate DEMQTKH GI 112399 DEMQTKH E1 1: Oxidoreductase DEMQTKH E2 1.14: Oxygen paired donor oxidoreductase DEMQTKH E3 1.14.11: 2-oxoglutarate donor oxidoreductase DEMQTKH EC 1.14.11.29 DEMQTKH RC Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha:R-HSA-1234176 DEMQTKH KG HIF-1 signaling pathway:hsa04066; Pathways in cancer:hsa05200; Renal cell carcinoma:hsa05211 DEMQTKH SQ MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALTED DEMQTKH TD Primarily distributed in heart muscle and skin. DEMQTKH FC This enzyme is able to catalyze the hydroxylation of proteins such as the subunits of hypoxia-inducible factor. DEMQTKH KD 33208: Metazoa DEMQTKH PL 7711: Chordata DEMQTKH CL 40674: Mammalia DEMQTKH OD 9443: Primates DEMQTKH FM 9604: Hominidae DEMQTKH GE 9605: Homo DEMQTKH SP 9606: Homo sapiens DE63NYG ID DE63NYG DE63NYG DN Galactose mutarotase (GALM) DE63NYG GN GALM DE63NYG SN Aldose 1-epimerase; Aldose 1-epimerase-like protein; Galactose mutarotase/UDP-galactose 4-epimerase protein; Galactomutarotase; Galactose mutarotase; BLOCK25; GALM DE63NYG UC GALM_HUMAN DE63NYG RD Alpha-D-galactose DE63NYG GI 130589 DE63NYG E1 5: Isomerase DE63NYG E2 5.1: Racemase/epimerase DE63NYG E3 5.1.3: Carbohydrate racemase/epimerase DE63NYG EC 5.1.3.3 DE63NYG KG Galactose metabolism:hsa00052; Glycolysis / Gluconeogenesis:hsa00010; Metabolic pathways:hsa01100 DE63NYG PD 1SNZ; 1SO0 DE63NYG SQ MASVTRAVFGELPSGGGTVEKFQLQSDLLRVDIISWGCTITALEVKDRQGRASDVVLGFAELEGYLQKQPYFGAVIGRVANRIAKGTFKVDGKEYHLAINKEPNSLHGGVRGFDKVLWTPRVLSNGVQFSRISPDGEEGYPGELKVWVTYTLDGGELIVNYRAQASQATPVNLTNHSYFNLAGQASPNINDHEVTIEADTYLPVDETLIPTGEVAPVQGTAFDLRKPVELGKHLQDFHLNGFDHNFCLKGSKEKHFCARVHHAASGRVLEVYTTQPGVQFYTGNFLDGTLKGKNGAVYPKHSGFCLETQNWPDAVNQPRFPPVLLRPGEEYDHTTWFKFSVA DE63NYG TD Primarily distributed in adrenal. DE63NYG FC This enzyme converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. DE63NYG KD 33208: Metazoa DE63NYG PL 7711: Chordata DE63NYG CL 40674: Mammalia DE63NYG OD 9443: Primates DE63NYG FM 9604: Hominidae DE63NYG GE 9605: Homo DE63NYG SP 9606: Homo sapiens DEDZRQ1 ID DEDZRQ1 DEDZRQ1 DN Cytochrome P450 7A1 (CYP7A1) DEDZRQ1 GN CYP7A1 DEDZRQ1 SN Cytochrome P450 family 7 subfamily A member 1; Cholesterol 7-alpha-hydroxylase; Cholesterol 7-alpha-monooxygenase; CYP7; CYP7A1; CYPVII DEDZRQ1 UC CP7A1_HUMAN DEDZRQ1 RD Bile acid DEDZRQ1 GI 1581 DEDZRQ1 E1 1: Oxidoreductase DEDZRQ1 E2 1.14: Oxygen paired donor oxidoreductase DEDZRQ1 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEDZRQ1 EC 1.14.14.23 DEDZRQ1 RC Endogenous sterols:R-HSA-211976; PPARA activates gene expression:R-HSA-1989781; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368; Synthesis of bile acids and bile salts:R-HSA-192105 DEDZRQ1 KG Bile secretion:hsa04976; Cholesterol metabolism:hsa04979; Metabolic pathways:hsa01100; PPAR signaling pathway:hsa03320; Primary bile acid biosynthesis:hsa00120; Steroid hormone biosynthesis:hsa00140 DEDZRQ1 PD 3DAX; 3SN5; 3V8D DEDZRQ1 SQ MMTTSLIWGIAIAACCCLWLILGIRRRQTGEPPLENGLIPYLGCALQFGANPLEFLRANQRKHGHVFTCKLMGKYVHFITNPLSYHKVLCHGKYFDWKKFHFATSAKAFGHRSIDPMDGNTTENINDTFIKTLQGHALNSLTESMMENLQRIMRPPVSSNSKTAAWVTEGMYSFCYRVMFEAGYLTIFGRDLTRRDTQKAHILNNLDNFKQFDKVFPALVAGLPIHMFRTAHNAREKLAESLRHENLQKRESISELISLRMFLNDTLSTFDDLEKAKTHLVVLWASQANTIPATFWSLFQMIRNPEAMKAATEEVKRTLENAGQKVSLEGNPICLSQAELNDLPVLDSIIKESLRLSSASLNIRTAKEDFTLHLEDGSYNIRKDDIIALYPQLMHLDPEIYPDPLTFKYDRYLDENGKTKTTFYCNGLKLKYYYMPFGSGATICPGRLFAIHEIKQFLILMLSYFELELIEGQAKCPPLDQSRAGLGILPPLNDIEFKYKFKHL DEDZRQ1 TD Primarily distributed in liver. DEDZRQ1 FC This enzyme involves in the metabolism of endogenous cholesterol and its oxygenated derivatives. DEDZRQ1 KD 33208: Metazoa DEDZRQ1 PL 7711: Chordata DEDZRQ1 CL 40674: Mammalia DEDZRQ1 OD 9443: Primates DEDZRQ1 FM 9604: Hominidae DEDZRQ1 GE 9605: Homo DEDZRQ1 SP 9606: Homo sapiens DEXKD7J ID DEXKD7J DEXKD7J DN Carboxypeptidase A4 (CPA4) DEXKD7J GN CPA4 DEXKD7J SN Carboxypeptidase A/B subfamily member 4; Carboxypeptidase A3; CPA3; CPA4; UNQ694/PRO1339 DEXKD7J UC CBPA4_HUMAN DEXKD7J RD GTPL-989 DEXKD7J GI 51200 DEXKD7J E1 3: Hydrolases DEXKD7J E2 3.4: Peptidase DEXKD7J E3 3.4.17: Metallocarboxypeptidase DEXKD7J EC 3.4.17.1 DEXKD7J PD 2BO9; 2BOA; 2PCU; 4A94; 4BD9 DEXKD7J SQ MRWILFIGALIGSSICGQEKFFGDQVLRINVRNGDEISKLSQLVNSNNLKLNFWKSPSSFNRPVDVLVPSVSLQAFKSFLRSQGLEYAVTIEDLQALLDNEDDEMQHNEGQERSSNNFNYGAYHSLEAIYHEMDNIAADFPDLARRVKIGHSFENRPMYVLKFSTGKGVRRPAVWLNAGIHSREWISQATAIWTARKIVSDYQRDPAITSILEKMDIFLLPVANPDGYVYTQTQNRLWRKTRSRNPGSSCIGADPNRNWNASFAGKGASDNPCSEVYHGPHANSEVEVKSVVDFIQKHGNFKGFIDLHSYSQLLMYPYGYSVKKAPDAEELDKVARLAAKALASVSGTEYQVGPTCTTVYPASGSSIDWAYDNGIKFAFTFELRDTGTYGFLLPANQIIPTAEETWLGLKTIMEHVRDNLY DEXKD7J TD Primarily distributed in esophagus and skin. DEXKD7J FC This enzyme can be involved in the histone hyperacetylation pathway. It releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val. DEXKD7J KD 33208: Metazoa DEXKD7J PL 7711: Chordata DEXKD7J CL 40674: Mammalia DEXKD7J OD 9443: Primates DEXKD7J FM 9604: Hominidae DEXKD7J GE 9605: Homo DEXKD7J SP 9606: Homo sapiens DETECWH ID DETECWH DETECWH DN Amiloride-sensitive amine oxidase (AOC1) DETECWH GN AOC1 DETECWH SN Amiloride-sensitive amine oxidase [copper-containing]; Amine oxidase copper domain-containing protein 1; Amiloride-binding protein 1; Diamine oxidase; Histaminase; KAO; Kidney amine oxidase; ABP1; AOC1 DETECWH UC AOC1_HUMAN DETECWH RD Histamine DETECWH GI 26 DETECWH E1 1: Oxidoreductase DETECWH E2 1.4: CH-NH2 donor oxidoreductase DETECWH E3 1.4.3: Oxygen acceptor oxidoreductase DETECWH EC 1.4.3.22 DETECWH RC Neutrophil degranulation:R-HSA-6798695; Phase I - Functionalization of compounds:R-HSA-211945 DETECWH KG Arginine and proline metabolism:hsa00330; Histidine metabolism:hsa00340; Metabolic pathways:hsa01100; Tryptophan metabolism:hsa00380 DETECWH PD 3HI7; 3HIG; 3HII; 3K5T; 3MPH DETECWH SQ MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSSTTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLPGPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDRCLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNGKFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGPRLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYGGHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFEMPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMHATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENITNPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRTYRLQIHSMADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWHPPVVFEQFLHNNENIENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRDNGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV DETECWH TD Primarily distributed in intestine and placenta. DETECWH FC This enzyme catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. DETECWH KD 33208: Metazoa DETECWH PL 7711: Chordata DETECWH CL 40674: Mammalia DETECWH OD 9443: Primates DETECWH FM 9604: Hominidae DETECWH GE 9605: Homo DETECWH SP 9606: Homo sapiens DELOWRJ ID DELOWRJ DELOWRJ DN Alpha-N-acetylglucosaminidase (NAG) DELOWRJ GN NAGLU DELOWRJ SN N-acetyl-alpha-glucosaminidase; Alpha-N-acetylglucosaminidase 77 kDa form; Alpha-N-acetylglucosaminidase 82 kDa form; NAG; NAGLU; UFHSD1 DELOWRJ UC ANAG_HUMAN DELOWRJ RD Human calcitonin DELOWRJ GI 4669 DELOWRJ E1 3: Hydrolases DELOWRJ E2 3.2: Glycosylase DELOWRJ E3 3.2.1: O/S-glycosyl compound glycosidase DELOWRJ EC 3.2.1.50 DELOWRJ RC HS-GAG degradation:R-HSA-2024096; MPS IIIB - Sanfilippo syndrome B:R-HSA-2206282 DELOWRJ KG Glycosaminoglycan degradation:hsa00531; Lysosome:hsa04142; Metabolic pathways:hsa01100 DELOWRJ PD 4XWH DELOWRJ SQ MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKPGLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGELTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYLALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTPVLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELIKEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQFWGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGALEAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAARRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAWRLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAYELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYANKQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPRGDTVDLAKKIFLKYYPRWVAGSW DELOWRJ TD Primarily distributed in liver, ovary, peripheral blood leukocytes, testis, prostate, spleen, colon, lung, placenta and kidney. DELOWRJ FC This enzyme is involved in the degradation of heparan sulfate. DELOWRJ KD 33208: Metazoa DELOWRJ PL 7711: Chordata DELOWRJ CL 40674: Mammalia DELOWRJ OD 9443: Primates DELOWRJ FM 9604: Hominidae DELOWRJ GE 9605: Homo DELOWRJ SP 9606: Homo sapiens DEP7E8X ID DEP7E8X DEP7E8X DN Sulfotransferase 1A3 (SULT1A3) DEP7E8X GN SULT1A3 DEP7E8X SN Sulfotransferase family cytosolic 1A member 3; Aryl sulfotransferase 1A3; Aryl sulfotransferase 3; Aryl sulfotransferase 1A3/1A4; Catecholamine-sulfating phenol sulfotransferase; Monoamine-sulfating phenol sulfotransferase; Placental estrogen sulfotransferase; Sulfotransferase 1A3/1A4; Monoamine-preferring sulfotransferase; TL-PST; Thermolabile phenol sulfotransferase; HAST3; M-PST; ST1A3; STM; SULT1A3 DEP7E8X UC ST1A3_HUMAN DEP7E8X RD Rotigotine DEP7E8X GI 6818 DEP7E8X E1 2: Transferase DEP7E8X E2 2.8: Sulfotransferase DEP7E8X E3 2.8.2: Sulfotransferase DEP7E8X EC 2.8.2.1 DEP7E8X RC Cytosolic sulfonation of small molecules:R-HSA-156584; XBP1(S) activates chaperone genes:R-HSA-381038 DEP7E8X KG Chemical carcinogenesis:hsa05204 DEP7E8X PD 1CJM; 2A3R DEP7E8X SQ MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL DEP7E8X TD Primarily distributed in Liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte. DEP7E8X FC This enzyme utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs. DEP7E8X KD 33208: Metazoa DEP7E8X PL 7711: Chordata DEP7E8X CL 40674: Mammalia DEP7E8X OD 9443: Primates DEP7E8X FM 9604: Hominidae DEP7E8X GE 9605: Homo DEP7E8X SP 9606: Homo sapiens DEL7GFA ID DEL7GFA DEL7GFA DN Sterol Delta(7)-reductase (DHCR7) DEL7GFA GN DHCR7 DEL7GFA SN Delta7-sterol reductase; Sterol reductase SR-2; 7-DHC reductase; 7-dehydrocholesterol reductase; D7SR; DHCR7 DEL7GFA UC DHCR7_HUMAN DEL7GFA RD Desmosterol DEL7GFA GI 1717 DEL7GFA E1 1: Oxidoreductase DEL7GFA E2 1.3: CH-CH donor oxidoreductase DEL7GFA E3 1.3.1: NAD/NADP acceptor oxidoreductase DEL7GFA EC 1.3.1.21 DEL7GFA RC Activation of gene expression by SREBF (SREBP):R-HSA-2426168; Cholesterol biosynthesis via desmosterol:R-HSA-6807047; Cholesterol biosynthesis via lathosterol:R-HSA-6807062 DEL7GFA KG Metabolic pathways:hsa01100; Steroid biosynthesis:hsa00100 DEL7GFA SQ MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF DEL7GFA TD Primarily distributed in liver, adrenal gland, testis and brain. DEL7GFA FC This enzyme reduces C7-C8 double bond of 7-dehydrocholesterol (7-DHC) to produce cholesterol. DEL7GFA KD 33208: Metazoa DEL7GFA PL 7711: Chordata DEL7GFA CL 40674: Mammalia DEL7GFA OD 9443: Primates DEL7GFA FM 9604: Hominidae DEL7GFA GE 9605: Homo DEL7GFA SP 9606: Homo sapiens DEOH5V3 ID DEOH5V3 DEOH5V3 DN Spermine oxidase (SMOX) DEOH5V3 GN SMOX DEOH5V3 SN Polyamine oxidase 1; SMO; SMOX; PAO-1; PAOh1; C20orf16; UNQ3039/PRO9854 DEOH5V3 UC SMOX_HUMAN DEOH5V3 RD KM-1406 DEOH5V3 GI 54498 DEOH5V3 E1 1: Oxidoreductase DEOH5V3 E2 1.5: CH-NH donor oxidoreductase DEOH5V3 E3 1.5.3: Oxygen acceptor oxidoreductase DEOH5V3 EC 1.5.3.16 DEOH5V3 RC Interconversion of polyamines [Q9NWM0-3]:R-HSA-351200; PAOs oxidise polyamines to amines [Q9NWM0-3]:R-HSA-141334 DEOH5V3 KG Arginine and proline metabolism:hsa00330; Metabolic pathways:hsa01100; beta-Alanine metabolism:hsa00410 DEOH5V3 SQ MQSCESSGDSADDPLSRGLRRRGQPRVVVIGAGLAGLAAAKALLEQGFTDVTVLEASSHIGGRVQSVKLGHATFELGATWIHGSHGNPIYHLAEANGLLEETTDGERSVGRISLYSKNGVACYLTNHGRRIPKDVVEEFSDLYNEVYNLTQEFFRHDKPVNAESQNSVGVFTREEVRNRIRNDPDDPEATKRLKLAMIQQYLKVESCESSSHSMDEVSLSAFGEWTEIPGAHHIIPSGFMRVVELLAEGIPAHVIQLGKPVRCIHWDQASARPRGPEIEPRGEGDHNHDTGEGGQGGEEPRGGRWDEDEQWSVVVECEDCELIPADHVIVTVSLGVLKRQYTSFFRPGLPTEKVAAIHRLGIGTTDKIFLEFEEPFWGPECNSLQFVWEDEAESHTLTYPPELWYRKICGFDVLYPPERYGHVLSGWICGEEALVMEKCDDEAVAEICTEMLRQFTGNPNIPKPRRILRSAWGSNPYFRGSYSYTQVGSSGADVEKLAKPLPYTESSKTAPMQVLFSGEATHRKYYSTTHGALLSGQREAARLIEMYRDLFQQGT DEOH5V3 TD Low tissue/organ specificity. DEOH5V3 FC This enzyme catalyzes the oxidation of spermine to spermidine. It can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on the experimental conditions. DEOH5V3 KD 33208: Metazoa DEOH5V3 PL 7711: Chordata DEOH5V3 CL 40674: Mammalia DEOH5V3 OD 9443: Primates DEOH5V3 FM 9604: Hominidae DEOH5V3 GE 9605: Homo DEOH5V3 SP 9606: Homo sapiens DEHJU7E ID DEHJU7E DEHJU7E DN Serum paraoxonase/arylesterase 2 (PON2) DEHJU7E GN PON2 DEHJU7E SN Aromatic esterase 2; Serum aryldialkylphosphatase 2; A-esterase 2; PON 2; PON2 DEHJU7E UC PON2_HUMAN DEHJU7E RD Paraoxon DEHJU7E GI 5445 DEHJU7E E1 3: Hydrolases DEHJU7E E2 3.1: Ester bond hydrolase DEHJU7E E3 3.1.1: Carboxylic ester hydrolase DEHJU7E EC 3.1.1.2 DEHJU7E RC Synthesis of 5-eicosatetraenoic acids:R-HSA-2142688 DEHJU7E SQ MGRLVAVGLLGIALALLGERLLALRNRLKASREVESVDLPHCHLIKGIEAGSEDIDILPNGLAFFSVGLKFPGLHSFAPDKPGGILMMDLKEEKPRARELRISRGFDLASFNPHGISTFIDNDDTVYLFVVNHPEFKNTVEIFKFEEAENSLLHLKTVKHELLPSVNDITAVGPAHFYATNDHYFSDPFLKYLETYLNLHWANVVYYSPNEVKVVAEGFDSANGINISPDDKYIYVADILAHEIHVLEKHTNMNLTQLKVLELDTLVDNLSIDPSSGDIWVGCHPNGQKLFVYDPNNPPSSEVLRIQNILSEKPTVTTVYANNGSVLQGSSVASVYDGKLLIGTLYHRALYCEL DEHJU7E TD Primarily distributed in liver, lung, placenta, testis and heart. DEHJU7E FC This enzyme can hydrolyze lactones and a number of aromatic carboxylic acid esters. DEHJU7E KD 33208: Metazoa DEHJU7E PL 7711: Chordata DEHJU7E CL 40674: Mammalia DEHJU7E OD 9443: Primates DEHJU7E FM 9604: Hominidae DEHJU7E GE 9605: Homo DEHJU7E SP 9606: Homo sapiens DEKOQX7 ID DEKOQX7 DEKOQX7 DN Serine racemase (SRR) DEKOQX7 GN SRR DEKOQX7 SN D-serine ammonia-lyase; D-serine dehydratase; L-serine ammonia-lyase; L-serine dehydratase; SRR DEKOQX7 UC SRR_HUMAN DEKOQX7 RD D-Serine DEKOQX7 GI 63826 DEKOQX7 E1 5: Isomerase DEKOQX7 E2 5.1: Racemase/epimerase DEKOQX7 E3 5.1.1: Amino acid racemase/epimerase DEKOQX7 EC 5.1.1.18 DEKOQX7 RC Serine biosynthesis:R-HSA-977347 DEKOQX7 KG Glycine, serine and threonine metabolism:hsa00260; Metabolic pathways:hsa01100 DEKOQX7 PD 3L6B; 3L6R; 5X2L DEKOQX7 SQ MCAQYCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDLTSSITWVKQAERPASYQSVSV DEKOQX7 TD Primarily distributed in heart, skeletal muscle, kidney and liver. DEKOQX7 FC This enzyme catalyzes the synthesis of D-serine from L-serine. It has dehydratase activity towards both L-serine and D-serine. DEKOQX7 KD 33208: Metazoa DEKOQX7 PL 7711: Chordata DEKOQX7 CL 40674: Mammalia DEKOQX7 OD 9443: Primates DEKOQX7 FM 9604: Hominidae DEKOQX7 GE 9605: Homo DEKOQX7 SP 9606: Homo sapiens DEJVDAT ID DEJVDAT DEJVDAT DN Sepiapterin reductase (SPR) DEJVDAT GN SPR DEJVDAT SN L-threo-7,8-dihydrobiopterin forming sepiapterin reductase; MDSPR; SPR DEJVDAT UC SPRE_HUMAN DEJVDAT RD Menadione DEJVDAT GI 6697 DEJVDAT E1 1: Oxidoreductase DEJVDAT E2 1.1: CH-OH donor oxidoreductase DEJVDAT E3 1.1.1: NAD/NADP oxidoreductase DEJVDAT EC 1.1.1.153 DEJVDAT RC Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation:R-HSA-1474151; eNOS activation:R-HSA-203615 DEJVDAT KG Folate biosynthesis:hsa00790; Metabolic pathways:hsa01100 DEJVDAT PD 4J7U; 4J7X; 4XWY; 4Z3K; 6I6C; 6I6F; 6I6P; 6I6T; 6I6V DEJVDAT SQ MEGGLGRAVCLLTGASRGFGRTLAPLLASLLSPGSVLVLSARNDEALRQLEAELGAERSGLRVVRVPADLGAEAGLQQLLGALRELPRPKGLQRLLLINNAGSLGDVSKGFVDLSDSTQVNNYWALNLTSMLCLTSSVLKAFPDSPGLNRTVVNISSLCALQPFKGWALYCAGKAARDMLFQVLALEEPNVRVLNYAPGPLDTDMQQLARETSVDPDMRKGLQELKAKGKLVDCKVSAQKLLSLLEKDEFKSGAHVDFYDK DEJVDAT TD Primarily distributed in pancreas. DEJVDAT FC This enzyme catalyzes the final one or two reductions in tetra- hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. DEJVDAT KD 33208: Metazoa DEJVDAT PL 7711: Chordata DEJVDAT CL 40674: Mammalia DEJVDAT OD 9443: Primates DEJVDAT FM 9604: Hominidae DEJVDAT GE 9605: Homo DEJVDAT SP 9606: Homo sapiens DEH4TD6 ID DEH4TD6 DEH4TD6 DN Selenocysteine lyase (SCLY) DEH4TD6 GN SCLY DEH4TD6 SN Selenocysteine beta-lyase; L-selenocysteine selenide-lyase; Selenocysteine reductase; SCL; SCLY; hSCL DEH4TD6 UC SCLY_HUMAN DEH4TD6 RD Selenium DEH4TD6 GI 51540 DEH4TD6 E1 4: Lyases DEH4TD6 E2 4.4: Carbon-sulfur lyase DEH4TD6 E3 4.4.1: Carbon-sulfur lyase DEH4TD6 EC 4.4.1.16 DEH4TD6 RC Metabolism of ingested SeMet, Sec, MeSec into H2Se:R-HSA-2408508 DEH4TD6 KG Metabolic pathways:hsa01100; Selenocompound metabolism:hsa00450 DEH4TD6 PD 3GZC; 3GZD DEH4TD6 SQ MEAAVAPGRDAPAPAASQPSGCGKHNSPERKVYMDYNATTPLEPEVIQAMTKAMWEAWGNPSSPYSAGRKAKDIINAARESLAKMIGGKPQDIIFTSGGTESNNLVIHSVVKHFHANQTSKGHTGGHHSPVKGAKPHFITSSVEHDSIRLPLEHLVEEQVAAVTFVPVSKVSGQAEVDDILAAVRPTTRLVTIMLANNETGIVMPVPEISQRIKALNQERVAAGLPPILVHTDAAQALGKQRVDVEDLGVDFLTIVGHKFYGPRIGALYIRGLGEFTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAAELVTQNCEAYEAHMRDVRDYLEERLEAEFGQKRIHLNSQFPGTQRLPNTCNFSIRGPRLQGHVVLAQCRVLMASVGAACHSDHGDQPSPVLLSYGVPFDVARNALRLSVGRSTTRAEVDLVVQDLKQAVAQLEDQA DEH4TD6 TD Low tissue/organ specificity. DEH4TD6 FC This enzyme catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium. DEH4TD6 KD 33208: Metazoa DEH4TD6 PL 7711: Chordata DEH4TD6 CL 40674: Mammalia DEH4TD6 OD 9443: Primates DEH4TD6 FM 9604: Hominidae DEH4TD6 GE 9605: Homo DEH4TD6 SP 9606: Homo sapiens DETH24K ID DETH24K DETH24K DN Red cell/liver pyruvate kinase (PKLR) DETH24K GN PKLR DETH24K SN Pyruvate kinase PKLR; R-type/L-type pyruvate kinase; Pyruvate kinase isozymes L/R; Pyruvate kinase 1; PK1; PKL; PKLR DETH24K UC KPYR_HUMAN DETH24K RD Phosphoenolpyruvate DETH24K GI 5313 DETH24K E1 2: Transferase DETH24K E2 2.7: Kinase DETH24K E3 2.7.1: Phosphotransferase DETH24K EC 2.7.1.40 DETH24K RC ChREBP activates metabolic gene expression [P30613-1]:R-HSA-163765; Glycolysis:R-HSA-70171; Regulation of gene expression in beta cells [P30613-2]:R-HSA-210745 DETH24K KG Biosynthesis of amino acids:hsa01230; Carbon metabolism:hsa01200; Glycolysis / Gluconeogenesis:hsa00010; Insulin signaling pathway:hsa04910; Maturity onset diabetes of the young:hsa04950; Metabolic pathways:hsa01100; Non-alcoholic fatty liver disease (NAFLD):hsa04932; Purine metabolism:hsa00230; Pyruvate metabolism:hsa00620; Type II diabetes mellitus:hsa04930 DETH24K PD 2VGB; 2VGF; 2VGG; 4IMA; 4IP7; 6NN4; 6NN5; 6NN7; 6NN8 DETH24K SQ MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS DETH24K TD Primarily distributed in intestine, kidney and liver. DETH24K FC This enzyme plays a key role in glycolysis. DETH24K KD 33208: Metazoa DETH24K PL 7711: Chordata DETH24K CL 40674: Mammalia DETH24K OD 9443: Primates DETH24K FM 9604: Hominidae DETH24K GE 9605: Homo DETH24K SP 9606: Homo sapiens DE3OALH ID DE3OALH DE3OALH DN Prostaglandin E synthase 2 (PTGES2) DE3OALH GN PTGES2 DE3OALH SN Prostaglandin E synthase 2 truncated form; Prostaglandin-H(2) E-isomerase; mPGE synthase-2; Membrane-associated prostaglandin E synthase-2; Microsomal prostaglandin E synthase 2; PGES2; PTGES2; mPGES-2; C9orf15 DE3OALH UC PGES2_HUMAN DE3OALH RD NSC-6292 DE3OALH GI 80142 DE3OALH E1 5: Isomerase DE3OALH E2 5.3: Intramolecular oxidoreductase DE3OALH E3 5.3.99: Intramolecular oxidoreductase DE3OALH EC 5.3.99.3 DE3OALH RC Neutrophil degranulation:R-HSA-6798695; Synthesis of Prostaglandins (PG) and Thromboxanes (TX):R-HSA-2162123 DE3OALH KG Arachidonic acid metabolism:hsa00590; Metabolic pathways:hsa01100 DE3OALH SQ MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLGAAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH DE3OALH TD Primarily distributed in skeletal. DE3OALH FC This enzyme catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2). DE3OALH KD 33208: Metazoa DE3OALH PL 7711: Chordata DE3OALH CL 40674: Mammalia DE3OALH OD 9443: Primates DE3OALH FM 9604: Hominidae DE3OALH GE 9605: Homo DE3OALH SP 9606: Homo sapiens DEW7V0G ID DEW7V0G DEW7V0G DN Polyamine oxidase (PAOX) DEW7V0G GN PAOX DEW7V0G SN Peroxisomal N(1)-acetyl-spermine/spermidine oxidase; PAO; PAOX; UNQ1923/PRO4398 DEW7V0G UC PAOX_HUMAN DEW7V0G RD KM-1406 DEW7V0G GI 196743 DEW7V0G E1 1: Oxidoreductase DEW7V0G E2 1.5: CH-NH donor oxidoreductase DEW7V0G E3 1.5.3: Oxygen acceptor oxidoreductase DEW7V0G EC 1.5.3.13 DEW7V0G RC Interconversion of polyamines:R-HSA-351200; PAOs oxidise polyamines to amines:R-HSA-141334; Peroxisomal protein import:R-HSA-9033241 DEW7V0G KG Peroxisome:hsa04146 DEW7V0G SQ MESTGSVGEAPGGPRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLEATARAGGRIRSERCFGGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLVETGGHVGLPSVSYASSGASVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKEIGQHVAGWTEDEETRKLKLAVLNSFFNLECCVSGTHSMDLVALAPFGEYTVLPGLDCTFSKGYQGLTNCMMAALPEDTVVFEKPVKTIHWNGSFQEAAFPGETFPVSVECEDGDRFPAHHVIVTVPLGFLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFLEFEEPFWEPDCQLIQLVWEDTSPLEDAAPELQDAWFRKLIGFVVLPAFASVHVLCGFIAGLESEFMETLSDEEVLLCLTQVLRRVTGNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLLAQPLPADGAGAQLQILFAGEATHRTFYSTTHGALLSGWREADRLLSLWAPQVQQPRPRL DEW7V0G TD Primarily distributed in testis. DEW7V0G FC This enzyme catalyzes the oxidation of N(1)- acetylspermine to spermidine and is thus involved in the polyamine back-conversion. It can also oxidize N(1)- acetylspermidine to putrescine. Substrate specificity: N(1)- acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. But it does not oxidize spermidine. DEW7V0G KD 33208: Metazoa DEW7V0G PL 7711: Chordata DEW7V0G CL 40674: Mammalia DEW7V0G OD 9443: Primates DEW7V0G FM 9604: Hominidae DEW7V0G GE 9605: Homo DEW7V0G SP 9606: Homo sapiens DE2HB58 ID DE2HB58 DE2HB58 DN Nicotinate-nucleotide adenylyltransferase 2 (NMNAT2) DE2HB58 GN NMNAT2 DE2HB58 SN NMN adenylyltransferase 2; NMN/NaMN adenylyltransferase 2; NaMN adenylyltransferase 2; Nicotinamide mononucleotide adenylyltransferase 2; Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2; NMNAT2; C1orf15; KIAA0479 DE2HB58 UC NMNA2_HUMAN DE2HB58 RD Nicotinate-MN DE2HB58 GI 23057 DE2HB58 E1 2: Transferase DE2HB58 E2 2.7: Kinase DE2HB58 E3 2.7.7: Nucleotidyltransferase DE2HB58 EC 2.7.7.1 DE2HB58 RC Nicotinate metabolism:R-HSA-196807 DE2HB58 KG Metabolic pathways:hsa01100; Nicotinate and nicotinamide metabolism:hsa00760 DE2HB58 SQ MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG DE2HB58 TD Primarily distributed in brain, particularly in incerebrum, cerebellum, occipital lobe, frontal lobe, temporal lobe and putamen. DE2HB58 FC This enzyme catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. It can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency but cannot use triazofurin monophosphate (TrMP) as substrate. It also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). DE2HB58 KD 33208: Metazoa DE2HB58 PL 7711: Chordata DE2HB58 CL 40674: Mammalia DE2HB58 OD 9443: Primates DE2HB58 FM 9604: Hominidae DE2HB58 GE 9605: Homo DE2HB58 SP 9606: Homo sapiens DEMWKYT ID DEMWKYT DEMWKYT DN Neutral alpha-glucosidase AB (GANAB) DEMWKYT GN GANAB DEMWKYT SN Alpha-glucosidase 2; Glucosidase II subunit alpha; G2AN; GANAB; KIAA0088 DEMWKYT UC GANAB_HUMAN DEMWKYT RD PNA-D-glucopyranoside DEMWKYT GI 23193 DEMWKYT E1 3: Hydrolases DEMWKYT E2 3.2: Glycosylase DEMWKYT E3 3.2.1: O/S-glycosyl compound glycosidase DEMWKYT EC 3.2.1.207 DEMWKYT RC Calnexin/calreticulin cycle:R-HSA-901042; N-glycan trimming in the ER and Calnexin/Calreticulin cycle:R-HSA-532668 DEMWKYT KG Metabolic pathways:hsa01100; N-Glycan biosynthesis:hsa00510; Protein processing in endoplasmic reticulum:hsa04141 DEMWKYT SQ MAAVAAVAARRRRSWASLVLAFLGVCLGITLAVDRSNFKTCEESSFCKRQRSIRPGLSPYRALLDSLQLGPDSLTVHLIHEVTKVLLVLELQGLQKNMTRFRIDELEPRRPRYRVPDVLVADPPIARLSVSGRDENSVELTMAEGPYKIILTARPFRLDLLEDRSLLLSVNARGLLEFEHQRAPRVSQGSKDPAEGDGAQPEETPRDGDKPEETQGKAEKDEPGAWEETFKTHSDSKPYGPMSVGLDFSLPGMEHVYGIPEHADNLRLKVTEGGEPYRLYNLDVFQYELYNPMALYGSVPVLLAHNPHRDLGIFWLNAAETWVDISSNTAGKTLFGKMMDYLQGSGETPQTDVRWMSETGIIDVFLLLGPSISDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHNLPCDVIWLDIEHADGKRYFTWDPSRFPQPRTMLERLASKRRKLVAIVDPHIKVDSGYRVHEELRNLGLYVKTRDGSDYEGWCWPGSAGYPDFTNPTMRAWWANMFSYDNYEGSAPNLFVWNDMNEPSVFNGPEVTMLKDAQHYGGWEHRDVHNIYGLYVHMATADGLRQRSGGMERPFVLARAFFAGSQRFGAVWTGDNTAEWDHLKISIPMCLSLGLVGLSFCGADVGGFFKNPEPELLVRWYQMGAYQPFFRAHAHLDTGRREPWLLPSQHNDIIRDALGQRYSLLPFWYTLLYQAHREGIPVMRPLWVQYPQDVTTFNIDDQYLLGDALLVHPVSDSGAHGVQVYLPGQGEVWYDIQSYQKHHGPQTLYLPVTLSSIPVFQRGGTIVPRWMRVRRSSECMKDDPITLFVALSPQGTAQGELFLDDGHTFNYQTRQEFLLRRFSFSGNTLVSSSADPEGHFETPIWIERVVIIGAGKPAAVVLQTKGSPESRLSFQHDPETSVLVLRKPGINVASDWSIHLR DEMWKYT TD Primarily distributed in kidney and liver. DEMWKYT FC This enzyme cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. DEMWKYT KD 33208: Metazoa DEMWKYT PL 7711: Chordata DEMWKYT CL 40674: Mammalia DEMWKYT OD 9443: Primates DEMWKYT FM 9604: Hominidae DEMWKYT GE 9605: Homo DEMWKYT SP 9606: Homo sapiens DEAPJSO ID DEAPJSO DEAPJSO DN Microsomal glutathione S-transferase 1 (MGST1) DEAPJSO GN MGST1 DEAPJSO SN Microsomal GST-1; Microsomal GST-I; GST12; MGST; MGST1 DEAPJSO UC MGST1_HUMAN DEAPJSO RD Glyceryl trinitrate DEAPJSO GI 4257 DEAPJSO E1 2: Transferase DEAPJSO E2 2.5: Alkyl/aryl transferase DEAPJSO E3 2.5.1: Alkyl/aryl transferase DEAPJSO EC 2.5.1.18 DEAPJSO RC Aflatoxin activation and detoxification:R-HSA-5423646; Glutathione conjugation:R-HSA-156590; Neutrophil degranulation:R-HSA-6798695 DEAPJSO KG Chemical carcinogenesis:hsa05204; Drug metabolism - cytochrome P450:hsa00982; Drug metabolism - other enzymes:hsa00983; Fluid shear stress and atherosclerosis:hsa05418; Glutathione metabolism:hsa00480; Hepatocellular carcinoma:hsa05225; Metabolic pathways:hsa01100; Metabolism of xenobiotics by cytochrome P450:hsa00980; Pathways in cancer:hsa05200; Platinum drug resistance:hsa01524 DEAPJSO SQ MVDLTQVMDDEVFMAFASYATIILSKMMLMSTATAFYRLTRKVFANPEDCVAFGKGENAKKYLRTDDRVERVRRAHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIAYLTPLPQPNRALSFFVGYGVTLSMAYRLLKSKLYL DEAPJSO TD Primarily distributed in liver. DEAPJSO FC This enzyme has a wide substrate specificity and it conjugates of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. DEAPJSO KD 33208: Metazoa DEAPJSO PL 7711: Chordata DEAPJSO CL 40674: Mammalia DEAPJSO OD 9443: Primates DEAPJSO FM 9604: Hominidae DEAPJSO GE 9605: Homo DEAPJSO SP 9606: Homo sapiens DELNI4J ID DELNI4J DELNI4J DN Lecithin-cholesterol acyltransferase (LCAT) DELNI4J GN LCAT DELNI4J SN Phosphatidylcholine-sterol acyltransferase; Phospholipid-cholesterol acyltransferase; LCAT DELNI4J UC LCAT_HUMAN DELNI4J RD Phosphatidylcholine DELNI4J GI 3931 DELNI4J E1 2: Transferase DELNI4J E2 2.3: Acyltransferase DELNI4J E3 2.3.1: Acyltransferase DELNI4J EC 2.3.1.43 DELNI4J RC HDL remodeling:R-HSA-8964058 DELNI4J KG Cholesterol metabolism:hsa04979; Glycerophospholipid metabolism:hsa00564 DELNI4J PD 4X96; 4XWG; 4XX1; 5BV7; 5TXF; 6MVD DELNI4J SQ MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLGAYRQGPPASPTASPEPPPPE DELNI4J TD Primarily distributed in brain and liver. DELNI4J FC This enzyme is central in the extracellular metabolism of plasma lipoproteins. It converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs). DELNI4J KD 33208: Metazoa DELNI4J PL 7711: Chordata DELNI4J CL 40674: Mammalia DELNI4J OD 9443: Primates DELNI4J FM 9604: Hominidae DELNI4J GE 9605: Homo DELNI4J SP 9606: Homo sapiens DEBJ2NL ID DEBJ2NL DEBJ2NL DN Inositol polyphosphate 4-phosphatase I (INPP4A) DEBJ2NL GN INPP4A DEBJ2NL SN Inositol polyphosphate 4-phosphatase type I; Inositol polyphosphate-4-phosphatase type I A; Type I inositol 3,4-bisphosphate 4-phosphatase; INPP4A DEBJ2NL UC INP4A_HUMAN DEBJ2NL RD DMI-trisphosphate DEBJ2NL GI 3631 DEBJ2NL E1 3: Hydrolases DEBJ2NL E2 3.1: Ester bond hydrolase DEBJ2NL E3 3.1.3: Phosphoric monoester hydrolase DEBJ2NL EC 3.1.3.66 DEBJ2NL RC Synthesis of IP2, IP, and Ins in the cytosol:R-HSA-1855183; Synthesis of PIPs at the early endosome membrane:R-HSA-1660516; Synthesis of PIPs at the plasma membrane:R-HSA-1660499 DEBJ2NL KG Inositol phosphate metabolism:hsa00562; Metabolic pathways:hsa01100; Phosphatidylinositol signaling system:hsa04070 DEBJ2NL SQ MTAREHSPRHGARARAMQRASTIDVAADMLGLSLAGNIQDPDEPILEFSLACSELHTPSLDRKPNSFVAVSVTTPPQAFWTKHAQTEIIEGTNNPIFLSSIAFFQDSLINQMTQVKLSVYDVKDRSQGTMYLLGSGTFIVKDLLQDRHHRLHLTLRSAESDRVGNITVIGWQMEEKSDQRPPVTRSVDTVNGRMVLPVDESLTEALGIRSKYASLRKDTLLKSVFGGAICRMYRFPTTDGNHLRILEQMAESVLSLHVPRQFVKLLLEEDAARVCELEELGELSPCWESLRRQIVTQYQTIILTYQENLTDLHQYRGPSFKASSLKADKKLEFVPTNLHIQRMRVQDDGGSDQNYDIVTIGAPAAHCQGFKSGGLRKKLHKFEETKKHFEECCTSSGCQSIIYIPQDVVRAKEIIAQINTLKTQVSYYAERLSRAAKDRSATGLERTLAILADKTRQLVTVCDCKLLANSIHGLNAARPDYIASKASPTSTEEEQVMLRNDQDTLMARWTGRNSRSSLQVDWHEEEWEKVWLNVDKSLECIIQRVDKLLQKERLHGEGCEDVFPCAGSCTSKKGNPDSHAYWIRPEDPFCDVPSSPCPSTMPSTACHPHLTTHCSPPPEESSPGEWSEALYPLLTTLTDCVAMMSDKAKKAMVFLLMQDSAPTIATYLSLQYRRDVVFCQTLTALICGFIIKLRNCLHDDGFLRQLYTIGLLAQFESLLSTYGEELAMLEDMSLGIMDLRNVTFKVTQATSSASADMLPVITGNRDGFNVRVPLPGPLFDALPREIQSGMLLRVQPVLFNVGINEQQTLAERFGDTSLQEVINVESLVRLNSYFEQFKEVLPEDCLPRSRSQTCLPELLRFLGQNVHARKNKNVDILWQAAEICRRLNGVRFTSCKSAKDRTAMSVTLEQCLILQHEHGMAPQVFTQALECMRSEGCRRENTMKNVGSRKYAFNSLQLKAFPKHYRPPEGTYGKVET DEBJ2NL TD Low tissue/organ specificity. DEBJ2NL FC This enzyme catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2). It also catalyzes inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. DEBJ2NL KD 33208: Metazoa DEBJ2NL PL 7711: Chordata DEBJ2NL CL 40674: Mammalia DEBJ2NL OD 9443: Primates DEBJ2NL FM 9604: Hominidae DEBJ2NL GE 9605: Homo DEBJ2NL SP 9606: Homo sapiens DEWO724 ID DEWO724 DEWO724 DN HIF-prolyl hydroxylase 2 (EGLN1) DEWO724 GN EGLN1 DEWO724 SN Hypoxia-inducible factor prolyl hydroxylase 2; Prolyl hydroxylase domain-containing protein 2; Egl nine homolog 1; PHD2; PNAS-118; PNAS-137; SM-20; EGLN1; HIF-PH2; HPH-2; C1orf12 DEWO724 UC EGLN1_HUMAN DEWO724 RD Ascorbic acid DEWO724 GI 54583 DEWO724 E1 1: Oxidoreductase DEWO724 E2 1.14: Oxygen paired donor oxidoreductase DEWO724 E3 1.14.11: 2-oxoglutarate donor oxidoreductase DEWO724 EC 1.14.11.29 DEWO724 RC Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha:R-HSA-1234176 DEWO724 KG HIF-1 signaling pathway:hsa04066; Pathways in cancer:hsa05200; Renal cell carcinoma:hsa05211 DEWO724 PD 2HBT; 2HBU; 2Y33; 2Y34; 3HQR; 3HQU; 3OUH; 3OUI; 3OUJ DEWO724 SQ MANDSGGPGGPSPSERDRQYCELCGKMENLLRCSRCRSSFYCCKEHQRQDWKKHKLVCQGSEGALGHGVGPHQHSGPAPPAAVPPPRAGAREPRKAAARRDNASGDAAKGKVKAKPPADPAAAASPCRAAAGGQGSAVAAEAEPGKEEPPARSSLFQEKANLYPPSNTPGDALSPGGGLRPNGQTKPLPALKLALEYIVPCMNKHGICVVDDFLGKETGQQIGDEVRALHDTGKFTDGQLVSQKSDSSKDIRGDKITWIEGKEPGCETIGLLMSSMDDLIRHCNGKLGSYKINGRTKAMVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF DEWO724 TD Primarily distributed in blood and skeletal muscle. DEWO724 FC This enzyme catalyses the hydroxylation of two sites on HIF-. DEWO724 KD 33208: Metazoa DEWO724 PL 7711: Chordata DEWO724 CL 40674: Mammalia DEWO724 OD 9443: Primates DEWO724 FM 9604: Hominidae DEWO724 GE 9605: Homo DEWO724 SP 9606: Homo sapiens DEQPEMB ID DEQPEMB DEQPEMB DN Glutathione S-transferase zeta-1 (GSTZ1) DEQPEMB GN GSTZ1 DEQPEMB SN Glutathione S-transferase zeta 1; Maleylacetoacetate isomerase; GSTZ1; GSTZ1-1; MAAI DEQPEMB UC MAAI_HUMAN DEQPEMB RD CPC-211 DEQPEMB GI 2954 DEQPEMB E1 2: Transferase DEQPEMB E2 2.5: Alkyl/aryl transferase DEQPEMB E3 2.5.1: Alkyl/aryl transferase DEQPEMB EC 2.5.1.18 DEQPEMB RC Glutathione conjugation:R-HSA-156590; Regulation of pyruvate dehydrogenase (PDH) complex:R-HSA-204174; Tyrosine catabolism:R-HSA-8963684 DEQPEMB KG Metabolic pathways:hsa01100; Tyrosine metabolism:hsa00350 DEQPEMB PD 1FW1 DEQPEMB SQ MQAGKPILYSYFRSSCSWRVRIALALKGIDYKTVPINLIKDRGQQFSKDFQALNPMKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQNLSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAERFKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA DEQPEMB TD Primarily distributed in liver. Also expressed in kidney, skeletal muscle, brain, melanocytes, synovium, placenta, breast, fetal liver and heart. DEQPEMB FC This enzyme shows minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity, and it can catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. DEQPEMB KD 33208: Metazoa DEQPEMB PL 7711: Chordata DEQPEMB CL 40674: Mammalia DEQPEMB OD 9443: Primates DEQPEMB FM 9604: Hominidae DEQPEMB GE 9605: Homo DEQPEMB SP 9606: Homo sapiens DE073GW ID DE073GW DE073GW DN Glucosidase II beta (PRKCSH) DE073GW GN PRKCSH DE073GW SN Glucosidase 2 subunit beta; Glucosidase II subunit beta; Protein kinase C substrate 60.1 kDa protein heavy chain; 80K-H protein; G19P1; PKCSH; PRKCSH DE073GW UC GLU2B_HUMAN DE073GW RD PNA-D-glucopyranoside DE073GW GI 5589 DE073GW E1 3: Hydrolases DE073GW E2 3.2: Glycosylase DE073GW E3 3.2.1: O/S-glycosyl compound glycosidase DE073GW EC 3.2.1.84 DE073GW RC Advanced glycosylation endproduct receptor signaling:R-HSA-879415; Calnexin/calreticulin cycle:R-HSA-901042; N-glycan trimming in the ER and Calnexin/Calreticulin cycle:R-HSA-532668; Post-translational protein phosphorylation:R-HSA-8957275; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs):R-HSA-381426 DE073GW KG Protein processing in endoplasmic reticulum:hsa04141 DE073GW SQ MLLPLLLLLPMCWAVEVKRPRGVSLTNHHFYDESKPFTCLDGSATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYIPSNRVNDGVCDCCDGTDEYNSGVICENTCKEKGRKERESLQQMAEVTREGFRLKKILIEDWKKAREEKQKKLIELQAGKKSLEDQVEMLRTVKEEAEKPEREAKEQHQKLWEEQLAAAKAQQEQELAADAFKELDDDMDGTVSVTELQTHPELDTDGDGALSEAEAQALLSGDTQTDATSFYDRVWAAIRDKYRSEALPTDLPAPSAPDLTEPKEEQPPVPSSPTEEEEEEEEEEEEEAEEEEEEEDSEEAPPPLSPPQPASPAEEDKMPPYDEQTQAFIDAAQEARNKFEEAERSLKDMEESIRNLEQEISFDFGPNGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKLGGSPTSLGTWGSWIGPDHDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETMVTSTTEPSRCEYLMELMTPAACPEPPPEAPTEDDHDEL DE073GW TD Low tissue/organ specificity. DE073GW FC This enzyme is a regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. DE073GW KD 33208: Metazoa DE073GW PL 7711: Chordata DE073GW CL 40674: Mammalia DE073GW OD 9443: Primates DE073GW FM 9604: Hominidae DE073GW GE 9605: Homo DE073GW SP 9606: Homo sapiens DEPJGQB ID DEPJGQB DEPJGQB DN Glucosamine-6-phosphate deaminase 2 (GNPDA2) DEPJGQB GN GNPDA2 DEPJGQB SN Glucosamine-6-phosphate isomerase 2; Glucosamine-6-phosphate isomerase SB52; GlcN6P deaminase 2; GNP2; GNPDA 2; GNPDA2 DEPJGQB UC GNPI2_HUMAN DEPJGQB RD D-glucosamine-phosphate DEPJGQB GI 132789 DEPJGQB E1 3: Hydrolases DEPJGQB E2 3.5: Carbon-nitrogen hydrolase DEPJGQB E3 3.5.99: Carbon-nitrogen hydrolase DEPJGQB EC 3.5.99.6 DEPJGQB RC Glycolysis:R-HSA-70171 DEPJGQB KG Amino sugar and nucleotide sugar metabolism:hsa00520; Metabolic pathways:hsa01100 DEPJGQB SQ MRLVILDNYDLASEWAAKYICNRIIQFKPGQDRYFTLGLPTGSTPLGCYKKLIEYHKNGHLSFKYVKTFNMDEYVGLPRNHPESYHSYMWNNFFKHIDIDPNNAHILDGNAADLQAECDAFENKIKEAGGIDLFVGGIGPDGHIAFNEPGSSLVSRTRLKTLAMDTILANAKYFDGDLSKVPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTIFVCDEDATLELRVKTVKYFKGLMHVHNKLVDPLFSMKDGN DEPJGQB TD Low tissue/organ specificity. DEPJGQB FC This enzyme catalyzes the deamination of the glucosamine-6-phosphate involved in the hexosamine signaling pathway. DEPJGQB KD 33208: Metazoa DEPJGQB PL 7711: Chordata DEPJGQB CL 40674: Mammalia DEPJGQB OD 9443: Primates DEPJGQB FM 9604: Hominidae DEPJGQB GE 9605: Homo DEPJGQB SP 9606: Homo sapiens DELB4KP ID DELB4KP DELB4KP DN Epoxide hydrolase 1 (EPHX1) DELB4KP GN EPHX1 DELB4KP SN Epoxide hydratase; Microsomal epoxide hydrolase; mEH; EPHX; EPHX1; EPOX DELB4KP UC HYEP_HUMAN DELB4KP RD Carbamazepine DELB4KP GI 2052 DELB4KP E1 3: Hydrolases DELB4KP E2 3.3: Ether hydrolase DELB4KP E3 3.3.2: Ether hydrolase DELB4KP EC 3.3.2.9 DELB4KP RC Phase I - Functionalization of compounds:R-HSA-211945 DELB4KP KG Bile secretion:hsa04976; Chemical carcinogenesis:hsa05204; Metabolism of xenobiotics by cytochrome P450:hsa00980 DELB4KP SQ MWLEILLTSVLGFAIYWFISRDKEETLPLEDGWWGPGTRSAAREDDSIRPFKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNEFDWKKQVEILNRYPHFKTKIEGLDIHFIHVKPPQLPAGHTPKPLLMVHGWPGSFYEFYKIIPLLTDPKNHGLSDEHVFEVICPSIPGYGFSEASSKKGFNSVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNMALVLSNFSTLTLLLGQRFGRFLGLTERDVELLYPVKEKVFYSLMRESGYMHIQCTKPDTVGSALNDSPVGLAAYILEKFSTWTNTEFRYLEDGGLERKFSLDDLLTNVMLYWTTGTIISSQRFYKENLGQGWMTQKHERMKVYVPTGFSAFPFELLHTPEKWVRFKYPKLISYSYMVRGGHFAAFEEPELLAQDIRKFLSVLERQ DELB4KP TD Primarily distributed in adrenal gland and liver. DELB4KP FC This enzyme catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water. DELB4KP KD 33208: Metazoa DELB4KP PL 7711: Chordata DELB4KP CL 40674: Mammalia DELB4KP OD 9443: Primates DELB4KP FM 9604: Hominidae DELB4KP GE 9605: Homo DELB4KP SP 9606: Homo sapiens DE0EUXB ID DE0EUXB DE0EUXB DN Dihydropyrimidinase-related protein 1 (DRP1) DE0EUXB GN CRMP1 DE0EUXB SN Collapsin response mediator protein 1; Inactive dihydropyrimidinase; Unc-33-like phosphoprotein 3; CRMP-1; CRMP1; DPYSL1; DRP-1; ULIP-3; ULIP3 DE0EUXB UC DPYL1_HUMAN DE0EUXB RD Dexrazoxane hydrochloride DE0EUXB GI 1400 DE0EUXB E1 3: Hydrolases DE0EUXB E2 3.5: Carbon-nitrogen hydrolase DE0EUXB E3 3.5.2: Cyclic amide hydrolase DE0EUXB EC 3.5.2.2 DE0EUXB RC CRMPs in Sema3A signaling:R-HSA-399956 DE0EUXB PD 4B3Z DE0EUXB SQ MSYQGKKSIPHITSDRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFPEHLYQRVKIRNKVFGLQGVSRGMYDGPVYEVPATPKYATPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG DE0EUXB TD Primarily distributed in brain and pituitary gland. DE0EUXB FC This enzyme has hydrolase activity and hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides. DE0EUXB KD 33208: Metazoa DE0EUXB PL 7711: Chordata DE0EUXB CL 40674: Mammalia DE0EUXB OD 9443: Primates DE0EUXB FM 9604: Hominidae DE0EUXB GE 9605: Homo DE0EUXB SP 9606: Homo sapiens DEGTB1K ID DEGTB1K DEGTB1K DN Dehydrogenase/reductase retSDR3 (HSD17B14) DEGTB1K GN HSD17B14 DEGTB1K SN Retinal short-chain dehydrogenase/reductase retSDR3; Short chain dehydrogenase/reductase family 47C member 1; Dehydrogenase/reductase SDR family member 10; 17-beta-hydroxysteroid dehydrogenase 14; 17-beta-hydroxysteroid dehydrogenase DHRS10; UNQ502/PRO474; 17-beta-HSD 14; HSD17B14; SDR3; SDR47C1; DHRS10 DEGTB1K UC DHB14_HUMAN DEGTB1K RD Testosterone cypionate DEGTB1K GI 51171 DEGTB1K E1 1: Oxidoreductase DEGTB1K E2 1.1: CH-OH donor oxidoreductase DEGTB1K E3 1.1.1: NAD/NADP oxidoreductase DEGTB1K EC 1.1.1.62 DEGTB1K RC Estrogen biosynthesis:R-HSA-193144 DEGTB1K PD 1YDE; 5EN4; 5HS6 DEGTB1K SQ MATGTRYAGKVVVVTGGGRGIGAGIVRAFVNSGARVVICDKDESGGRALEQELPGAVFILCDVTQEDDVKTLVSETIRRFGRLDCVVNNAGHHPPPQRPEETSAQGFRQLLELNLLGTYTLTKLALPYLRKSQGNVINISSLVGAIGQAQAVPYVATKGAVTAMTKALALDESPYGVRVNCISPGNIWTPLWEELAALMPDPRATIREGMLAQPLGRMGQPAEVGAAAVFLASEANFCTGIELLVTGGAELGYGCKASRSTPVDAPDIPS DEGTB1K TD Primarily distributed in brain, placenta, liver and kidney. DEGTB1K FC This enzyme has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. And it converts oestradiol to oestrone. DEGTB1K KD 33208: Metazoa DEGTB1K PL 7711: Chordata DEGTB1K CL 40674: Mammalia DEGTB1K OD 9443: Primates DEGTB1K FM 9604: Hominidae DEGTB1K GE 9605: Homo DEGTB1K SP 9606: Homo sapiens DE8PQ7T ID DE8PQ7T DE8PQ7T DN D-aspartate oxidase (DDO) DE8PQ7T GN DDO DE8PQ7T SN Aspartic oxidase; D-aspartic oxidase; D-Asp oxidase; ChDASPO; ChDDO; DASOX; DDO DE8PQ7T UC OXDD_HUMAN DE8PQ7T RD Glutamic acid DE8PQ7T GI 8528 DE8PQ7T E1 1: Oxidoreductase DE8PQ7T E2 1.4: CH-NH2 donor oxidoreductase DE8PQ7T E3 1.4.3: Oxygen acceptor oxidoreductase DE8PQ7T EC 1.4.3.1 DE8PQ7T RC Glyoxylate metabolism and glycine degradation:R-HSA-389661; Peroxisomal protein import:R-HSA-9033241 DE8PQ7T KG Alanine, aspartate and glutamate metabolism:hsa00250; Metabolic pathways:hsa01100; Peroxisome:hsa04146 DE8PQ7T SQ MDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL DE8PQ7T TD Low tissue/organ specificity. DE8PQ7T FC This enzyme selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. DE8PQ7T KD 33208: Metazoa DE8PQ7T PL 7711: Chordata DE8PQ7T CL 40674: Mammalia DE8PQ7T OD 9443: Primates DE8PQ7T FM 9604: Hominidae DE8PQ7T GE 9605: Homo DE8PQ7T SP 9606: Homo sapiens DETL4WB ID DETL4WB DETL4WB DN Cytochrome P450 8B1 (CYP8B1) DETL4WB GN CYP8B1 DETL4WB SN Cytochrome P450 family 8 subfamily B member 1; 7-alpha-hydroxy-4-cholesten-3-one 12-alpha-hydroxylase; 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase; CYP12; CYP8B1; CYPVIIIB1; Sterol 12-alpha-hydroxylase DETL4WB UC CP8B1_HUMAN DETL4WB RD Chenodeoxycholic acid DETL4WB GI 1582 DETL4WB E1 1: Oxidoreductase DETL4WB E2 1.14: Oxygen paired donor oxidoreductase DETL4WB E3 1.14.18: Oxygen paired donor oxidoreductase DETL4WB EC 1.14.18.8 DETL4WB RC Eicosanoids:R-HSA-211979; Nicotinamide salvaging:R-HSA-197264; Sterols are 12-hydroxylated by CYP8B1:R-HSA-211994; Synthesis of Prostaglandins (PG) and Thromboxanes (TX):R-HSA-2162123; Synthesis of bile acids and bile salts via 24-hydroxycholesterol:R-HSA-193775; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368 DETL4WB KG Metabolic pathways:hsa01100; PPAR signaling pathway:hsa03320; Primary bile acid biosynthesis:hsa00120 DETL4WB SQ MVLWGPVLGALLVVIAGYLCLPGMLRQRRPWEPPLDKGTVPWLGHAMAFRKNMFEFLKRMRTKHGDVFTVQLGGQYFTFVMDPLSFGSILKDTQRKLDFGQYAKKLVLKVFGYRSVQGDHEMIHSASTKHLRGDGLKDLNETMLDSLSFVMLTSKGWSLDASCWHEDSLFRFCYYILFTAGYLSLFGYTKDKEQDLLQAGELFMEFRKFDLLFPRFVYSLLWPREWLEVGRLQRLFHKMLSVSHSQEKEGISNWLGNMLQFLREQGVPSAMQDKFNFMMLWASQGNTGPTSFWALLYLLKHPEAIRAVREEATQVLGEARLETKQSFAFKLGALQHTPVLDSVVEETLRLRAAPTLLRLVHEDYTLKMSSGQEYLFRHGDILALFPYLSVHMDPDIHPEPTVFKYDRFLNPNGSRKVDFFKTGKKIHHYTMPWGSGVSICPGRFFALSEVKLFILLMVTHFDLELVDPDTPLPHVDPQRWGFGTMQPSHDVRFRYRLHPTE DETL4WB TD Primarily distributed in liver. DETL4WB FC This enzyme involves in bile acid synthesis and is responsible for the conversion of 7 alpha-hydroxy-4-cholesten-3-one into 7 alpha, 12 alpha-dihydroxy-4-cholesten-3-one. And it is responsible for the balance between formation of cholic acid and chenodeoxycholic acid. Has a rather broad substrate specificity including a number of 7-alpha-hydroxylated C27 steroids. DETL4WB KD 33208: Metazoa DETL4WB PL 7711: Chordata DETL4WB CL 40674: Mammalia DETL4WB OD 9443: Primates DETL4WB FM 9604: Hominidae DETL4WB GE 9605: Homo DETL4WB SP 9606: Homo sapiens DE36TMY ID DE36TMY DE36TMY DN Cytochrome P450 7B1 (CYP7B1) DE36TMY GN CYP7B1 DE36TMY SN Cytochrome P450 family 7 subfamily B member 1; 25/26-hydroxycholesterol 7-alpha-hydroxylase; 3-hydroxysteroid 7-alpha hydroxylase; CYP7B1 DE36TMY UC CP7B1_HUMAN DE36TMY RD Dehydroepiandrosterone DE36TMY GI 9420 DE36TMY E1 1: Oxidoreductase DE36TMY E2 1.14: Oxygen paired donor oxidoreductase DE36TMY E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE36TMY EC 1.14.14.29 DE36TMY RC Defective CYP7B1 causes Spastic paraplegia 5A, autosomal recessive (SPG5A) and Congenital bile acid synthesis defect 3 (CBAS3):R-HSA-5579013; Endogenous sterols:R-HSA-211976; Synthesis of bile acids and bile salts via 27-hydroxycholesterol:R-HSA-193807; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol:R-HSA-193368; Synthesis of bile acids and bile salts:R-HSA-192105 DE36TMY KG Primary bile acid biosynthesis:hsa00120; Steroid hormone biosynthesis:hsa00140 DE36TMY SQ MAGEVSAATGRFSLERLGLPGLALAAALLLLALCLLVRRTRRPGEPPLIKGWLPYLGVVLNLRKDPLRFMKTLQKQHGDTFTVLLGGKYITFILDPFQYQLVIKNHKQLSFRVFSNKLLEKAFSISQLQKNHDMNDELHLCYQFLQGKSLDILLESMMQNLKQVFEPQLLKTTSWDTAELYPFCSSIIFEITFTTIYGKVIVCDNNKFISELRDDFLKFDDKFAYLVSNIPIELLGNVKSIREKIIKCFSSEKLAKMQGWSEVFQSRQDVLEKYYVHEDLEIGAHHLGFLWASVANTIPTMFWAMYYLLRHPEAMAAVRDEIDRLLQSTGQKKGSGFPIHLTREQLDSLICLESSIFEALRLSSYSTTIRFVEEDLTLSSETGDYCVRKGDLVAIFPPVLHGDPEIFEAPEEFRYDRFIEDGKKKTTFFKRGKKLKCYLMPFGTGTSKCPGRFFALMEIKQLLVILLTYFDLEIIDDKPIGLNYSRLLFGIQYPDSDVLFRYKVKS DE36TMY TD Primarily distributed in brain, testis, ovary, prostate, liver, colon, kidney, small intestine, thymus and spleen. DE36TMY FC This enzyme involves in the metabolism of endogenous oxysterols and steroid hormones, including neurosteroids. DE36TMY KD 33208: Metazoa DE36TMY PL 7711: Chordata DE36TMY CL 40674: Mammalia DE36TMY OD 9443: Primates DE36TMY FM 9604: Hominidae DE36TMY GE 9605: Homo DE36TMY SP 9606: Homo sapiens DEMRAYN ID DEMRAYN DEMRAYN DN Choline kinase alpha (CHKA) DEMRAYN GN CHKA DEMRAYN SN Choline-kinase A; Choline phosphokinase; CHETK-alpha; CHK; CHKA; CK; CKI DEMRAYN UC CHKA_HUMAN DEMRAYN RD BRN-1736748 DEMRAYN GI 1119 DEMRAYN E1 2: Transferase DEMRAYN E2 2.7: Kinase DEMRAYN E3 2.7.1: Phosphotransferase DEMRAYN EC 2.7.1.32 DEMRAYN RC Synthesis of PC:R-HSA-1483191; Synthesis of PE:R-HSA-1483213 DEMRAYN KG Choline metabolism in cancer:hsa05231; Glycerophospholipid metabolism:hsa00564; Metabolic pathways:hsa01100 DEMRAYN PD 2CKQ; 2I7Q; 3F2R; 3G15; 3ZM9; 4BR3; 4CG8; 4CG9; 4CGA DEMRAYN SQ MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPPPPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV DEMRAYN TD Low tissue/organ specificity. DEMRAYN FC This enzyme has a key role in phospholipid biosynthesis. It catalyzes the first step in phosphatidylcholine biosynthesis and contributes to phosphatidylethanolamine biosynthesis. It also phosphorylates choline and ethanolamine. DEMRAYN KD 33208: Metazoa DEMRAYN PL 7711: Chordata DEMRAYN CL 40674: Mammalia DEMRAYN OD 9443: Primates DEMRAYN FM 9604: Hominidae DEMRAYN GE 9605: Homo DEMRAYN SP 9606: Homo sapiens DEAHED0 ID DEAHED0 DEAHED0 DN Choline dehydrogenase (CHDH) DEAHED0 GN CHDH DEAHED0 SN Mitochondrial choline dehydrogenase; CDH; CHD; CHDH DEAHED0 UC CHDH_HUMAN DEAHED0 RD Choline salicylate DEAHED0 GI 55349 DEAHED0 E1 1: Oxidoreductase DEAHED0 E2 1.1: CH-OH donor oxidoreductase DEAHED0 E3 1.1.99: CH-OH donor oxidoreductase DEAHED0 EC 1.1.99.1 DEAHED0 RC Choline catabolism:R-HSA-6798163 DEAHED0 KG Glycine, serine and threonine metabolism:hsa00260; Metabolic pathways:hsa01100 DEAHED0 SQ MWCLLRGLGRPGALARGALGQQQSLGARALASAGSESRDEYSYVVVGAGSAGCVLAGRLTEDPAERVLLLEAGPKDVLAGSKRLSWKIHMPAALVANLCDDRYNWCYHTEVQRGLDGRVLYWPRGRVWGGSSSLNAMVYVRGHAEDYERWQRQGARGWDYAHCLPYFRKAQGHELGASRYRGADGPLRVSRGKTNHPLHCAFLEATQQAGYPLTEDMNGFQQEGFGWMDMTIHEGKRWSAACAYLHPALSRTNLKAEAETLVSRVLFEGTRAVGVEYVKNGQSHRAYASKEVILSGGAINSPQLLMLSGIGNADDLKKLGIPVVCHLPGVGQNLQDHLEIYIQQACTRPITLHSAQKPLRKVCIGLEWLWKFTGEGATAHLETGGFIRSQPGVPHPDIQFHFLPSQVIDHGRVPTQQEAYQVHVGPMRGTSVGWLKLRSANPQDHPVIQPNYLSTETDIEDFRLCVKLTREIFAQEALAPFRGKELQPGSHIQSDKEIDAFVRAKADSAYHPSCTCKMGQPSDPTAVVDPQTRVLGVENLRVVDASIMPSMVSGNLNAPTIMIAEKAADIIKGQPALWDKDVPVYKPRTLATQR DEAHED0 TD Primarily distributed in kidney and liver. DEAHED0 FC This enzyme participates in glycine, serine and threonine metabolism. DEAHED0 KD 33208: Metazoa DEAHED0 PL 7711: Chordata DEAHED0 CL 40674: Mammalia DEAHED0 OD 9443: Primates DEAHED0 FM 9604: Hominidae DEAHED0 GE 9605: Homo DEAHED0 SP 9606: Homo sapiens DERPD8Z ID DERPD8Z DERPD8Z DN Carboxymethylenebutenolidase (CMBL) DERPD8Z GN CMBL DERPD8Z SN Maleylacetate enol-lactonase; Dienelactone hydrolase; Carboxymethylene butenolide hydrolase; Carboxymethylenebutenolidase homolog; CMBL DERPD8Z UC CMBL_HUMAN DERPD8Z RD Azilsartan medoxomil DERPD8Z GI 134147 DERPD8Z E1 3: Hydrolases DERPD8Z E2 3.1: Ester bond hydrolase DERPD8Z E3 3.1.1: Carboxylic ester hydrolase DERPD8Z EC 3.1.1.45 DERPD8Z RC Phase I - Functionalization of compounds:R-HSA-211945 DERPD8Z KG Metabolic pathways:hsa01100 DERPD8Z SQ MANEAYPCPCDIGHRLEYGGLGREVQVEHIKAYVTKSPVDAGKAVIVIQDIFGWQLPNTRYIADMISGNGYTTIVPDFFVGQEPWDPSGDWSIFPEWLKTRNAQKIDREISAILKYLKQQCHAQKIGIVGFCWGGTAVHHLMMKYSEFRAGVSVYGIVKDSEDIYNLKNPTLFIFAENDVVIPLKDVSLLTQKLKEHCKVEYQIKTFSGQTHGFVHRKREDCSPADKPYIDEARRNLIEWLNKYM DERPD8Z TD Primarily distributed in liver, kidney, small intestine and colon. DERPD8Z FC This enzyme can convert the prodrug olmesartan medoxomil into its pharmacologically active metabolite olmerstatan, an angiotensin receptor blocker, in liver and intestine. It may also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. DERPD8Z KD 33208: Metazoa DERPD8Z PL 7711: Chordata DERPD8Z CL 40674: Mammalia DERPD8Z OD 9443: Primates DERPD8Z FM 9604: Hominidae DERPD8Z GE 9605: Homo DERPD8Z SP 9606: Homo sapiens DE6BOK3 ID DE6BOK3 DE6BOK3 DN Beta,beta-carotene 15,15'-dioxygenase (BCO1) DE6BOK3 GN BCO1 DE6BOK3 SN Beta-carotene dioxygenase 1; Beta-carotene oxygenase 1; BCDO; BCDO1; BCMO1; BCO1 DE6BOK3 UC BCDO1_HUMAN DE6BOK3 RD Beta carotene DE6BOK3 GI 53630 DE6BOK3 E1 1: Oxidoreductase DE6BOK3 E2 1.13: Oxygen single donor oxidoreductase DE6BOK3 E3 1.13.11: Oxygen single donor oxidoreductase DE6BOK3 EC 1.13.11.63 DE6BOK3 RC Retinoid metabolism and transport:R-HSA-975634 DE6BOK3 KG Metabolic pathways:hsa01100; Retinol metabolism:hsa00830 DE6BOK3 SQ MDIIFGRNRKEQLEPVRAKVTGKIPAWLQGTLLRNGPGMHTVGESRYNHWFDGLALLHSFTIRDGEVYYRSKYLRSDTYNTNIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATSETNYIRKINPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSIVEKGKTKYVIFKIPATVPEGKKQGKSPWKHTEVFCSIPSRSLLSPSYYHSFGVTENYVIFLEQPFRLDILKMATAYIRRMSWASCLAFHREEKTYIHIIDQRTRQPVQTKFYTDAMVVFHHVNAYEEDGCIVFDVIAYEDNSLYQLFYLANLNQDFKENSRLTSVPTLRRFAVPLHVDKNAEVGTNLIKVASTTATALKEEDGQVYCQPEFLYEGLELPRVNYAHNGKQYRYVFATGVQWSPIPTKIIKYDILTKSSLKWREDDCWPAEPLFVPAPGAKDEDDGVILSAIVSTDPQKLPFLLILDAKSFTELARASVDVDMHMDLHGLFITDMDWDTKKQAASEEQRDRASDCHGAPLT DE6BOK3 TD Primarily distributed in intestine and retina. DE6BOK3 FC This enzyme symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism. DE6BOK3 KD 33208: Metazoa DE6BOK3 PL 7711: Chordata DE6BOK3 CL 40674: Mammalia DE6BOK3 OD 9443: Primates DE6BOK3 FM 9604: Hominidae DE6BOK3 GE 9605: Homo DE6BOK3 SP 9606: Homo sapiens DE2PJF5 ID DE2PJF5 DE2PJF5 DN Acid cholesteryl ester hydrolase (LIPA) DE2PJF5 GN LIPA DE2PJF5 SN Cholesteryl esterase; Lysosomal acid lipase/cholesteryl ester hydrolase; Sterol esterase; LAL; LIPA; Lipase A DE2PJF5 UC LICH_HUMAN DE2PJF5 RD BRN-0456976 DE2PJF5 GI 3988 DE2PJF5 E1 3: Hydrolases DE2PJF5 E2 3.1: Ester bond hydrolase DE2PJF5 E3 3.1.1: Carboxylic ester hydrolase DE2PJF5 EC 3.1.1.13 DE2PJF5 RC LDL clearance:R-HSA-8964038 DE2PJF5 KG Cholesterol metabolism:hsa04979; Lysosome:hsa04142; Steroid biosynthesis:hsa00100 DE2PJF5 SQ MKMRFLGLVVCLVLWTLHSEGSGGKLTAVDPETNMNVSEIISYWGFPSEEYLVETEDGYILCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNSRGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIGFIAFSQIPELAKRIKMFFALGPVASVAFCTSPMAKLGRLPDHLIKDLFGDKEFLPQSAFLKWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAVKFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDVNILLTQITNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMRKYQ DE2PJF5 TD Primarily distributed in adipose. DE2PJF5 FC This enzyme is crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides. It is important in activation of endogenous cellular cholesteryl ester formation. DE2PJF5 KD 33208: Metazoa DE2PJF5 PL 7711: Chordata DE2PJF5 CL 40674: Mammalia DE2PJF5 OD 9443: Primates DE2PJF5 FM 9604: Hominidae DE2PJF5 GE 9605: Homo DE2PJF5 SP 9606: Homo sapiens DEDG68B ID DEDG68B DEDG68B DN Sulfurylase kinase 1 (PAPSS1) DEDG68B GN PAPSS1 DEDG68B SN Sulfate adenylate transferase; Sulfate adenylyltransferase; PAPS synthase 1; 3'-phosphoadenosine-5'-phosphosulfate synthase; APS kinase; ATP-sulfurylase; ATPSK1; Adenosine-5'-phosphosulfate 3'-phosphotransferase; Adenylyl-sulfate kinase; Adenylylsulfate 3'-phosphotransferase; Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1; PAPSS; PAPSS 1; PAPSS1; SAT DEDG68B UC PAPS1_HUMAN DEDG68B RD Adenylylsulfate DEDG68B GI 9061 DEDG68B E1 2: Transferase DEDG68B E2 2.7: Kinase DEDG68B E3 2.7.7: Nucleotidyltransferase DEDG68B EC 2.7.7.4 DEDG68B RC Metabolism of ingested H2SeO4 and H2SeO3 into H2Se:R-HSA-2408550; Signaling by BRAF and RAF fusions:R-HSA-6802952; Transport and synthesis of PAPS:R-HSA-174362 DEDG68B KG Metabolic pathways:hsa01100; Purine metabolism:hsa00230; Selenocompound metabolism:hsa00450; Sulfur metabolism:hsa00920 DEDG68B PD 1X6V; 1XJQ; 1XNJ; 2OFW; 2OFX; 2PEY; 2PEZ; 2QJF DEDG68B SQ MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEKA DEDG68B TD Primarily distributed in testis, pancreas, kidney, thymus, prostate, ovary, small intestine, colon, leukocytes and liver. DEDG68B FC This enzyme is with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). DEDG68B KD 33208: Metazoa DEDG68B PL 7711: Chordata DEDG68B CL 40674: Mammalia DEDG68B OD 9443: Primates DEDG68B FM 9604: Hominidae DEDG68B GE 9605: Homo DEDG68B SP 9606: Homo sapiens DET64RG ID DET64RG DET64RG DN Pancreatic alpha-amylase (AMY2A) DET64RG GN AMY2A DET64RG SN Alpha-D-glucan glucanohydrolase; 1,4-alpha-D-glucan glucanohydrolase; AMY2A; PA DET64RG UC AMYP_HUMAN DET64RG RD Icodextrin DET64RG GI 279 DET64RG E1 3: Hydrolases DET64RG E2 3.2: Glycosylase DET64RG E3 3.2.1: O/S-glycosyl compound glycosidase DET64RG EC 3.2.1.1 DET64RG RC Digestion of dietary carbohydrate:R-HSA-189085 DET64RG KG Carbohydrate digestion and absorption:hsa04973; Metabolic pathways:hsa01100; Pancreatic secretion:hsa04972; Starch and sucrose metabolism:hsa00500 DET64RG PD 1CPU; 1HNY; 1KB3; 1KBB; 1KBK; 1KGU; 1KGW; 1KGX; 1U2Y DET64RG SQ MKFFLLLFTIGFCWAQYSPNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIYNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLTGLLDLALEKDYVRSKIAEYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNSNWFPAGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFVPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRQFQNGNDVNDWVGPPNNNGVIKEVTINPDTTCGNDWVCEHRWRQIRNMVIFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWSFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL DET64RG TD Primarily distributed in pancreas. DET64RG FC This enzyme hydrolyzes 1,4-alpha-glucoside bonds in oligosaccharides and polysaccharides, and thus catalyze the first step in digestion of dietary starch and glycogen. DET64RG KD 33208: Metazoa DET64RG PL 7711: Chordata DET64RG CL 40674: Mammalia DET64RG OD 9443: Primates DET64RG FM 9604: Hominidae DET64RG GE 9605: Homo DET64RG SP 9606: Homo sapiens DEHGR57 ID DEHGR57 DEHGR57 DN Hydroxyindole O-methyltransferase (ASMT) DEHGR57 GN ASMT DEHGR57 SN Acetylserotonin O-methyltransferase; Hydroxyindolemethyltransferase; Hydroxyindole-O-methyl transferase; Hydroxyindole-O-methyltransferase; HIOMT; ASMT DEHGR57 UC ASMT_HUMAN DEHGR57 RD Melatonin DEHGR57 GI 438 DEHGR57 E1 2: Transferase DEHGR57 E2 2.1: Methylase DEHGR57 E3 2.1.1: Methyltransferase DEHGR57 EC 2.1.1.4 DEHGR57 RC Serotonin and melatonin biosynthesis:R-HSA-209931 DEHGR57 KG Metabolic pathways:hsa01100; Tryptophan metabolism:hsa00380 DEHGR57 PD 4A6D; 4A6E DEHGR57 SQ MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVAAGVRASAHGTELLLDICVSLKLLKVETRGGKAFYRNTELSSDYLTTVSPTSQCSMLKYMGRTSYRCWGHLADAVREGRNQYLETFGVPAEELFTAIYRSEGERLQFMQALQEVWSVNGRSVLTAFDLSVFPLMCDLGGGAGALAKECMSLYPGCKITVFDIPEVVWTAKQHFSFQEEEQIDFQEGDFFKDPLPEADLYILARVLHDWADGKCSHLLERIYHTCKPGGGILVIESLLDEDRRGPLLTQLYSLNMLVQTEGQERTPTHYHMLLSSAGFRDFQFKKTGAIYDAILARK DEHGR57 TD Primarily distributed in brain and epididymis. DEHGR57 FC This enzyme catalyzes the transfer of a methyl group onto N- acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). DEHGR57 KD 33208: Metazoa DEHGR57 PL 7711: Chordata DEHGR57 CL 40674: Mammalia DEHGR57 OD 9443: Primates DEHGR57 FM 9604: Hominidae DEHGR57 GE 9605: Homo DEHGR57 SP 9606: Homo sapiens DEHDW40 ID DEHDW40 DEHDW40 DN Cytochrome P450 154C2 (cyp154) DEHDW40 GN cyp154C4-2 DEHDW40 SN Cytochrome P450 family 154 subfamily C member 2; Cytochrome cyp154C2; P450 154C2; cyp154C2 DEHDW40 UC A0A345AH95_STRSQ DEHDW40 RD Testosterone cypionate DEHDW40 E1 1: Oxidoreductase DEHDW40 E2 1.14: Oxygen paired donor oxidoreductase DEHDW40 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEHDW40 EC 1.14.14.1 DEHDW40 SQ MTRIALDPFVRDLDGESAALRAAGPLAEVELPGGVHVYAVTHHKEARALLTDSRVVKDINVWNAWQRGEIPADWPLIGLVNPGRSMLTVDGPDHRRLRTLVAQALTVKRVEKLRAGIEALTNASLERLAALPAGEPVDLKAEFAYPLPMNVISELMGVDAADHPRLKELFEKFFSTQTPPEEVPQMMADLGTLFTKIVEEKKANPGDDLTSALIAASEDGDHLTDEEILNTLQLIIAAGHETTISLIVNVVEALAIHPEQRKKVLSGEIPWEGVIEETLRWNTPTSHVLIRFATEDIEVGDKVLPKGEGLVVSFGALGRDEEQYGPTAGDFDATRTPNRHIAFGHGPHVCPGAALSRLEAGIALPALYERFPELDLAVPAAELRNKPIVTQNDLHDLPVKLGCPFGHDA DEHDW40 TD Primarily distributed in human gut. DEHDW40 FC This enzyme is P-450 heme-thiolate protein, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. DEHDW40 KD 2: Bacteria DEHDW40 PL 201174: Actinobacteria DEHDW40 CL 1760: Actinobacteria DEHDW40 OD 85011: Streptomycetales DEHDW40 FM 2062: Streptomycetaceae DEHDW40 GE 1883: Streptomyces DEHDW40 SP 33903: Streptomyces avermitilis DE10BJ5 ID DE10BJ5 DE10BJ5 DN Tyrosine-protein phosphatase STS1/TULA2 (UBASH3B) DE10BJ5 GN UBASH3B DE10BJ5 SN T-cell ubiquitin ligand 2; Cbl-interacting protein p70; Suppressor of T-cell receptor signaling 1; Ubiquitin-associated and SH3 domain-containing protein B; TULA-2; STS-1; STS1; KIAA1959; UBASH3B DE10BJ5 UC UBS3B_HUMAN DE10BJ5 RD Estrone sulfate DE10BJ5 GI 84959 DE10BJ5 E1 3: Hydrolases DE10BJ5 E2 3.1: Ester bond hydrolase DE10BJ5 E3 3.1.3: Phosphoric monoester hydrolase DE10BJ5 EC 3.1.3.48 DE10BJ5 PD 2CPW; 2E5K; 5VR6; 5W5G DE10BJ5 SQ MAQYGHPSPLGMAAREELYSKVTPRRNRQQRPGTIKHGSALDVLLSMGFPRARAQKALASTGGRSVQAACDWLFSHVGDPFLDDPLPREYVLYLRPTGPLAQKLSDFWQQSKQICGKNKAHNIFPHITLCQFFMCEDSKVDALGEALQTTVSRWKCKFSAPLPLELYTSSNFIGLFVKEDSAEVLKKFAADFAAEAASKTEVHVEPHKKQLHVTLAYHFQASHLPTLEKLAQNIDVKLGCDWVATIFSRDIRFANHETLQVIYPYTPQNDDELELVPGDFIFMSPMEQTSTSEGWIYGTSLTTGCSGLLPENYITKADECSTWIFHGSYSILNTSSSNSLTFGDGVLERRPYEDQGLGETTPLTIICQPMQPLRVNSQPGPQKRCLFVCRHGERMDVVFGKYWLSQCFDAKGRYIRTNLNMPHSLPQRSGGFRDYEKDAPITVFGCMQARLVGEALLESNTIIDHVYCSPSLRCVQTAHNILKGLQQENHLKIRVEPGLFEWTKWVAGSTLPAWIPPSELAAANLSVDTTYRPHIPISKLVVSESYDTYISRSFQVTKEIISECKSKGNNILIVAHASSLEACTCQLQGLSPQNSKDFVQMVRKIPYLGFCSCEELGETGIWQLTDPPILPLTHGPTGGFNWRETLLQE DE10BJ5 TD Primarily distributed in brain and lymphoid tissue. DE10BJ5 FC This enzyme interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. It exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. DE10BJ5 KD 33208: Metazoa DE10BJ5 PL 7711: Chordata DE10BJ5 CL 40674: Mammalia DE10BJ5 OD 9443: Primates DE10BJ5 FM 9604: Hominidae DE10BJ5 GE 9605: Homo DE10BJ5 SP 9606: Homo sapiens DEXSRCY ID DEXSRCY DEXSRCY DN Glutamate racemase (MurI) DEXSRCY GN murI DEXSRCY SN D-glutamate racemase; MurI; murI; BAS0806; BAS4379; BcGR; BsGR; BsRacE; DapF; FnGR; GBAA_0847; GBAA_4717 DEXSRCY UC MURI_AQUPY DEXSRCY RD L-glutamine DEXSRCY E1 5: Isomerase DEXSRCY E2 5.1: Racemase/epimerase DEXSRCY E3 5.1.1: Amino acid racemase/epimerase DEXSRCY EC 5.1.1.3 DEXSRCY PD 1B73; 1B74 DEXSRCY SQ MKIGIFDSGVGGLTVLKAIRNRYRKVDIVYLGDTARVPYGIRSKDTIIRYSLECAGFLKDKGVDIIVVACNTASAYALERLKKEINVPVFGVIEPGVKEALKKSRNKKIGVIGTPATVKSGAYQRKLEEGGADVFAKACPLFVPLAEEGLLEGEITRKVVEHYLKEFKGKIDTLILGCTHYPLLKKEIKKFLGDVEVVDSSEALSLSLHNFIKDDGSSSLELFFTDLSPNLQFLIKLILGRDYPVKLAEGVFTH DEXSRCY TD Primarily distributed in human gut. DEXSRCY FC This enzyme is a pyridoxal-phosphate protein providing the (R)-glutamate required for cell wall biosynthesis and converting L- or D-glutamate to D- or L-glutamate, respectively, but not other amino acids such as alanine, aspartate, and glutamine. DEXSRCY KD 2: Bacteria DEXSRCY PL 200783: Aquificae DEXSRCY CL 187857: Aquificae DEXSRCY OD 32069: Aquificales DEXSRCY FM 64898: Aquificaceae DEXSRCY GE 2713: Aquifex DEXSRCY SP 2714: Aquifex pyrophilus DE793VL ID DE793VL DE793VL DN Glutamate decarboxylase (gadB) DE793VL GN gadB DE793VL SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; BDP_1749; GAD-beta DE793VL UC D2Q5X3_BIFDB DE793VL RD L-glutamine DE793VL GI 31606910 DE793VL E1 4: Lyases DE793VL E2 4.1: Carbon-carbon lyase DE793VL E3 4.1.1: Carboxy-lyase DE793VL EC 4.1.1.15 DE793VL KG Alanine, aspartate and glutamate metabolism:bde00250; Biosynthesis of secondary metabolites:bde01110; Butanoate metabolism:bde00650; Metabolic pathways:bde01100; Microbial metabolism in diverse environments:bde01120; Quorum sensing:bde02024; Taurine and hypotaurine metabolism:bde00430; beta-Alanine metabolism:bde00410 DE793VL SQ MSIMHSNINTIAAGYGYSGGADSDSVEVNPLFARPKEAKAFSKFKIPQEGSLPETAYQVVHDDAMLDGNARLNLATFVSTWMDDYANRLYMEAADKNMIDKDEYPKTAEVESRCWHMLADLWHAPDPMNTIGTSTIGSSEACMLGGLALKRRWKEAREKAGLPADRPNLVMSSAVQVCWEKFCNYFDVEPRYVPISEEHKVLDGYDLDKYVDENTIGVVAIMGVTYTGMYEPVKKISDALDRIEERTGLDVRIHVDAASGGMIAPFIQPDLQWDFRVKRVYSISTSGHKYGLVYPGLGWVVWRETADLPESLIFKVSYLGGEMPTFALNFSRPGAQVLLQYYMFLRLGFEGYRRVQQAAHDVAKYLSGEIAKMDDFTLWNDGSDIPVFAWMLKDKPDRKWNLYDLQDRLRMKGWLVPAYPMPVDLTQVTVQRIVVRNGFSHDMAESFLKDLKACVKYLDGLKAPMPSEARVSGFHH DE793VL TD Primarily distributed in human gut. DE793VL FC This enzyme acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DE793VL KD 2: Bacteria DE793VL PL 201174: Actinobacteria DE793VL CL 1760: Actinobacteria DE793VL OD 85004: Bifidobacteriales DE793VL FM 31953: Bifidobacteriaceae DE793VL GE 1678: Bifidobacterium DE793VL SP 1689: Bifidobacterium dentium DEBDLXO ID DEBDLXO DEBDLXO DN Glutamate decarboxylase (gadB) DEBDLXO GN gadB DEBDLXO SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB; Bang102_004600; GAD-beta DEBDLXO UC A0A126SV18_9BIFI DEBDLXO RD L-glutamine DEBDLXO E1 4: Lyases DEBDLXO E2 4.1: Carbon-carbon lyase DEBDLXO E3 4.1.1: Carboxy-lyase DEBDLXO EC 4.1.1.15 DEBDLXO SQ MSDMHFSTTASSTCCGNDTRDADRLGSVEINPLFARPKEARSFPKNRIPDTGSLPETAYQVVHDDAMLDGNARLNLATFVGTWMDDYANRIYMEAADKNMIDKDEYPKTAEIEDRCWRMLADLWNNLDIDHAIGTSTIGSSEACMLGGLALKRRWVKARKAAGLPTDKPNLVMSSAVQVCWEKFCNYFDVEPRFVPISEEHKVLDGYDLDKYVDENTIGVVAIMGVTYTGMYEPVQHISDALDRIQEKTGLNIHIHVDAASGGMIAPFIQPDLAWDFRVKRVVSISTSGHKYGLVYPGLGWVVWRSTADLPESLVFKVSYLGGEMPTFALNFSRPGAQVLLQYYMFLRLGVEGYRRVQQASHDVAKYLSSEIAAMDDFTLWNDGSDIPVFAWMLKDKPGRKWNLYDLQDRLRMKGWLVPAYPMPVDLTDVTVQRIVVRNGFSHDLAESFLKDLKACVAYLDNLQAPMPSEAHVSGFHH DEBDLXO TD Primarily distributed in human gut. DEBDLXO FC This enzyme acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DEBDLXO KD 2: Bacteria DEBDLXO PL 201174: Actinobacteria DEBDLXO CL 1760: Actinobacteria DEBDLXO OD 85004: Bifidobacteriales DEBDLXO FM 31953: Bifidobacteriaceae DEBDLXO GE 1678: Bifidobacterium DEBDLXO SP 1683: Bifidobacterium angulatum DEXF6AQ ID DEXF6AQ DEXF6AQ DN Glutamate decarboxylase (gadB) DEXF6AQ GN gadA DEXF6AQ SN Glutamic acid decarboxylase; Bacterial glutamate--ammonia ligase; gad; gadB DEXF6AQ UC A0A0B5GI57_LACBR DEXF6AQ RD L-glutamine DEXF6AQ E1 4: Lyases DEXF6AQ E2 4.1: Carbon-carbon lyase DEXF6AQ E3 4.1.1: Carboxy-lyase DEXF6AQ EC 4.1.1.15 DEXF6AQ SQ AMENYCVSMIAHLWGIPDNEKIYDDFIGTSTVGSSEGCMLGGLALLHSWKHRAKAAGFDIEDLHSHKPNLVIMSGYQVVWEKFCTYWNVEMRQVPINGDQVSLDMDHVMDYVDENTIGIIGIEGITYTGSVDDIQTLDNLVSEYNKTATMPVRIHVDAAFGGLFAPFVDGFNPWDFRLKNVVSINVSGHKYGMVYPGLGWIVWRHNTADILPAEMRFQVPYLGKTVDSIAINFSHSGAHISAQYYNFIRFGLSGYKTIMQNVRKVSLKLTAALKTYGIFDILVDGSQLPINCWKLADDAPVGWTLYDLESELAKYG DEXF6AQ TD Primarily distributed in human gut. DEXF6AQ FC This enzyme acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate. DEXF6AQ KD 2: Bacteria DEXF6AQ PL 1239: Firmicutes DEXF6AQ CL 91061: Bacilli DEXF6AQ OD 186826: Lactobacillales DEXF6AQ FM 33958: Lactobacillaceae DEXF6AQ GE 1578: Lactobacillus DEXF6AQ SP 1580: Lactobacillus brevis DE1QMDG ID DE1QMDG DE1QMDG DN Molybdopterin-dependent enzyme (molD) DE1QMDG GN molD DE1QMDG SN Molybdopterin-dependent oxidoreductase; Oxidoreductase molD; molD DE1QMDG UC A0A327U7N1_9ACTN DE1QMDG RD Doxorubicin DE1QMDG E1 1: Oxidoreductase DE1QMDG E2 1.1: CH-OH donor oxidoreductase DE1QMDG E3 1.1.1: NAD/NADP oxidoreductase DE1QMDG EC 1.1.1.40 DE1QMDG SQ MTLARLALSGDLVRPSRLTVPDLLRWPQHRVAVSFECATSGTQHHRFTGPRLYDVLADAGPGFDPVRRKDRLRFLIAVTGTDGHHALLSWAEIDPDFADAPVLLGVSIDDTPLDAAGPQLVLPQDRCGARHISQITAIRVDGSYRCAPVEVAAVP DE1QMDG TD Primarily distributed in human gut. DE1QMDG FC This enzyme catalyzes the conversion of doxorubicin to 7-deoxydoxorubicinol and 7-deoxydoxorubicinolone via a reductive deglycosylation mechanism. DE1QMDG KD 2: Bacteria DE1QMDG PL 1224: Proteobacteria DE1QMDG CL 1236: Gammaproteobacteria DE1QMDG OD 91347: Enterobacterales DE1QMDG FM 543: Enterobacteriaceae DE1QMDG GE 160674: Raoultella DE1QMDG SP 575: Raoultella planticola DECV2ME ID DECV2ME DECV2ME DN Cytochrome P450 105D7 (cyp105) DECV2ME GN cyp28 DECV2ME SN Cytochrome P450 family 105 subfamily D member 7; Pentalenic acid synthase; SAV_7469; cyp105d7; cyp28 DECV2ME UC CYP28_STRAW DECV2ME RD Diclofenac sodium DECV2ME E1 1: Oxidoreductase DECV2ME E2 1.14: Oxygen paired donor oxidoreductase DECV2ME E3 1.14.15: Iron-sulfur protein donor oxidoreductase DECV2ME EC 1.14.15.11 DECV2ME KG Biosynthesis of secondary metabolites:sma01110; Biosynthesis of various secondary metabolites:sma00999 DECV2ME PD 4UBS DECV2ME SQ MTEPGTSVSAPVAFPQDRTCPYDPPTAYDPLREGRPLSRVSLYDGRSVWVVTGHAAARALLSDQRLSSDRTLPRFPATTERFEAVRTRRVALLGVDDPEHRTQRRMLVPSFTLKRAAALRPRIQETVDGLLDAMEAQGPPAELVSAFALPLPSMVICALLGVPYADHDFFESQSRRLLRGPGIAEVQDARAQLDDYLYALIDRKRKEPGDGLLDDLIQEQLNRGTVDRAELVSLATLLLIAGHETTANMISLGTFTLLRHPEQLAELRAEPGLMPAAVEELLRFLSIADGLLRVATEDIEVAGTTIRADEGVVFATSVINRDAAGFAEPDALDWHRSARHHVAFGFGIHQCLGQNLARAEMEIALGTLFERLPGLRLAAPADEIPFKPGDTIQGMLELPVTW DECV2ME TD Primarily distributed in human gut. DECV2ME FC This enzyme is a P-450 heme-thiolate protein, and it catalyzes the conversion of 1-deoxypentalenic acid to pentalenic acid in the biosynthesis of neopentalenolactone antibiotic. DECV2ME KD 2: Bacteria DECV2ME PL 201174: Actinobacteria DECV2ME CL 1760: Actinobacteria DECV2ME OD 85011: Streptomycetales DECV2ME FM 2062: Streptomycetaceae DECV2ME GE 1883: Streptomyces DECV2ME SP 33903: Streptomyces avermitilis DEG8NJD ID DEG8NJD DEG8NJD DN Alcohol dehydrogenase (ADH) DEG8NJD GN ADH DEG8NJD SN Alcohol dehydrogenase AdhP; Zinc-dependent alcohol dehydrogenase; Zn-dependent alcohol dehydrogenase; CYK00_08895 DEG8NJD UC A0A2I1XAT4_NEISI DEG8NJD RD Ethanol DEG8NJD E1 1: Oxidoreductase DEG8NJD E2 1.1: CH-OH donor oxidoreductase DEG8NJD E3 1.1.1: NAD/NADP oxidoreductase DEG8NJD EC 1.1.1.1 DEG8NJD SQ MKAMVYHGANDIRFEEKPRPQIIDPTDAVVKIVKTTICGTDLGIWKGKNPEVADGRILGHEGIGIVEEVGEAVKNIKVGDKVIISCVSKCCTCDNCKIQLYSHCRNGGWILGYIIDGTQAEYVRTPYADNSLVPLPDNVNEEVALLLSDALPTAHEIGVQYGDVKPGDTVFIAGAGPVGMSALLTAQLYSPAAIIVCDMDENRLKLAKELGATHTISPASGDVSKQVFAIVGEDGVDCAIEAVGIPATWNMCQDIVKPGGHIAVVGVHGQSVDFKLEKLWIKNLAITTGLVNANTTEMLMKAISSSSVDYTKMLTHHFKFSELEKAYDVFKHAAENQAMKVVLEAD DEG8NJD TD Primarily distributed in human oral cavity. DEG8NJD FC This enzyme acts on primary or secondary alcohols or hemi-acetals with very broad specificity and the enzyme oxidizes methanol much more poorly than ethanol. DEG8NJD KD 2: Bacteria DEG8NJD PL 1224: Proteobacteria DEG8NJD CL 28216: Betaproteobacteria DEG8NJD OD 206351: Neisseriales DEG8NJD FM 481: Neisseriaceae DEG8NJD GE 482: Neisseria DEG8NJD SP 490: Neisseria sicca DE3U2Y6 ID DE3U2Y6 DE3U2Y6 DN Nitroreductase (NTR) DE3U2Y6 GN nfrA2 DE3U2Y6 SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; NCTC12362_00253 DE3U2Y6 UC A0A377KR04_ENTCA DE3U2Y6 RD Metronidazole DE3U2Y6 E1 1: Oxidoreductase DE3U2Y6 E2 1.5: CH-NH donor oxidoreductase DE3U2Y6 E3 1.5.1: NAD/NADP acceptor oxidoreductase DE3U2Y6 EC 1.5.1.39 DE3U2Y6 SQ MNETIELLHNHRTYRQFDPDYRLSQEQVTAILTAARQAPSWMNGQAYSILVIDDPQIRQQMVEWNPGNPHIAACSLFLLFLADLNRTKKVADEKQTPYPIDEGYQPLLIATTDASIALQSGAIAAESLGLGTVISGSVRKDSAKIAELLHLPEYVYPVAGLSIGKPIVEMKVKPRLPEEAVIHYNHYQDYSYEAIEAYDQTMTAFGEARETKPWSEKFAGFYSNRPDQGFDAFLKKQNLIK DE3U2Y6 TD Primarily distributed in human gut. DE3U2Y6 FC This enzyme contains FMN and can utilize NADH and NADPH with similar reaction rates. It also reduces riboflavin and FAD, but more slowly. DE3U2Y6 KD 2: Bacteria DE3U2Y6 PL 1239: Firmicutes DE3U2Y6 CL 91061: Bacilli DE3U2Y6 OD 186826: Lactobacillales DE3U2Y6 FM 81852: Enterococcaceae DE3U2Y6 GE 1350: Enterococcus DE3U2Y6 SP 37734: Enterococcus casseliflavus DE6PKFB ID DE6PKFB DE6PKFB DN Rifampicin monooxygenase (rox) DE6PKFB GN rox DE6PKFB SN Monooxygenase rifampicin; RIF-O; RIFMO; RifMO; rox; roxNFA_35380 DE6PKFB UC ROX_NOCFA DE6PKFB RD Rifampicin DE6PKFB E1 1: Oxidoreductase DE6PKFB E2 1.14: Oxygen paired donor oxidoreductase DE6PKFB E3 1.14.13: NADH/NADPH donor oxidoreductase DE6PKFB EC 1.14.13.- DE6PKFB PD 5KOW; 5KOX; 6C7S DE6PKFB SQ MIDVIIAGGGPTGLMLAGELRLHGVRTVVLEKEPTPNQHSRSRGLHARSIEVMDQRGLLERFLAHGEQFRVGGFFAGLAAEWPADLDTAHSYVLAIPQVVTERLLTEHATELGAEIRRGCEVAGLDQDADGVTAELADGTRLRARYLVGCDGGRSTVRRLLGVDFPGEPTRVETLLADVRIDVPVETLTAVVAEVRKTQLRFGAVPAGDGFFRLIVPAQGLSADRAAPTLDELKRCLHATAGTDFGVHSPRWLSRFGDATRLAERYRTGRVLLAGDAAHIHPPTGGQGLNLGIQDAFNLGWKLAAAIGGWAPPDLLDSYHDERHPVAAEVLDNTRAQMTLLSLDPGPRAVRRLMAELVEFPDVNRHLIEKITAIAVRYDLGDGHDLVGRRLRDIPLTEGRLYERMRGGRGLLLDRTGRLSVSGWSDRVDHLADPGAALDVPAALLRPDGHVAWVGEDQDDLLAHLPRWFGAAT DE6PKFB TD Primarily distributed in human lung. DE6PKFB FC This enzyme can modify rifampicin, thereby inactivating its antibiotic activity. And it constitutes a secondary rifampicin resistance factor. DE6PKFB KD 2: Bacteria DE6PKFB PL 201174: Actinobacteria DE6PKFB CL 1760: Actinobacteria DE6PKFB OD 85007: Corynebacteriales DE6PKFB FM 85025: Nocardiaceae DE6PKFB GE 1817: Nocardia DE6PKFB SP 37329: Nocardia farcinica DEL0D64 ID DEL0D64 DEL0D64 DN Dopamine dehydroxylase (dadH) DEL0D64 GN dadH DEL0D64 SN Inactive dopamine dehydroxylase; Dopamine de-monooxygenase; dadH; DADH; C1859_04790 DEL0D64 UC DADH_EGGLN DEL0D64 RD Dopamine hydrochloride DEL0D64 E1 1: Oxidoreductase DEL0D64 E2 1.1: CH-OH donor oxidoreductase DEL0D64 E3 1.1.1: NAD/NADP oxidoreductase DEL0D64 EC 1.1.1.- DEL0D64 SQ MGNLTMSRRTFVKTAAITGAAAAAFGASTHTALAEETYSSVSGNDTVAVKTCCRGCGKMECGVKVIVQNGRAIRVEGDEGAFQSMGNCCTKSQSSIQAAYHPDRLHYPMKRTNPKGEEPGWQRISWDEAMQSIVDNFMDIKAKHGGEAIACQVGTSRIWCMHSESILKNMLETPNNVEAWQICKGPRHFATTMVSQFAMSWMETITRPKVYVQWGGASELSNYDDSCRTTVDVASRADVHISVDPRMANMGKEADYWQHLRPGTDGALALAWTNVIIEKKLYDELYVKKWTNAPFLVCEDMEPSGFPTVRTDGSYWDVKTALLKESDIKEGGSPYKFLVYDNNWEKLKAEGVEHEYGAFTWFNADQEGVIDETGGFWEGENYDSEKARQGREAAQDNLLPGQTQGWLPDPMPFDPAIDPALEGEFEITLKDGKTVKVKPVWEHYKARAAEYKPEVAAEITGIPASEIEAAATAYGTRIDPSTGYGNGGIQYMLAVEHFCSAIQNCRAFDNLVGITGNMDTPGGNRGPTIVPIDGDLQGFSAWAPGATTPPEEVNRKQIGIDKFPLLGWWQYWCDSHSLWDAVITGDPYPVRALWNESGNFMSQTNTTRAWEALCSLDFYVDLNLWHTPQNDTADIILPVAHWIELNSPRASQGSAGAMGATVKCVQPPAEAKYDPEIVMDLARRMNWKWTDEPGNEWPDINWQLDDSIKLLTDDELTYTTWHVENGKPTFERHGVPMAEVTPKYKTWDEYVKAFQEHGWWQAKDIEPRNWGTYRRYQTGAMRARDRVWGRLDYTAGKGIGDWKPGWFTPTMKQEIWSTVMESHHPDHPEWRLPTYTEPPHGPKDGDRIKEYPLTATTGRRIPVYFHSEHRQLPWCRELWPVPRVEINPKTAAEYGIEQGDWVWIETEWGKIREVADLYYGVKEDVINLEHTWWYPEVKDAGHGWQFSQVNQLIDHYAQDPHSGTSNLRAYQVKIYKATPENSPFNNPVPCDSTGTPIIHTSDDPRLKEWLPTYEGRE DEL0D64 TD Primarily distributed in human gut. DEL0D64 FC This enzyme involves in drug metabolism, as part of an interspecies gut bacterial pathway for Levodopa (L-dopa) metabolism, acting on dopamine produced by Enterecoccus L-dopa decarboxylase. Removes the para hydroxyl group of dopamine to produce m-tyramine (3-tyramine). DEL0D64 KD 2: Bacteria DEL0D64 PL 201174: Actinobacteria DEL0D64 CL 84998: Coriobacteriia DEL0D64 OD 1643822: Eggerthellales DEL0D64 FM 1643826: Eggerthellaceae DEL0D64 GE 84111: Eggerthella DEL0D64 SP 84112: Eggerthella lenta DE1GYMX ID DE1GYMX DE1GYMX DN Dihydrofolate reductase (folA) DE1GYMX GN folA DE1GYMX SN DHF reductase; 5,6,7,8-tetrahydrofolate: NADP+ oxidoreductase; Bifunctional TS-DHFR; BmDHFR; Bacterial DFR-TS; Bacterial DHFR; TC_0902; folA DE1GYMX UC Q9PJC7_CHLMU DE1GYMX RD Folic acid DE1GYMX GI 1246271 DE1GYMX E1 1: Oxidoreductase DE1GYMX E2 1.5: CH-NH donor oxidoreductase DE1GYMX E3 1.5.1: NAD/NADP acceptor oxidoreductase DE1GYMX EC 1.5.1.3 DE1GYMX KG Folate biosynthesis:cmu00790; Metabolic pathways:cmu01100; One carbon pool by folate:cmu00670 DE1GYMX SQ MIQATGIVAIDPRGVMGGAGKLPWNYPEDLRFFSETIQDHPIIMGRKTWESLPDRYKCGRTVIVFSRQHSCAQGIWISSLVEYEKLSLNSPFLIGGAELFDWFFQYNLLKSCFVTHIKREYQGDTFFPVERLSGWKRESVLKTEDFNIYHYENYANQNP DE1GYMX TD Primarily distributed in human gut and vagina. DE1GYMX FC This enzyme can slowly reduces folate to 5,6,7,8-tetrahydrofolate in animals and some micro-organisms. DE1GYMX KD 2: Bacteria DE1GYMX PL 204428: Chlamydiae DE1GYMX CL 204429: Chlamydiia DE1GYMX OD 51291: Chlamydiales DE1GYMX FM 809: Chlamydiaceae DE1GYMX GE 810: Chlamydia DE1GYMX SP 83560: Chlamydia muridarum DEQGIMN ID DEQGIMN DEQGIMN DN Nitroreductase (NTR) DEQGIMN GN ntr1 DEQGIMN SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; ntr1 DEQGIMN UC A4K8Z3_ENTHI DEQGIMN RD Metronidazole DEQGIMN E1 1: Oxidoreductase DEQGIMN E2 1.5: CH-NH donor oxidoreductase DEQGIMN E3 1.5.1: NAD/NADP acceptor oxidoreductase DEQGIMN EC 1.5.1.39 DEQGIMN SQ MNMDLFYDRRSVRSYTGEKISEEDIDKIVRAGFYAPTAVNKQETEFIIIREKSLLENITKIHPYSSMLKSSSHAIVVCANLKKAYTPEYWVCDASAATENILLAAHMLGYGAVWLGVYPEKDRMESIKKLLQLPEQVEILSIVSIGVSKVQPVNRPERFDATRLHNDKW DEQGIMN TD Primarily distributed in human vagina. DEQGIMN FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DEQGIMN KD 554915: Amoebozoa DEQGIMN PL 2605435: Evosea DEQGIMN CL 2682482: Mastigamoebida DEQGIMN OD 2682482: Mastigamoebida DEQGIMN FM 33084: Entamoebidae DEQGIMN GE 5758: Entamoeba DEQGIMN SP 5759: Entamoeba histolytica DE8R7QY ID DE8R7QY DE8R7QY DN Nitroreductase (NTR) DE8R7QY GN NTR DE8R7QY SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; DHA2_15307 DE8R7QY UC A0A482G3K9_GIAIN DE8R7QY RD Metronidazole DE8R7QY E1 1: Oxidoreductase DE8R7QY E2 1.5: CH-NH donor oxidoreductase DE8R7QY E3 1.5.1: NAD/NADP acceptor oxidoreductase DE8R7QY EC 1.5.1.39 DE8R7QY SQ MPPICDAILRRRAIKQYTKESVSIEAIEYLRKVAVAIPTGHNTRHTEFAFVTNPRIIKTISQAKGEKAEYMQHAKLLIVVMGIQNDGVTSIATDMSIAAAMIQLACSDFGLACSWEQFYGRKNVYGEDSERIVLDVLRLLNSPNRRVLCALAIGYPAVQMPPADMHENGRIYMIE DE8R7QY TD Primarily distributed in human vagina. DE8R7QY FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DE8R7QY KD 2611341: Metamonada DE8R7QY PL 207245: Fornicata DE8R7QY CL 5738: Diplomonadida DE8R7QY OD 5738: Diplomonadida DE8R7QY FM 5739: Hexamitidae DE8R7QY GE 5740: Giardia DE8R7QY SP 5741: Giardia intestinalis DE2VSMT ID DE2VSMT DE2VSMT DN Nitroreductase (NTR) DE2VSMT GN NTR DE2VSMT SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; TVAG_026310 DE2VSMT UC A2DZ34_TRIVA DE2VSMT RD Metronidazole DE2VSMT GI 4772298 DE2VSMT E1 1: Oxidoreductase DE2VSMT E2 1.5: CH-NH donor oxidoreductase DE2VSMT E3 1.5.1: NAD/NADP acceptor oxidoreductase DE2VSMT EC 1.5.1.39 DE2VSMT SQ MTSVFECIERRRTIRHYDQNWVCPKEHLEAIVNAALKSPTACNRQSIDLLVITNKEVLDKIGEVGLNTLKKGTKEHMEERKHEGYKNVFTCDAPVLFLLVKNDRVNPLYTDVDAGIMCESIMLTAASYGYGTMCIGVLRATDLYEAVGIHKEDLAMAVCMGKIEDGYVPPEKPIKCKATYIE DE2VSMT TD Primarily distributed in human vagina. DE2VSMT FC This enzyme can reduce other azo dyes, such as Methyl Red, Rocceline, Solar Orange and Sumifix Black B. DE2VSMT KD 2611341: Metamonada DE2VSMT PL 5719: Parabasalia DE2VSMT CL 37104: Trichomonadida DE2VSMT OD 37104: Trichomonadida DE2VSMT FM 181550: Trichomonadidae DE2VSMT GE 5721: Trichomonas DE2VSMT SP 5722: Trichomonas vaginalis DELAPDY ID DELAPDY DELAPDY DN Nitroreductase (NTR) DELAPDY GN nfrA2 DELAPDY SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; CQW34_03043; HMPREF1018_03053 DELAPDY UC A0A1C0X0J8_BACFG DELAPDY RD Metronidazole DELAPDY E1 1: Oxidoreductase DELAPDY E2 1.5: CH-NH donor oxidoreductase DELAPDY E3 1.5.1: NAD/NADP acceptor oxidoreductase DELAPDY EC 1.5.1.39 DELAPDY SQ MIILFISLQKKDMMDTVKNRRTIRKYQQKDITPDLLNDLLETSFRASTMGGMQLYSVVVTRDAEKKEILSPAHFNQPMVKEAPVVLTFCADFRRFCKYCQERNAVPGYGNLMSFLNAAMDTLLVAQTFCTLAEEAGLGICYLGTTTYNPQMIIDALHLPELVFPITTVTVGYPAESPKQVDRLPIEGIIHEESYHDYTAEDINRLYAYKESLPENKLFIEENQKETLAQVFTDVRYTKKDNEFMSENLLKVLRRQGFMD DELAPDY TD Primarily distributed in human gut. DELAPDY FC This enzyme contains FMN and can utilize NADH and NADPH with similar reaction rates. It also reduces riboflavin and FAD, but more slowly. DELAPDY KD 2: Bacteria DELAPDY PL 976: Bacteroidetes DELAPDY CL 200643: Bacteroidia DELAPDY OD 171549: Bacteroidales DELAPDY FM 815: Bacteroidaceae DELAPDY GE 816: Bacteroides DELAPDY SP 817: Bacteroides fragilis DEV7UZD ID DEV7UZD DEV7UZD DN Hyaluronoglucosaminidase (nagH) DEV7UZD GN nagH DEV7UZD SN Hyaluronidase; Lung carcinoma protein; Mu toxin; LuCa; Hyal DEV7UZD UC NAGH_CLOPE DEV7UZD RD Hyaluronic acid DEV7UZD E1 3: Hydrolases DEV7UZD E2 3.2: Glycosylase DEV7UZD E3 3.2.1: O/S-glycosyl compound glycosidase DEV7UZD EC 3.2.1.35 DEV7UZD KG Metabolic pathways:cpe01100 DEV7UZD PD 2JNK; 2OZN; 2W1Q; 2W1S; 2W1U; 2WDB DEV7UZD SQ MNKNIRKIITSTVLAAMTISVLPSNLVVFATDGITENFYEIYPKPQEISYSGGEFQISDEINIVYDDGIDTYTKKRVDEVLEASNLEATVSNEIVPGKTNFLVGINESGGVVDNYFNKNIPHDESFFDEKMDANIVSVKDGVIGVIGEDTDSAFYGVTTLKHVFNQLEEGNKIQSFRADDYAEVAHRGFIEGYYGNPWSNEDRAELMKFGGDYKLNQYVFAPKDDPYHNSKWRDLYPEEKLSEIKKLAQVGNETKNRYVYALHPFMNNPVRFDTEENYQNDLGVIKAKFTQLLENDVRQFAILADDASAPAQGASMYVKLLTDLTRWLEEQQSTYPDLKTDLMFCPSDYYGNGSSAQLKELNKAEDNVSIVMTGGRIWGEVDENFANNFMNNISTEGHPGRAPFFWINWPCSDNSKQHLIMGGNDTFLHPGVDPSKIDGIVLNPMQQAEANKSALFAIADYAWNIWDNKEEADENWNDSFKYMDHGTAEETNSSLALREISKHMINQNMDGRVRPLQESVELAPKLEAFKQKYDSGASIKEDALELIAEFTNLQKAADYYKNNPGNERTRDQIIYWLNCWEDTMDAAIGYLKSAIAIEEGDDEAAWANYSEAQGAFEKSKTYGFHYVDHTEYAEVGVQHIVPFIKSMGQNLSVVIGSIVDPNRIIATYISNRQDAPTGNPDNIFDNNASTELVYKNPNRIDVGTYVGVKYSNPITLNNVEFLMGANSNPNDTMQKAKIQYTVDGREWIDLEEGVEYTMPGAIKVENLDLKVRGVRLIATEARENTWLGVRDINVNKKEDSNSGVEFNPSLIRSESWQVYEGNEANLLDGDDNTGVWYKTLNGDTSLAGEFIGLDLGKEIKLDGIRFVIGKNGGGSSDKWNKFKLEYSLDNESWTTIKEYDKTGAPAGKDVIEESFETPISAKYIRLTNMENINKWLTFSEFAIISDELENAGNKENVYTNTELDLLSLAKEDVTKLIPTDDISLNHGEYIGVKLNRIKDLSNINLEISNDTGLKLQSSMNGVEWTEITDKNTLEDGRYVRLINTSNEAVNFNLTKFEVNSNEVYEPSLVDAYVGDDGAKKAVDGDLKTRVKFLGAPSTGDTIVYDLGQEILVDNLKYVVLDTEVDHVRDGKIQLSLDGETWTDAITIGDGVENGVDDMFSTPLKNGYKHGNQSGGIVPIDSAYVEGDNLNQKARYVRILFTAPYRHRWTVINELMINNGEYISTVNDPTYISNPIEERGFAPSNLRDGNLTTSYKPNTNNGEISEGSITYRLSEKTDVRKVTIVQSGSSISNAKVMARVGDGSENVTDQWVQLGTLSNSLNEFINRDYNNIYEIKIEWTDVAPNIYEIITLNQEFEFPVNDSLKAKYDELINLSGDEYTLSSFETLKEALNEAKSILDDSNSSQKKIDKALEKLNKAEERLDLRATDFEDFNKVLTLGNSLVEEEYTAESWALFSEVLEAANEANKNKADYTQDQINQIVIDLDASIKALVKETPEVDKTNLGELINQGKSLLDESVEGFNVGEYHKGAKDGLTVEINKAEEVFNKEDATEEEINLAKESLEGAIARFNSLLIEESTGDFNGNGKIDIGDLAMVSKNIGSTTNTSLDLNKDGSIDEYEISFINHRILN DEV7UZD TD Primarily distributed in human oral cavity. DEV7UZD FC This enzyme hydrolyzes 1,4-beta-D-glycosidic linkages between N-acetyl-galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan. DEV7UZD KD 2: Bacteria DEV7UZD PL 203691: Spirochaetes DEV7UZD CL 203692: Spirochaetia DEV7UZD OD 136: Spirochaetales DEV7UZD FM 137: Spirochaetaceae DEV7UZD GE 157: Treponema DEV7UZD SP 69710: Treponema vincentii DEH31BC ID DEH31BC DEH31BC DN Hyaluronate lyase (hyaL) DEH31BC GN hyaL DEH31BC SN Alginate lyase; Poly-beta-D-glucuronate lyase; Endolytic polysaccharide lyase; Multifunctional polysaccharide lyase; Polysaccharide lyase; PL; Smon_0117 DEH31BC UC D1AWD4_STRM9 DEH31BC RD Chondroitin sulfate DEH31BC GI 29673833 DEH31BC E1 4: Lyases DEH31BC E2 4.2: Carbon-oxygen lyase DEH31BC E3 4.2.2: Polysaccharide-lyase DEH31BC EC 4.2.2.1 DEH31BC SQ MYELLLKRREYLIGNFKDLPLNKRKQIEEIQEKNIEKLEYLENLNIAEVKLKYNNILELAKAYNQVGNVRYRDEKIKVIILKTLKLLRITYYNLSSVEKVNWWQWEIGIPLLLNDIFILMNEKDFDFEKEENLKTSIYFQKDPRYSGNNPVATHPSKKPFRISTGGNRVDTVKVSLFRSILLNNEEELKLALNSLPEVWKCREKINRIETDTQRDGFYNDGSFIQHGSLAYNGTYGNVLLQGIGEILYVIGDSKYLKYLGDIYSLKDIILNSYKPFMYKGSFPDMLNGRAITRENSSDKTIGHMLLNSIMLISCGLNDEELKNLVASEILKYEDYSYFDKELSPFMYDLVKKNIHNRKKEEYGKIIKVSNIMNRVFIKDDKKAIAIAGHSENISNYESINGENTKGWYTGDGMIYLYTSDVTYTNYWNNSDTRYMSGTTEVYEDLNGINTSQILNVNMSSAKIVKAIEKDNKMIFFMEFENHNKSLKMYKSYVYTGKKLICLNTNIDTKEKIYTTIDNRLYKEKPKIVMEDKRILINDLIFNIITDHKFNFDIKESEFGYFVKIWIEHKYNENLYYEIIFEYDDKTSLIEDNKENIIIRNGNEKYLINTKEKEVLRFE DEH31BC TD Primarily distributed in human blood. DEH31BC FC This enzyme catalyzes the degradation of hyaluronan by a beta-elimination reaction and it also acts on chondroitin. DEH31BC KD 2: Bacteria DEH31BC PL 32066: Fusobacteria DEH31BC CL 203490: Fusobacteriia DEH31BC OD 203491: Fusobacteriales DEH31BC FM 1129771: Leptotrichiaceae DEH31BC GE 34104: Streptobacillus DEH31BC SP 34105: Streptobacillus moniliformis DEYILK4 ID DEYILK4 DEYILK4 DN Cytidine deaminase (cdd) DEYILK4 GN cdd DEYILK4 SN Cytidine aminohydrolase; Activation-induced cytidine deaminase; Canine hepatic cyd deaminase; AICDA; MHR_0312 DEYILK4 UC E0TLJ6_MYCHH DEYILK4 RD Azacitidine DEYILK4 E1 3: Hydrolases DEYILK4 E2 3.5: Carbon-nitrogen hydrolase DEYILK4 E3 3.5.4: Cyclic amidine hydrolase DEYILK4 EC 3.5.4.5 DEYILK4 KG Metabolic pathways:mhr01100; Pyrimidine metabolism:mhr00240 DEYILK4 SQ MFQELEKLLKITYSPYSKFPVAAVIKDAKGNIWKGVNVENAAYPSGLCAERNALFSSITYGFIPGKIQEIHILANTKEFIKPCAACLQVMIELMEYDADVYLYSITGAVEKRKLVEFLPLAFRKEFLN DEYILK4 TD Primarily distributed in human gut. DEYILK4 FC This enzyme catalyzes the deamination of cytidine and 2'-deoxycytidine with similar efficiencies. It is involved in salvage of both exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. DEYILK4 KD 2: Bacteria DEYILK4 PL 544448: Tenericutes DEYILK4 CL 31969: Mollicutes DEYILK4 OD 2085: Mycoplasmatales DEYILK4 FM 2092: Mycoplasmataceae DEYILK4 GE 2093: Mycoplasma DEYILK4 SP 2100: Mycoplasma hyorhinis DE7WRSB ID DE7WRSB DE7WRSB DN Sulfatase (sulF) DE7WRSB GN DDZ04_02500 DE7WRSB SN Dehydroepiandrosterone sulfatase; Sulfate sulfatase; Cholesterol sulfate sulfohydrolase; Arylsufatase; Arylsulfatase C; AtsA; ASC; DDZ04_02500 DE7WRSB UC A0A354WVI8_9BACT DE7WRSB RD Estrone sulfate DE7WRSB E1 3: Hydrolases DE7WRSB E2 3.1: Ester bond hydrolase DE7WRSB E3 3.1.6: Sulfuric ester hydrolase DE7WRSB EC 3.1.6.1 DE7WRSB SQ MKKKVLFLILNYFAWLPLFVIQKPWFMTYNHPSAGNISLKDGWEVILHGLKLDCTVAGYLTVIPLLMTLISIWVTGKWYKKGIYAYTVMALLAITAIFSVDVALYAFWGFRIDSTLLFYLQSPKDALASIPARLFLQQTTSFLIYSTLGYLYLKRIIINHVPVEPVSNKVGATFAIIIVGAILFIPIRGGVTTSTANVGMVYFSQNQFLNHAAINPCFSLLSSLSKQEDFSKQFNFFDEKERQDNIESLLSPVTSSDTTRILLKTRTPDILIIILESFSANVVEITGGLPDITPHLNQLGKEGVLFSHVYANSFRTDRGLVAILNGYPAQPTTSIMKYPAKSQTLPSIASSLRKAGYRSDMLYGGDINFTNMQSYFFSSGYSQITSDVDFPISDRLSKWGANDDVTFRFLLDHLKGREKEKAPWMTTFLTLSSHEPFEVPYHRFSHPYLNSVAFTDSCLGNFISRLKQSEIWDNLLIVLVADHGFRYPEQLKDYEPDRFHIPMIWSGGAINKPAEINTICNQTDLAATLLGQLGISHQEYSFSKNILSPHRCDYSFYTFNNGFAFADSLGRYTIYDNESNRVLMEDAGNTMDRLQKGKALLQTLYDDLGNR DE7WRSB TD Primarily distributed in human gut. DE7WRSB FC This enzyme catalyzes the hydrolysis of sulfate esters. DE7WRSB KD 2: Bacteria DE7WRSB PL 976: Bacteroidetes DE7WRSB CL 200643: Bacteroidia DE7WRSB OD 171549: Bacteroidales DE7WRSB FM 2005525: Tannerellaceae DE7WRSB GE 375288: Parabacteroides DE7WRSB SP 387661: Parabacteroides johnsonii DE9THM7 ID DE9THM7 DE9THM7 DN Sulfatase (sulF) DE9THM7 GN HMPREF2983_01415 DE9THM7 SN Dehydroepiandrosterone sulfatase; Sulfate sulfatase; Cholesterol sulfate sulfohydrolase; Arylsufatase; Arylsulfatase C; AtsA; ASC; HMPREF2983_01415 DE9THM7 UC A0A1F0P5Q0_9BACT DE9THM7 RD Estrone sulfate DE9THM7 E1 3: Hydrolases DE9THM7 E2 3.1: Ester bond hydrolase DE9THM7 E3 3.1.6: Sulfuric ester hydrolase DE9THM7 EC 3.1.6.1 DE9THM7 SQ MNMNDKKLIYRNPIYLIGTRFLKLYIIIGLILRIILMHATPGDASFSLGEIVRLLSIGIVSDFCMAILLALPLLIIYLGLNERKYHRIIGWMIEILLIASFVYVLFFHTIFHEYGGGAPTIARIFLGWKLFSFSMRFFFPKIRETWRRVSLYLTWAVYVFLFLCVTAGEYIFWGEFGVRYNFIAVDYLVYTHEVIGNIMESYAIIPMIGMTLLLTVGIIFLQSRHYRFNITKLYGVKMLIIHLFLYAVLATSAYFILWETHSLKSDNQYVTQLEQNGACDFVIAFQSNKLAYDQFYAMLPKQECISMYRQLSGLNKDGKKNIGDSLAENRPNIVLITVESLSADFLTRYGNKQNLTPRLDRLMQESLVFDSLFAAGNRTVRGLEALSLCLPPSAGESIIKRKANRMGNLSVGSVLSRLGYKSQFIYGGDSYFDNMGDFFSHNGYEVIDRKNIPDNQVTFANIWGVCDEDIFRKSLQVFDTNNKSGHPFFAQIMTTSNHRPYTYPAGKITVNGDPNTREASVKYTDYAIGKFIDDAKKKVWFKNTVFIVIADHCASSAGKTSLPIDRYHIPCLVYAPEIIQQEKIEKICSQIDLMPTVLSLLNLRSSVSFTGQDILAPTYHPRAFMATYQDLGYMEDNRLTVLSPVRNVQQYTLRPLQDGTYDEQLARKTDEKLVRKAQAYYQYTNLYVKAK DE9THM7 TD Primarily distributed in human gut. DE9THM7 FC This enzyme catalyzes the hydrolysis of sulfate esters. DE9THM7 KD 2: Bacteria DE9THM7 PL 976: Bacteroidetes DE9THM7 CL 200643: Bacteroidia DE9THM7 OD 171549: Bacteroidales DE9THM7 FM 171552: Prevotellaceae DE9THM7 GE 838: Prevotella DE9THM7 SP 28126: Prevotella buccae DEJEWXB ID DEJEWXB DEJEWXB DN D-Lactate dehydrogenase (ldhA) DEJEWXB GN ldhA DEJEWXB SN Glycolate dehydrogenase; D-lactate ferricytochrome C oxidoreductase; Fermentative lactate dehydrogenase; D-LDH; Q058_03541; ldhA DEJEWXB UC A0A1C7BXR3_PSEAI DEJEWXB RD DB-053072 DEJEWXB E1 1: Oxidoreductase DEJEWXB E2 1.1: CH-OH donor oxidoreductase DEJEWXB E3 1.1.1: NAD/NADP oxidoreductase DEJEWXB EC 1.1.1.28 DEJEWXB SQ MRILFFSSQAYDSESFQASNHRHGFELHFQQAHLQADTAVLAQGFEVVCAFVNDDLSRPVLERLAAGGTRLVALRSAGYNHVDLAAAEALGLPVVHVPAYSPHAVAEHAVGLILTLNRRLHRAYNRTREGDFSLHGLTGFDLHGKRVGVIGTGQIGETFARIMTGFGCELLAYDPYPNPRIQALGGRYLALDALLAESDIVSLHCPLTADTRHLIDAQRLATMKPGAMLINTGRGALVNAAALIEALKSGQLGYLGLDVYEEEADIFFEDRSDQPLQDDVLARLLSFPNVVVTAHQAFLTREALAAIADTTLDNIAAWQDGTPRNRVRA DEJEWXB TD Primarily distributed in human gut. DEJEWXB FC This enzyme has D-lactate dehydrogenase activity. DEJEWXB KD 2: Bacteria DEJEWXB PL 1224: Proteobacteria DEJEWXB CL 1236: Gammaproteobacteria DEJEWXB OD 72274: Pseudomonadales DEJEWXB FM 135621: Pseudomonadaceae DEJEWXB GE 286: Pseudomonas DEJEWXB SP 287: Pseudomonas aeruginosa DEW6V07 ID DEW6V07 DEW6V07 DN Ribosomal 23S RNA methyltransferase Erm (erm) DEW6V07 GN erm DEW6V07 SN Ribosomal RNA methyltransferase Erm; 23S rRNA methyltransferase Erm; 23S ribosomal RNA methyltransferase Erm; F6I42_04815; erm(X) DEW6V07 UC A0A5N1AHF6_CORAY DEW6V07 RD Tacrolimus DEW6V07 E1 2: Transferase DEW6V07 E2 2.1: Methylase DEW6V07 E3 2.1.1: Methyltransferase DEW6V07 EC 2.1.1.182 DEW6V07 SQ MSTYGYGRHEHGQNFLTDHKIINSIVDLVKQTSGPIIEIGPGSGALTHPISRLGRAITAVEVDAKLAAKLTKKTASASVEVVHDDFLNFPLPATPCVIVGNIPFHLTTAILRKLLHAPAWTDAVLLMQWEVARRRAGVGASTMMTAQWSPWFTFHLGSRVPRFAFRPQPNVDGGILVIRRVGDPKIPIEQRKAFQAMVHTVFTARGRGIGEILRRAGLFSSRSETQSWLRSRGIDPATLPPRLRTSDWIDLFQVTGSSPSHHRPISQSGSSQRPPQRKKRGRRR DEW6V07 TD Primarily distributed in human skin. DEW6V07 FC This enzyme introduces the most highly conserved ribosomal RNA modification, the dimethylation of adenine1518 and adenine1519 in 16S rRNA. And Strains lacking the methylase are resistant to kasugamycin. DEW6V07 KD 2: Bacteria DEW6V07 PL 201174: Actinobacteria DEW6V07 CL 1760: Actinobacteria DEW6V07 OD 85007: Corynebacteriales DEW6V07 FM 1653: Corynebacteriaceae DEW6V07 GE 1716: Corynebacterium DEW6V07 SP 43765: Corynebacterium amycolatum DEA65D8 ID DEA65D8 DEA65D8 DN Ribosomal 23S RNA methyltransferase Erm (erm) DEA65D8 GN erm(X) DEA65D8 SN Ribosomal RNA methyltransferase Erm; 23S rRNA methyltransferase Erm; 23S ribosomal RNA methyltransferase Erm; NCTC11913_00479; erm(X) DEA65D8 UC A0A381KDL2_CORJE DEA65D8 RD Tacrolimus DEA65D8 E1 2: Transferase DEA65D8 E2 2.1: Methylase DEA65D8 E3 2.1.1: Methyltransferase DEA65D8 EC 2.1.1.182 DEA65D8 SQ MSTYGYGRHEHGQNFLTDHKIINSIVDLVKESSGPIIEIGPGSGALTHPLSRLGRPITAVEVDAKLAAKLTKKTASASVEVVHGDFLNFPLPATPCVIVGNIPFHLTTAILRELLHAPAWTDAVLLMQWEVARRRAGVGASTMMTAQWSPWFTFHLGSRVPRSAFRPQPNVDGGILVIRRVGDPKIPIEQRKAFQAMVHTVFTARGRGIGEILRRAGLFSSRSETQSWLRSRGIDPATLPPRLRTSDWIDLFQVTGFSPPRHRPISQSGSSQRPPQRKKRGRRR DEA65D8 TD Primarily distributed in human skin. DEA65D8 FC This enzyme introduces the most highly conserved ribosomal RNA modification, the dimethylation of adenine1518 and adenine1519 in 16S rRNA. And Strains lacking the methylase are resistant to kasugamycin. DEA65D8 KD 2: Bacteria DEA65D8 PL 201174: Actinobacteria DEA65D8 CL 1760: Actinobacteria DEA65D8 OD 85007: Corynebacteriales DEA65D8 FM 1653: Corynebacteriaceae DEA65D8 GE 1716: Corynebacterium DEA65D8 SP 38289: Corynebacterium jeikeium DEIU0XN ID DEIU0XN DEIU0XN DN N-acylhomoserine lactone acylase (lacA) DEIU0XN GN AVS7_00617 DEIU0XN SN Acyl-homoserine lactone acylase; Acyl-HSL acylase; AHL acylase; AHL amidase; AHL-acylase; Protein related to penicillin acylase; AVS7_00617 DEIU0XN UC A0A0A1VBK6_9BURK DEIU0XN RD Carbenicillin DEIU0XN E1 3: Hydrolases DEIU0XN E2 3.5: Carbon-nitrogen hydrolase DEIU0XN E3 3.5.1: Linear amide hydrolase DEIU0XN EC 3.5.1.97 DEIU0XN PD 4YF9; 4YFA; 4YFB; 5C9I DEIU0XN SQ MRESIHRGAWPRSVLTLAAVAALAACGGSGGGDGSTYSAEIRRTTMGVPHIKAGNWGSAGYGFGYVQAQDNLCTMADSFLTYRGERSRHLGGSAQLVYNSTLGRPRNIDSDFFHRHVISDEAVDRTMAAQPAKLLQMVEGFAAGYNRYVREAKAGGSAHAACRSEAWVQPITARDVWRRIYAANLAGGYSNFAEAIANAQPPQAKAGAQEPAAFEPGRTRAPSLQVGGELGVGSNMYGFGTAATGEGSGVLFGNPHWYWKGPDRFYQAQLTIDGEANVSGVSFLGLPVIQIGFNDSVAWSHTVSTARRFGFFQLSLVQGEPTSYLRDGVPVKMKPATITVPSRNADGSVSDVTRTLYHSEFGPLVNLAGLNPALAWSQGTAFAIRDINGENFRTLRTWMRWNQAKSLDEFIAIQKEEASIPWVNTVAVGRGSAKAWYADIGAVPNVSPAQTAACTTPFGMAVGQALPNVPFFDGSRSECDWLTDADSVQKGAVGVSRMPSLQRDDYVGNMNDSYWLANVHAPLTGYPAIFGPAGTSAQTLRTRMGHTMALERLAGTDGYAGNKATSAVVREMVLGSRVFSAERFKDEVLDLICTPAQWTVNGAAVDAAQACAVLAAWDNRGRKDSRGSHLWDEFWSRVPTASLFTVPFSAADPLNTPRGINAAAADALRQAMATAIARVGQSGYALDAPRGEVLYATRGGTRLPLYGGCGAMGYFTITCSENDITQGGYSMDGQPNASNSYMQVVSFPASGVQAHTFLTFSLSDDPASPHHGDYTKAYSAGQWLRVPFTEAEITGNADYRTATVKE DEIU0XN TD Primarily distributed in human gut. DEIU0XN FC This enzyme catalyzes the conversion of N-acyl-L-homoserine lactone to N-acyl-L-homoserine. DEIU0XN KD 2: Bacteria DEIU0XN PL 1224: Proteobacteria DEIU0XN CL 28216: Betaproteobacteria DEIU0XN OD 80840: Burkholderiales DEIU0XN FM 80864: Comamonadaceae DEIU0XN GE 12916: Acidovorax DEIU0XN SP 721785: Acidovorax ebreus DE90ZBW ID DE90ZBW DE90ZBW DN Flavin adenine dinucleotide dehydrogenase (fadd) DE90ZBW GN apbE1 DE90ZBW SN FAD pyrophosphorylase; FAD synthase; FMN adenylyltransferase DE90ZBW UC APBE1_KLEP3 DE90ZBW RD RO-7-0207 DE90ZBW E1 1: Oxidoreductase DE90ZBW E2 1.5: CH-NH donor oxidoreductase DE90ZBW E3 1.5.1: NAD/NADP acceptor oxidoreductase DE90ZBW EC 1.5.1.37 DE90ZBW SQ MDMTFFRAALLGACVLLSGCDSATTPASPASTATVLDGKTMGTFWRVSVIGVDEAKAEALRAKVQAQLDADDRLLSTWKNDSALMRFNHAADTRPWPVSEAMVDIVTLSLRIGAKTHGAMDITVGPLVNLWGFGPDKQPVTTPDAQAIAAAKARTGLQHLQVINQSGRQFLQKDIPDLFVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALVSRGMNGEGKPWRVAIQKPTDRENAVQAIVDINGHGISTSGSYRNYYELDGKRISHVIDPQTGQPITHKLVSVTVIAPTALEADGWDTGLMVLGPEKAQQVVREQGLAVYMIVKEGEGFKTWMSPQFRTFLVGEKN DE90ZBW TD Primarily distributed in human gut. DE90ZBW FC This enzyme can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. But it can not reduce riboflavin and does not use NADPH as acceptor. DE90ZBW KD 2: Bacteria DE90ZBW PL 1239: Firmicutes DE90ZBW CL 186801: Clostridia DE90ZBW OD 186802: Clostridiales DE90ZBW FM 541000: Ruminococcaceae DE90ZBW GE 1485: Clostridium DE90ZBW SP 1535: Clostridium leptum DE5CJFM ID DE5CJFM DE5CJFM DN Flavin adenine dinucleotide dehydrogenase (fadd) DE5CJFM GN apbE1 DE5CJFM SN FAD pyrophosphorylase; FAD synthase; FMN adenylyltransferase DE5CJFM UC APBE1_KLEP3 DE5CJFM RD RO-7-0207 DE5CJFM E1 1: Oxidoreductase DE5CJFM E2 1.5: CH-NH donor oxidoreductase DE5CJFM E3 1.5.1: NAD/NADP acceptor oxidoreductase DE5CJFM EC 1.5.1.37 DE5CJFM SQ MDMTFFRAALLGACVLLSGCDSATTPASPASTATVLDGKTMGTFWRVSVIGVDEAKAEALRAKVQAQLDADDRLLSTWKNDSALMRFNHAADTRPWPVSEAMVDIVTLSLRIGAKTHGAMDITVGPLVNLWGFGPDKQPVTTPDAQAIAAAKARTGLQHLQVINQSGRQFLQKDIPDLFVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALVSRGMNGEGKPWRVAIQKPTDRENAVQAIVDINGHGISTSGSYRNYYELDGKRISHVIDPQTGQPITHKLVSVTVIAPTALEADGWDTGLMVLGPEKAQQVVREQGLAVYMIVKEGEGFKTWMSPQFRTFLVGEKN DE5CJFM TD Primarily distributed in human gut. DE5CJFM FC This enzyme can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. But it can not reduce riboflavin and does not use NADPH as acceptor. DE5CJFM KD 2: Bacteria DE5CJFM PL 1239: Firmicutes DE5CJFM CL 186801: Clostridia DE5CJFM OD 186802: Clostridiales DE5CJFM FM 31979: Clostridiaceae DE5CJFM GE 1485: Clostridium DE5CJFM SP 1509: Clostridium sporogenes DE9WXYE ID DE9WXYE DE9WXYE DN Flavin adenine dinucleotide dehydrogenase (fadd) DE9WXYE GN apbE1 DE9WXYE SN FAD pyrophosphorylase; FAD synthase; FMN adenylyltransferase DE9WXYE UC APBE1_KLEP3 DE9WXYE RD RO-7-0207 DE9WXYE E1 1: Oxidoreductase DE9WXYE E2 1.5: CH-NH donor oxidoreductase DE9WXYE E3 1.5.1: NAD/NADP acceptor oxidoreductase DE9WXYE EC 1.5.1.37 DE9WXYE SQ MDMTFFRAALLGACVLLSGCDSATTPASPASTATVLDGKTMGTFWRVSVIGVDEAKAEALRAKVQAQLDADDRLLSTWKNDSALMRFNHAADTRPWPVSEAMVDIVTLSLRIGAKTHGAMDITVGPLVNLWGFGPDKQPVTTPDAQAIAAAKARTGLQHLQVINQSGRQFLQKDIPDLFVDLSTVGEGYAADHLARLMEQEGISRYLVSVGGALVSRGMNGEGKPWRVAIQKPTDRENAVQAIVDINGHGISTSGSYRNYYELDGKRISHVIDPQTGQPITHKLVSVTVIAPTALEADGWDTGLMVLGPEKAQQVVREQGLAVYMIVKEGEGFKTWMSPQFRTFLVGEKN DE9WXYE TD Primarily distributed in human gut. DE9WXYE FC This enzyme can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. But it can not reduce riboflavin and does not use NADPH as acceptor. DE9WXYE KD 2: Bacteria DE9WXYE PL 1239: Firmicutes DE9WXYE CL 186801: Clostridia DE9WXYE OD 186802: Clostridiales DE9WXYE FM 186806: Eubacteriaceae DE9WXYE GE 1730: Eubacterium DE9WXYE SP 1732: Eubacterium oxidoreducens DEAVXGM ID DEAVXGM DEAVXGM DN Nitroreductase (NTR) DEAVXGM GN NTR DEAVXGM SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; DWW99_07865 DEAVXGM UC A0A412R9E4_9FIRM DEAVXGM RD Nitrofurantoin DEAVXGM E1 1: Oxidoreductase DEAVXGM E2 1.5: CH-NH donor oxidoreductase DEAVXGM E3 1.5.1: NAD/NADP acceptor oxidoreductase DEAVXGM EC 1.5.1.39 DEAVXGM SQ MKITEALKARRSYYAINRELPVAIDRVMDMVKELTELVPDAFNMKSSRVAVVHGEKQDQLWNKIYDVFEGKVAREKIDSFRAGSGTILYFYDRKVVESLQKQYPLYADNFPVWASQSSAMLQLAVWSGLRELNIGASLQHYNPVIDNAVKELLHLSGDYVLVAEMPFGGIVEEPAPKDKEEIEKRVFSAC DEAVXGM TD Primarily distributed in human gut. DEAVXGM FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DEAVXGM KD 2: Bacteria DEAVXGM PL 1239: Firmicutes DEAVXGM CL 186801: Clostridia DEAVXGM OD 186802: Clostridiales DEAVXGM FM 541000: Ruminococcaceae DEAVXGM GE 1485: Clostridium DEAVXGM SP 1535: Clostridium leptum DEU37LK ID DEU37LK DEU37LK DN L-arabinose isomerase (araA) DEU37LK GN araA DEU37LK SN Isomerase L-arabinose; D-arabinose aldose-ketose-isomerase; araA; CLOHYLEM_05792; LAJLEIBI_03201 DEU37LK UC C0C0X3_9FIRM DEU37LK RD CERC-801 DEU37LK GI 42452782 DEU37LK E1 5: Isomerase DEU37LK E2 5.3: Intramolecular oxidoreductase DEU37LK E3 5.3.1: Aldose/ketose isomerase DEU37LK EC 5.3.1.4 DEU37LK SQ MIKSKEYKFWFCTGSQDLYGEECLAHVAEHSRRIVEALNASGALPYEVVWKPTLITNELIRKTFNEANTDETCAGVITWMHTFSPAKSWILGLQEYRKPLLHLHTQFNEEIPYDTIDMDFMNENQAAHGDREYGHIFSRLRMERKVVAGYWADPKVQKKIGSWMRTAVGVIESSHVRVMRIADNMRNVAVTEGDKVEAQIKFGWEVDTYPVNEIAEAVAEVSKSDIGTLVEEYYDKYDILLEGRDEKEFREHVAVQAGIEIGFERFLEERDYQAIVTHFGDLGSLKQLPGLAIQRLMEKGYGFGGEGDWKTAAMVRIMKIMTEGVKDARGTSFMEDYTYNLIPGKEGILQAHMLEVCPSVAEGPISIKCQPLTMGDREDPARLVFTSKEGPAVAASLIDLGDRFRLIINDVDCKKTEKPMPKLPVATAFWTPQPDLQTGAEAWILAGGAHHTAFSYDLSAGQLGDWADAMGIEAVYIDKNTEIRQFKNELRWNAAAYKLGI DEU37LK TD Primarily distributed in human gut. DEU37LK FC This enzyme catalyzes the conversion of L-arabinose to L-ribulose. It requires a divalent metal ion and binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism. It can also convert D-galactose to D-tagatose with lower efficiency. DEU37LK KD 2: Bacteria DEU37LK PL 1239: Firmicutes DEU37LK CL 186801: Clostridia DEU37LK OD 186802: Clostridiales DEU37LK FM 186803: Lachnospiraceae DEU37LK GE 1506553: Lachnoclostridium DEU37LK SP 89153: Clostridium hylemonae DEUWV1D ID DEUWV1D DEUWV1D DN Heparin lyase (hepB) DEUWV1D GN hepB DEUWV1D SN Heparin and heparin-sulfate lyase; Heparin-sulfate lyase; Heparinase II; HepII DEUWV1D UC HEPB_PEDHD DEUWV1D RD Heparin DEUWV1D E1 4: Lyases DEUWV1D E2 4.2: Carbon-oxygen lyase DEUWV1D E3 4.2.2: Polysaccharide-lyase DEUWV1D EC 4.2.2.7 DEUWV1D PD 2FUQ; 2FUT; 3E7J; 3E80 DEUWV1D SQ MKRQLYLYVIFVVVELMVFTTKGYSQTKADVVWKDVDGVSMPIPPKTHPRLYLREQQVPDLKNRMNDPKLKKVWADMIKMQEDWKPADIPEVKDFRFYFNQKGLTVRVELMALNYLMTKDPKVGREAITSIIDTLETATFKPAGDISRGIGLFMVTGAIVYDWCYDQLKPEEKTRFVKAFVRLAKMLECGYPPVKDKSIVGHASEWMIMRDLLSVGIAIYDEFPEMYNLAAGRFFKEHLVARNWFYPSHNYHQGMSYLNVRFTNDLFALWILDRMGAGNVFNPGQQFILYDAIYKRRPDGQILAGGDVDYSRKKPKYYTMPALLAGSYYKDEYLNYEFLKDPNVEPHCKLFEFLWRDTQLGSRKPDDLPLSRYSGSPFGWMIARTGWGPESVIAEMKVNEYSFLNHQHQDAGAFQIYYKGPLAIDAGSYTGSSGGYNSPHNKNFFKRTIAHNSLLIYDPKETFSSSGYGGSDHTDFAANDGGQRLPGKGWIAPRDLKEMLAGDFRTGKILAQGFGPDNQTPDYTYLKGDITAAYSAKVKEVKRSFLFLNLKDAKVPAAMIVFDKVVASNPDFKKFWLLHSIEQPEIKGNQITIKRTKNGDSGMLVNTALLPDAANSNITSIGGKGKDFWVFGTNYTNDPKPGTDEALERGEWRVEITPKKAAAEDYYLNVIQIADNTQQKLHEVKRIDGDKVVGVQLADRIVTFSKTSETVDRPFGFSVVGKGTFKFVMTDLLPGTWQVLKDGKILYPALSAKGDDGALYFEGTEGTYRFLR DEUWV1D TD Primarily distributed in human blood. DEUWV1D FC This enzyme catalyzes the eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends DEUWV1D KD 2: Bacteria DEUWV1D PL 32066: Fusobacteria DEUWV1D CL 203490: Fusobacteriia DEUWV1D OD 203491: Fusobacteriales DEUWV1D FM 1129771: Leptotrichiaceae DEUWV1D GE 34104: Streptobacillus DEUWV1D SP 34105: Streptobacillus moniliformis DEQUGC0 ID DEQUGC0 DEQUGC0 DN D-Lactate dehydrogenase (ldhA) DEQUGC0 GN ldhA DEQUGC0 SN Glycolate dehydrogenase; D-lactate ferricytochrome C oxidoreductase; Fermentative lactate dehydrogenase; D-LDH; Q058_03541; ldhA DEQUGC0 UC A0A1C7BXR3_PSEAI DEQUGC0 RD D-glucose DEQUGC0 E1 1: Oxidoreductase DEQUGC0 E2 1.1: CH-OH donor oxidoreductase DEQUGC0 E3 1.1.1: NAD/NADP oxidoreductase DEQUGC0 EC 1.1.1.28 DEQUGC0 SQ MRILFFSSQAYDSESFQASNHRHGFELHFQQAHLQADTAVLAQGFEVVCAFVNDDLSRPVLERLAAGGTRLVALRSAGYNHVDLAAAEALGLPVVHVPAYSPHAVAEHAVGLILTLNRRLHRAYNRTREGDFSLHGLTGFDLHGKRVGVIGTGQIGETFARIMTGFGCELLAYDPYPNPRIQALGGRYLALDALLAESDIVSLHCPLTADTRHLIDAQRLATMKPGAMLINTGRGALVNAAALIEALKSGQLGYLGLDVYEEEADIFFEDRSDQPLQDDVLARLLSFPNVVVTAHQAFLTREALAAIADTTLDNIAAWQDGTPRNRVRA DEQUGC0 TD Primarily distributed in human gut. DEQUGC0 FC This enzyme has D-lactate dehydrogenase activity. DEQUGC0 KD 2: Bacteria DEQUGC0 PL 1239: Firmicutes DEQUGC0 CL 909932: Negativicutes DEQUGC0 OD 1843489: Veillonellales DEQUGC0 FM 31977: Veillonellaceae DEQUGC0 GE 906: Megasphaera DEQUGC0 SP 907: Megasphaera elsdenii DEIPST6 ID DEIPST6 DEIPST6 DN Cytochrome P450 147G1 (cyp147) DEIPST6 GN cyp147G1 DEIPST6 SN Cytochrome P450 family 147 subfamily G member 1; P450 147G1; MMAR_2930; P450 147G1; cyp147G1 DEIPST6 UC B2HE89_MYCMM DEIPST6 RD Omega-3 Fatty acids DEIPST6 E1 1: Oxidoreductase DEIPST6 E2 1.14: Oxygen paired donor oxidoreductase DEIPST6 E3 1.14.15: Iron-sulfur protein donor oxidoreductase DEIPST6 EC 1.14.15.28 DEIPST6 SQ MNAETAWAEAMKFENRPNPYPYFDELRKTPVAKVAEKTYVVTGYRELLALAHDPRISSDITRSPSGFGGEAPQPEPGSEHVQAYGQDASIIVSDPPDHDRARRQVMRHFAPPHSPDLIPSMEPFVVRLANDLLNQASARGSTRLDVVEDFAYPIPVAVICKILGVPIEDEPKFHAWIFDFMAGTDLGPEGDTEEGQVLAEKGRVSTAALTDYLGDLVRSYAKTPGEGLLSKLLHDDGPDGPMSVPETTANALLLLVAGHDSTVNTITNCVMTLLRNPGSWDLVRQRPELIPRTIEEVQRLQSAVQFFPSRSATDEIEIGGTVIPAGSAVHLIYAAANRDPRRFDNPNRFDPLREDNEHFGWGSGIHTCMGGPLARLEVNLAVEIFLRRVQSPKLVVDPPPYRHNQIFRGPRHLWVDFAAITE DEIPST6 TD Primarily distributed in human skin. DEIPST6 FC This enzyme catalyzes the selective hydroxylation of linear and -2 methyl branched fatty acids at the -1 position. Substrates of Cytochrome P450 147G1 include fatty acids ranging from octanoic to hexadecanoic acid. DEIPST6 KD 2: Bacteria DEIPST6 PL 201174: Actinobacteria DEIPST6 CL 1760: Actinobacteria DEIPST6 OD 85007: Corynebacteriales DEIPST6 FM 1762: Mycobacteriaceae DEIPST6 GE 1763: Mycobacterium DEIPST6 SP 1781: Mycobacterium marinum DEUWAV0 ID DEUWAV0 DEUWAV0 DN Cytochrome P450 102D1 (cyp102) DEUWAV0 GN cyp102A1 DEUWAV0 SN Cytochrome P450 family 102 subfamily D member 1; Flavocytochrome P450 102D1; P450 102D1; cyp102D1 DEUWAV0 UC CPXB_BACMB DEUWAV0 RD Daidzein DEUWAV0 GI 29911283 DEUWAV0 E1 1: Oxidoreductase DEUWAV0 E2 1.14: Oxygen paired donor oxidoreductase DEUWAV0 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEUWAV0 EC 1.14.14.1 DEUWAV0 KG Aminobenzoate degradation:bmeg00627; Fatty acid degradation:bmeg00071; Microbial metabolism in diverse environments:bmeg01120; Tryptophan metabolism:bmeg00380 DEUWAV0 PD 1BU7; 1BVY; 1FAG; 1FAH; 1JME; 1JPZ; 1P0V; 1P0W; 1P0X; 1SMI; 1SMJ; 1YQO; 1YQP; 1ZO4; 1ZO9; 1ZOA; 2BMH; 2HPD; 2IJ2; 2IJ3; 2IJ4; 2J1M; 2J4S; 2NNB; 2UWH; 2X7Y; 2X80; 3BEN; 3CBD; 3DGI; 3EKB; 3EKD; 3EKF; 3HF2; 3KX3; 3KX4; 3KX5; 3M4V; 3NPL; 3PSX; 3WSP; 4DQK; 4DQL; 4DTW; 4DTY; 4DTZ; 4DU2; 4DUA; 4DUB; 4DUC; 4DUD; 4DUE; 4DUF; 4H23; 4H24; 4HGF; 4HGG; 4HGH; 4HGI; 4HGJ; 4KEW; 4KEY; 4KF0; 4KF2; 4KPA; 4KPB; 4O4P; 4RSN; 4WG2; 4ZF6; 4ZF8; 4ZFA; 4ZFB; 5B2U; 5B2V; 5B2W; 5B2X; 5B2Y; 5DYP; 5DYZ; 5E78; 5E7Y; 5E9Z; 5JQ2; 5JQU; 5JQV; 5JTD; 5OG9; 5UCW; 5XA3; 5XHJ; 5ZIS; 5ZLH; 6H1O; 6H1S; 6IAO DEUWAV0 SQ MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGIPSPSTEQSAKKVRKKAENAHNTPLLVLYGSNMGTAEGTARDLADIAMSKGFAPQVATLDSHAGNLPREGAVLIVTASYNGHPPDNAKQFVDWLDQASADEVKGVRYSVFGCGDKNWATTYQKVPAFIDETLAAKGAENIADRGEADASDDFEGTYEEWREHMWSDVAAYFNLDIENSEDNKSTLSLQFVDSAADMPLAKMHGAFSTNVVASKELQQPGSARSTRHLEIELPKEASYQEGDHLGVIPRNYEGIVNRVTARFGLDASQQIRLEAEEEKLAHLPLAKTVSVEELLQYVELQDPVTRTQLRAMAAKTVCPPHKVELEALLEKQAYKEQVLAKRLTMLELLEKYPACEMKFSEFIALLPSIRPRYYSISSSPRVDEKQASITVSVVSGEAWSGYGEYKGIASNYLAELQEGDTITCFISTPQSEFTLPKDPETPLIMVGPGTGVAPFRGFVQARKQLKEQGQSLGEAHLYFGCRSPHEDYLYQEELENAQSEGIITLHTAFSRMPNQPKTYVQHVMEQDGKKLIELLDQGAHFYICGDGSQMAPAVEATLMKSYADVHQVSEADARLWLQQLEEKGRYAKDVWAG DEUWAV0 TD Primarily distributed in human gut. DEUWAV0 FC This enzyme is P-450 heme-thiolate protein, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. DEUWAV0 KD 2: Bacteria DEUWAV0 PL 201174: Actinobacteria DEUWAV0 CL 1760: Actinobacteria DEUWAV0 OD 85011: Streptomycetales DEUWAV0 FM 2062: Streptomycetaceae DEUWAV0 GE 1883: Streptomyces DEUWAV0 SP 33903: Streptomyces avermitilis DE30GZN ID DE30GZN DE30GZN DN Carboxylic ester hydrolase (CEH) DE30GZN GN CEH DE30GZN SN Carboxylic ester hydrolase CEH; Acyl coenzyme A:cholesterol acyltransferase; CPT75_14810 DE30GZN UC A0A317G4I6_BUTFI DE30GZN RD Alpha-linolenic acid DE30GZN E1 3: Hydrolases DE30GZN E2 3.1: Ester bond hydrolase DE30GZN E3 3.1.1: Carboxylic ester hydrolase DE30GZN EC 3.1.1.1 DE30GZN SQ MNTIIRDTDLGQIKGLELDDNTVQFRGIRYATARRFAYPEPVTSFDGIYDATRFGYACPQFRTYDPEDQKDPAPFYYKEFREGAEFTYDEDCLFLNIYAPKDAKKVPVIIYIHGGAFLGGCGNENHMDGTAYARKGIIFVSINYRLGVLGFLCDRKLTKESGHSGNYGLYDQLEAIKWVHDHIENFGGDKSNITLFGQSAGAMSIQQHCFSPLTKPYIQKVYMASGAGIGKEFAGVSPVEDSYDYFERLTSLLGDDPEDWRQIPVKELIEKFQSVIDRDLMSHCCPHIDGLIIPKDPAQSLEDKDYADVPYLLSTNSEDMAPQFLHQMSKDFCNTVNRNGGRAYYFYFSRKLPGDDKGAFHSAELWYTIGSIRKCWRPMTQEDFDLSDKLVDMICEFANTGAISYSSFDTPMASFEIHP DE30GZN TD Primarily distributed in human gut and stomach. DE30GZN FC This enzyme can hydrolyse vitamin A esters anh has wide specificity. DE30GZN KD 2: Bacteria DE30GZN PL 1239: Firmicutes DE30GZN CL 186801: Clostridia DE30GZN OD 186802: Clostridiales DE30GZN FM 186803: Lachnospiraceae DE30GZN GE 830: Butyrivibrio DE30GZN SP 831: Butyrivibrio fibrisolvens DET9I1W ID DET9I1W DET9I1W DN Beta-lactamase (blaB) DET9I1W GN cblA DET9I1W SN Penicillinase; Cephalosporinase; Beta-lactam; cblA DET9I1W UC BLAC_BACUN DET9I1W RD Piperacillin DET9I1W GI 31505337 DET9I1W E1 3: Hydrolases DET9I1W E2 3.5: Carbon-nitrogen hydrolase DET9I1W E3 3.5.2: Cyclic amide hydrolase DET9I1W EC 3.5.2.6 DET9I1W SQ MKAYFIAILTLFTCIATVVRAQQMSELENRIDSLLNGKKATVGIAVWTDKGDMLRYNDHVHFPLLSVFKFHVALAVLDKMDKQSISLDSIVSIKASQMPPNTYSPLRKKFPDQDFTITLRELMQYSISQSDNNACDILIEYAGGIKHINDYIHRLSIDSFNLSETEDGMHSSFEAVYRNWSTPSAMVRLLRTADEKELFSNKELKDFLWQTMIDTETGANKLKGMLPAKTVVGHKTGSSDRNADGMKTADNDAGLVILPDGRKYYIAAFVMDSYETDEDNANIIARISRMVYDAMR DET9I1W TD Primarily distributed in human gut. DET9I1W FC This enzyme hydrolyzes beta-lactam. DET9I1W KD 2: Bacteria DET9I1W PL 976: Bacteroidetes DET9I1W CL 200643: Bacteroidia DET9I1W OD 171549: Bacteroidales DET9I1W FM 815: Bacteroidaceae DET9I1W GE 816: Bacteroides DET9I1W SP 820: Bacteroides uniformis DET9I1W SU Bacteroides uniformis B 371 DENJ2SQ ID DENJ2SQ DENJ2SQ DN Beta-lactamase (blaB) DENJ2SQ GN ccrA DENJ2SQ SN Penicillinase; Cephalosporinase; Beta-lactam; Metallo-beta-lactamase type 2a; Carbapenem and cephamycin resistance; CCRA; Imipenem-cefoxitin hydrolyzing enzyme; Metallo-beta-lactamase type IIa; Zinc-requiring beta-lactamase; ccrA; cfiA DENJ2SQ UC BLAB_BACFG DENJ2SQ RD Meropenem DENJ2SQ E1 3: Hydrolases DENJ2SQ E2 3.5: Carbon-nitrogen hydrolase DENJ2SQ E3 3.5.2: Cyclic amide hydrolase DENJ2SQ EC 3.5.2.6 DENJ2SQ PD 1A7T; 1A8T; 1HLK; 1KR3; 1ZNB; 2BMI; 2ZNB; 3ZNB; 4ZNB DENJ2SQ SQ MKTVFILISMLFPVAVMAQKSVKISDDISITQLSDKVYTYVSLAEIEGWGMVPSNGMIVINNHQAALLDTPINDAQTEMLVNWVTDSLHAKVTTFIPNHWHGDCIGGLGYLQRKGVQSYANQMTIDLAKEKGLPVPEHGFTDSLTVSLDGMPLQCYYLGGGHATDNIVVWLPTENILFGGCMLKDNQATSIGNISDADVTAWPKTLDKVKAKFPSARYVVPGHGDYGGTELIEHTKQIVNQYIESTSKP DENJ2SQ TD Primarily distributed in human gut. DENJ2SQ FC This enzyme confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. DENJ2SQ KD 2: Bacteria DENJ2SQ PL 976: Bacteroidetes DENJ2SQ CL 200643: Bacteroidia DENJ2SQ OD 171549: Bacteroidales DENJ2SQ FM 815: Bacteroidaceae DENJ2SQ GE 816: Bacteroides DENJ2SQ SP 817: Bacteroides fragilis DEWTCUK ID DEWTCUK DEWTCUK DN Beta-glucuronidase (uidA) DEWTCUK GN gusA DEWTCUK SN Beta-galactosidase/beta-glucuronidase; Beta-galactosidase BgaB; gusA DEWTCUK UC Q9AHJ8_LACGS DEWTCUK RD Bazedoxifene DEWTCUK E1 3: Hydrolases DEWTCUK E2 3.2: Glycosylase DEWTCUK E3 3.2.1: O/S-glycosyl compound glycosidase DEWTCUK EC 3.2.1.31 DEWTCUK SQ MESALYPIQNKYRFNTLMNGTWQFETDPNSVGLDEGWNKELPDPEEMPVPGTFAELTTKRDRKYYTGDFWYQKDFFIPSFLKKKELYIRFGSVTHRAKVFINGHEVGQHEGGFLPFQVKISNYINYDQTNRVTVLVNNELSEKAIPCGTEEILDNGQKLAQPYFDFFNYSGIMRNVWLLALPQSQITNFKLNYQLANNKATITYNIEANNNAEFKVTLFDNQKEVACATSKNTSSLTIKNPHLWSPNDPYSYKIKIEMLEDGKTVDEYTDKIGIRTVKIVNDKILLNNHPIYLKGFGKHEDFNVLGKAVNESIIKRDYECMKWIGANCFRSSHYPYAEEWYQYADKYGFLIIDEVPAVGLNRSITNFLNVTNSNQSHFFASKTVPELKKVHEQEIKEMIDRDQRHPSVIAWSLFNEPESTTQESYDYFKDIFAFARKLDPQNRPYTGTLVMGSGPKVDKLHPLCDFVCLNRYYGWYVAGGPEIVNAKKMLEDELDGWQNLKLNKPFVFTEFGADTLSSSHRLPDEMWSQEYQNEYYQMYFDIFKKYPFICGELVWNFADFKTSEGIMRVGGNDKGIFTRDREPKDIAFTLKKRWQQLN DEWTCUK TD Primarily distributed in human gut. DEWTCUK FC This enzyme takes part in glucuronoside catabolic process. It catalyzes the hydrolysis of beta-glucuronide containing substrates. DEWTCUK KD 2: Bacteria DEWTCUK PL 1239: Firmicutes DEWTCUK CL 91061: Bacilli DEWTCUK OD 186826: Lactobacillales DEWTCUK FM 33958: Lactobacillaceae DEWTCUK GE 1578: Lactobacillus DEWTCUK SP 1596: Lactobacillus gasseri DEQB4LT ID DEQB4LT DEQB4LT DN Beta-galactosidase (bgaB) DEQB4LT GN bgaB DEQB4LT SN Beta-galactosidase/glucuronidase; Beta-galactosidase BgaBeta; Beta-Gal II; Beta-gal; C8D82_10873 DEQB4LT UC A0A2U1B4D0_9BACT DEQB4LT RD Lactose DEQB4LT E1 3: Hydrolases DEQB4LT E2 3.2: Glycosylase DEQB4LT E3 3.2.1: O/S-glycosyl compound glycosidase DEQB4LT EC 3.2.1.23 DEQB4LT SQ MTVIRNFRRILHGGDYNPDQWLHVPGTVDRDFELMDEAHCNTFSVAIFSWAQLEPEPDRFEFGWLDDIFERCGKSGKKLFLATPSASKPAWLAQRWPDSCRMDRDGTRQRWGVRQNSCFASPGFRERVRLINRKLAERYADHPALGGWHISNEYHGECACELCRNRFYDYLKQRYGTLEKLNQVYWSAFWGHTFTDWKQVEPFDHSMDAAALDWRRFCSDAVVEFFRMEIDAVREFSDAPVTTNMMGLFPTLDYWKFAPLCDFICDDCYPTWYDGDTEREAAWLSLLHDMHYTMLDKPFVMMESCPGIPNYKPYPKLRRPGEFEREMLLALGHGADGTLYFQWRKGRNNCEKFHGAVVGHDGTDRTMVFRQVAAYGEKLERIAGLADAAKKPEAAVVYDWESNWAFEQCNCAGGKEVKQWDATAISHYRALWNCNIDLAVIDSEQDFSRYKLLVAPMLFMFKPGVLERFRSFVEQGGTLVATYFSGYVDENNGCFLGGNPGGAAGRELFGVWSEDFDGLQPTTRQSIVWKGKSYPVTDYAELLHAEGAEVEAVYGDDFYAGTPAVTRKRAGKGNVIYLGARTGMEFLNDFYGALLKESGVEPVLAGLPETVRAARRSAVSGGDYFFLYNLSGKEQPVKLPEAMEDVWNGGGAADTVTLPPNGATVLYRA DEQB4LT TD Primarily distributed in human gut. DEQB4LT FC This enzyme hydrolyzes alpha-L-arabinoside and beta-D-fucosides and beta-D-glucosides. DEQB4LT KD 2: Bacteria DEQB4LT PL 256845: Lentisphaerae DEQB4LT CL 1313211: Lentisphaeria DEQB4LT OD 278082: Victivallales DEQB4LT FM 255528: Victivallaceae DEQB4LT GE 172900: Victivallis DEQB4LT SP 172901: Victivallis vadensis DEQB4LT SU Victivallis vadensis ATCC BAA-548 DEFHZW7 ID DEFHZW7 DEFHZW7 DN Arylamine N-acetyltransferase (NAT) DEFHZW7 GN nat DEFHZW7 SN N-hydroxyarylamine O-acetyltransferase; nhoA; nat; NCTC10741_01829; BVX91_14895 DEFHZW7 UC A0A3P8LE58_TSUPA DEFHZW7 RD Asacolitin DEFHZW7 E1 2: Transferase DEFHZW7 E2 2.3: Acyltransferase DEFHZW7 E3 2.3.1: Acyltransferase DEFHZW7 EC 2.3.1.5 DEFHZW7 SQ MNDDAAWGAPALDLPRYLHRIGLQAPPAPDLAGLSTLVRAHALTLPWENFDAVRGIPGELTIDALQRRMIEGRRGYGCTGHVPLLAAALQRTGFRFGAASGRVLVDGGPSASTHALLIVEVDGAPHLAEVGFGAVPLAPLRLESGLEQDAGGWRYRLTAEAVGFGEEWRLDFLDPSSGQWRPQYRFALADRTWSDLRMTNFYVATSPHSPFRGRLMAVVNRPGERHVLTRDAVISTRPDGFRETVPYVAADRRAILAESFAIDLPEDEAAALAAVSGS DEFHZW7 TD Primarily distributed in human lung. DEFHZW7 FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DEFHZW7 KD 2: Bacteria DEFHZW7 PL 1224: Proteobacteria DEFHZW7 CL 1236: Gammaproteobacteria DEFHZW7 OD 135623: Vibrionales DEFHZW7 FM 641: Vibrionaceae DEFHZW7 GE 662: Vibrio DEFHZW7 SP 666: Vibrio cholerae DEKBP7I ID DEKBP7I DEKBP7I DN Arylamine N-acetyltransferase (NAT) DEKBP7I GN nat DEKBP7I SN N-hydroxyarylamine O-acetyltransferase; nhoA; nat; TUEID40_02779; SAMEA3531848_04040 DEKBP7I UC A0A5E5R1G5_PSEAI DEKBP7I RD Asacolitin DEKBP7I E1 2: Transferase DEKBP7I E2 2.3: Acyltransferase DEKBP7I E3 2.3.1: Acyltransferase DEKBP7I EC 2.3.1.5 DEKBP7I SQ MTPLTPEQTHAYLHHIGIDDPGPPSLANLDRLIDAHLRRVAFENLDVLLDRPIEIDADKVFAKVVEGSRGGYCFELNSLFARLLLALGYELELLVARVRWGLPEDVPLTQQSHLMLRLYLAEGEFLVDVGFGSANPPRALPLPGDEADAGQVHCVRLVDPHAGLYESAVRGRSGWLPLYRFDLRPQLWIDYIPRNWYTSTHPHSVFRQGLKAAITEGDLRLTLADGLFGQRAGNGETLQRQLRDVEELLDILQTRFRLRLDPASEVPALARRLAGLISA DEKBP7I TD Primarily distributed in human gut. DEKBP7I FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DEKBP7I KD 2: Bacteria DEKBP7I PL 1224: Proteobacteria DEKBP7I CL 1236: Gammaproteobacteria DEKBP7I OD 91347: Enterobacterales DEKBP7I FM 702: Plesiomonas DEKBP7I GE 702: Plesiomonas DEKBP7I SP 703: Plesiomonas shigelloides DE6C3R7 ID DE6C3R7 DE6C3R7 DN Arylamine N-acetyltransferase (NAT) DE6C3R7 GN NAT DE6C3R7 SN N-hydroxyarylamine O-acetyltransferase; nhoA; DN589_02820; SAMEA1712935_00642; CI104_13255 DE6C3R7 UC A0A223JRX2_9ENTR DE6C3R7 RD Asacolitin DE6C3R7 E1 2: Transferase DE6C3R7 E2 2.3: Acyltransferase DE6C3R7 E3 2.3.1: Acyltransferase DE6C3R7 EC 2.3.1.5 DE6C3R7 SQ MTPILNAYFARLNWSGRADVNIETLRALHLQHNCTIPFENLDVLLPREMHLDDRSLEEKLITARRGGYCFEQNGVFERVLRELGFTVRSLLGRVVLANPPSLPPRTHRLLLVELDGESWIADVGFGGQTLTAPIRLQADIIQKTPHGEYRLQQEGDDWILQFCHHEHWQSMYRFDRVMQQQSDHVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTHYENDRAVEQRNLPDVASLYALLQERFGLGVTDAKHGFTETELARVMAAFDTHPEAGK DE6C3R7 TD Primarily distributed in human gut. DE6C3R7 FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DE6C3R7 KD 2: Bacteria DE6C3R7 PL 1224: Proteobacteria DE6C3R7 CL 1236: Gammaproteobacteria DE6C3R7 OD 91347: Enterobacterales DE6C3R7 FM 543: Enterobacteriaceae DE6C3R7 GE 544: Citrobacter DE6C3R7 SP 67824: Citrobacter farmeri DE8V274 ID DE8V274 DE8V274 DN Arylamine N-acetyltransferase (NAT) DE8V274 GN nhoA DE8V274 SN N-hydroxyarylamine O-acetyltransferase; nhoA; FEO47_11320; NCTC10805_02985 DE8V274 UC A0A381G6X4_CITAM DE8V274 RD Asacolitin DE8V274 E1 2: Transferase DE8V274 E2 2.3: Acyltransferase DE8V274 E3 2.3.1: Acyltransferase DE8V274 EC 2.3.1.5 DE8V274 SQ MTPILNAYFARLNWSGRAEVNIETLRALHLQHNCTIPFENLDVLLPREMHLDDRSLEEKLITARRGGYCFEQNGVFERVLRELGFTVRSLLGRVVLANPPSLPPRTHRLLLVELDGESWIADVGFGGQTLTAPIRLQADIIQKTPHGEYRLQQEGDDWILQFCHHDRWQSMYRFDRVVQQQSDYVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTHYEGDRVAEQRNLPDVASLYALLQERFGLGVTDAKHGFTETELARVMAAFDTHPEAGK DE8V274 TD Primarily distributed in human gut. DE8V274 FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DE8V274 KD 2: Bacteria DE8V274 PL 1224: Proteobacteria DE8V274 CL 1236: Gammaproteobacteria DE8V274 OD 91347: Enterobacterales DE8V274 FM 543: Enterobacteriaceae DE8V274 GE 544: Citrobacter DE8V274 SP 35703: Citrobacter amalonaticus DEAMSKV ID DEAMSKV DEAMSKV DN Alpha-glucosidase (aglA) DEAMSKV GN simA DEAMSKV SN Oligo-1,6-glucosidase; 6-phospho-alpha-glucosidase 1; LSEI_0369; simA DEAMSKV UC PAGL1_LACP3 DEAMSKV RD D-glucose DEAMSKV GI 4421568 DEAMSKV E1 3: Hydrolases DEAMSKV E2 3.2: Glycosylase DEAMSKV E3 3.2.1: O/S-glycosyl compound glycosidase DEAMSKV EC 3.2.1.20 DEAMSKV KG Metabolic pathways:lca01100; Starch and sucrose metabolism:lca00500 DEAMSKV SQ MDDRKFSVLIAGGGSTYTPGIVLTLLDHIQKFPLRKLKFYDIDGERQQRVADACEILVKERAPEVEFLATTDPEEAFTDVDFVMAQIRVGKYAMRSLDEKIPLKHGVVGQETTGPGGIAYGLRSIPGVIGLVDYMEKYSPNAWMLNYSNPAAIVAEATRRLRPHSRIINICDMPIGIMDRMAQIVGLKDRNDLVFRYYGLNHFGWWTDVRDKTGKDLMPALKQYVAKNGYWLGDKDKDTEASWVSTFKKAADVYALDPSTLPNTYLKYYLYPKYVVEHSDPNYTRTDEVEAYREKHVFDECDRIIAAGTAADTHFKSDDHATYIVDLCTAIAYDTKQRMLAIVPNDGAIENIDPEAMVEVPCLFGANGAERLAMGKAATFQKGLITEQNCVEKLTVDAFEQQSYTKLWEAMSLCKIVPDASVAKEILDEMVVANKDYWPELK DEAMSKV TD Primarily distributed in human gut. DEAMSKV FC This enzyme is probably involved in the catabolism of alpha-glycosides accumulated via a phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). And it hydrolyzes a wide variety of 6-phospho-alpha-D-glucosides including the five isomeric derivatives of sucrose, i.e. trehalulose-6'-phosphate, turanose-6'-phosphate, maltulose-6'-phosphate, leucrose-6'-phosphate, and palatinose-6'-phosphate, but is not active on sucrose-6-phosphate. Moreover, it can also hydrolyze maltose-6'-phosphate and methyl-alpha-glucose-6-phosphate, and poorly, trehalose-6-phosphate. However, it fails to hydrolyze beta-O-linked phosphorylated disaccharides such as cellobiose-6'-phosphate and gentiobiose-6'-phosphate. DEAMSKV KD 2: Bacteria DEAMSKV PL 1239: Firmicutes DEAMSKV CL 91061: Bacilli DEAMSKV OD 186826: Lactobacillales DEAMSKV FM 33958: Lactobacillaceae DEAMSKV GE 1578: Lactobacillus DEAMSKV SP 1597: Lactobacillus paracasei DEO8E75 ID DEO8E75 DEO8E75 DN VanA ligase (vanA) DEO8E75 GN vanA DEO8E75 SN Vancomycin/teicoplanin A-type resistance protein VanA; D-alanylalanine synthetase VanA; D-alanine--D-alanine ligase VanA; D-Ala-D-Ala ligase VanA; EK398_23325; vanA DEO8E75 UC A0A437UFE2_ENTAV DEO8E75 RD Vancomycin DEO8E75 E1 6: Ligase DEO8E75 E2 6.3: Carbon-nitrogen ligase DEO8E75 E3 6.3.2: Peptide synthase DEO8E75 EC 6.3.2.4 DEO8E75 SQ MNRIKVAILFGGCSEEHDVSVKSAIEIAANINKEKYEPLYIGITKSGVWKMCEKPCAEWENDNCYSAVLSPDKKMHGLLVKKNHEYEINHVDVAFSALHGKSGEDGSIQGLFELSGIPFVGCDIQSSAICMDKSLTYIVAKNAGIATPAFWVINKDDRPVAATFTYPVFVKPARSGSSFGVKKVNSADELDYAIESARQYDSKILIEQAVSGCEVGCAVLGNSAALAVGEVDQIRLQYGIFRIHQEVEPEKGSENAVITVPADLSAEERGRIQETAKKIYKALGCRGLARVDMFLQDNGRIVLNEVNTLPGFTSYSRYPRMMAAAGIALPELIDRLIVLALKG DEO8E75 TD Primarily distributed in human gut. DEO8E75 FC This enzyme is involved with UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase (EC 6.3.2.7) or UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase (EC 6.3.2.13), UDP-N-acetylmuramate---L-alanine ligase (EC 6.3.2.8), UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase (EC 6.3.2.9) and UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase (EC 6.3.2.10) in the synthesis of a cell-wall peptide. DEO8E75 KD 2: Bacteria DEO8E75 PL 1239: Firmicutes DEO8E75 CL 91061: Bacilli DEO8E75 OD 186826: Lactobacillales DEO8E75 FM 81852: Enterococcaceae DEO8E75 GE 1350: Enterococcus DEO8E75 SP 33945: Enterococcus avium DESOXHP ID DESOXHP DESOXHP DN VanA ligase (vanA) DESOXHP GN vanA DESOXHP SN Vancomycin/teicoplanin A-type resistance protein VanA; D-alanylalanine synthetase VanA; D-alanine--D-alanine ligase VanA; D-Ala-D-Ala ligase VanA; NCTC4725_01016; vanA DESOXHP UC A0A4U9YK96_ENTCA DESOXHP RD Vancomycin DESOXHP E1 6: Ligase DESOXHP E2 6.3: Carbon-nitrogen ligase DESOXHP E3 6.3.2: Peptide synthase DESOXHP EC 6.3.2.4 DESOXHP SQ MKKIAIIFGGNSPEYTVSLASATSAIEALQSSPYDYDLSLIGIAPDAMDWYLYTGELENIRQDTWLLDTKHTQKIQPLFEGNGFWISEAQQTLVPDVLFPIMHGKYGEDGSIQGLFELMKLPYVGCGVAASALCMNKWLLHQAAAAIGVQSAPTILLTNQANQQRQIEAFIQTHGFPVFFKPNEAGSSKGITKVTCVEEIAPALKEAFAYCSAVLLQKNIAGVEIGCGILGNDSLTVGACDAISLVDGFFDFEEKYQLISAKITVPAPLPETIETKVKEQAQLLYHSLGLKGLARIDFFVTDQGELYLNEINTMPGFTSHSRYPAMMAAVGLSYQELLQKLLVLAKEEGK DESOXHP TD Primarily distributed in human gut. DESOXHP FC This enzyme is involved with UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase (EC 6.3.2.7) or UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase (EC 6.3.2.13), UDP-N-acetylmuramate---L-alanine ligase (EC 6.3.2.8), UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase (EC 6.3.2.9) and UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase (EC 6.3.2.10) in the synthesis of a cell-wall peptide. DESOXHP KD 2: Bacteria DESOXHP PL 1239: Firmicutes DESOXHP CL 91061: Bacilli DESOXHP OD 186826: Lactobacillales DESOXHP FM 81852: Enterococcaceae DESOXHP GE 1350: Enterococcus DESOXHP SP 37734: Enterococcus casseliflavus DESOXHP SU Enterococcus casseliflavus BM4232 DE7XBKW ID DE7XBKW DE7XBKW DN Nitroreductase (NTR) DE7XBKW GN NTR DE7XBKW SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; CP373A1_10945 DE7XBKW UC A0A174SJF2_9CLOT DE7XBKW RD Nitrofurantoin DE7XBKW E1 1: Oxidoreductase DE7XBKW E2 1.5: CH-NH donor oxidoreductase DE7XBKW E3 1.5.1: NAD/NADP acceptor oxidoreductase DE7XBKW EC 1.5.1.39 DE7XBKW SQ MKEQHIIEVNKDICIGCGLCENDCPVNNITIKDKKSVIKNQDCIKCGHCSAICPTAAITLTGFDDEPIEIKNETTVDSNELLMAIKSRRTIRKFKNKEVHSEIIQQIIEAGRFTPSAKNSQDVSYIVLDENKSKYEEIAVKFFRRIKPIVSLFMKSAKEVTIDDNFFFKGAPVAIMVLTKDKISGSLAASNMALMAESYGLGVLYSGFFTTVVNNSRKLRKSLNLKHNDYVVTTLVLGYPDVRYRRTAQKERANVRFL DE7XBKW TD Primarily distributed in human gut. DE7XBKW FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DE7XBKW KD 2: Bacteria DE7XBKW PL 1239: Firmicutes DE7XBKW CL 186801: Clostridia DE7XBKW OD 186802: Clostridiales DE7XBKW FM 31979: Clostridiaceae DE7XBKW GE 1485: Clostridium DE7XBKW SP 29363: Clostridium paraputrificum DEH3ABM ID DEH3ABM DEH3ABM DN Nitroreductase (NTR) DEH3ABM GN DCW51_03155 DEH3ABM SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; DCW51_03155 DEH3ABM UC A0A351QTB1_CLOSP DEH3ABM RD Nitrofurantoin DEH3ABM E1 1: Oxidoreductase DEH3ABM E2 1.5: CH-NH donor oxidoreductase DEH3ABM E3 1.5.1: NAD/NADP acceptor oxidoreductase DEH3ABM EC 1.5.1.39 DEH3ABM SQ MNKEYLNDTIKLLCERASCRSFLDKKIPDELLNEIISCGLHAATGGNLQPYSIIKITDDKTKERLVNECDMQSLVKNAPVNLLFCIDWRRIQRWCEASDAPFVATKSYRHFWIALQDTIICAQNICTAADSIGLGSVYIGTVESCFMELKSIFNIPEGVFPVVLLSIGYPNQPLIPAPKLGIEAIVHEESYKDLTIDTLVKLQNEKYNSKKFPLSPTNTASMKEVTLDIGGEDYSNKIITSIEQQGYINMAQRYFGLHYKANWSCIGNKNFIEALKAYGFTWIMGEDFPTGDK DEH3ABM TD Primarily distributed in human gut. DEH3ABM FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DEH3ABM KD 2: Bacteria DEH3ABM PL 1239: Firmicutes DEH3ABM CL 186801: Clostridia DEH3ABM OD 186802: Clostridiales DEH3ABM FM 186804: Peptostreptococcaceae DEH3ABM GE 1485: Clostridium DEH3ABM SP 89152: Clostridium hiranonis DEGV7K0 ID DEGV7K0 DEGV7K0 DN Nitroreductase (NTR) DEGV7K0 GN NTR DEGV7K0 SN FMN reductase (NAD(P)H); FMN reductase NADPH; nfrA2; DW916_02940 DEGV7K0 UC A0A413TUJ8_9BACT DEGV7K0 RD Nitrazepam DEGV7K0 E1 1: Oxidoreductase DEGV7K0 E2 1.5: CH-NH donor oxidoreductase DEGV7K0 E3 1.5.1: NAD/NADP acceptor oxidoreductase DEGV7K0 EC 1.5.1.39 DEGV7K0 SQ MESIKNRTSIRKYAEKEVSEELLNRLLEEAERTPTMGNLQLYSVVVTRSEEGKKALAPAHFNQPMVTGAPVVLTICADYRRTTLWAENRKGTPGYDNILSFMNAATDALLFTQTFTNLAEEAGLGTCFLGTTVYMPKMIIDTLKLPKLVMPVATLTIGWPAEHPALSDRLPLRSIIHHEHFEDYTPEKIDDFYAEKEALEENKEFVRINNVETLAQVFTDIRYTKKDCEAMSQGFLEALKQQGFI DEGV7K0 TD Primarily distributed in human gut. DEGV7K0 FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DEGV7K0 KD 2: Bacteria DEGV7K0 PL 976: Bacteroidetes DEGV7K0 CL 200643: Bacteroidia DEGV7K0 OD 171549: Bacteroidales DEGV7K0 FM 171552: Prevotellaceae DEGV7K0 GE 838: Prevotella DEGV7K0 SP 165179: Prevotella copri DEE76YZ ID DEE76YZ DEE76YZ DN Naphthalene dioxygenase (doxB) DEE76YZ GN doxB DEE76YZ SN Naphthalene 1,2-dioxygenase ISP alpha; Naphthalene 1,2-dioxygenase subunit alpha; Naphthalene 1,2-dioxygenase system large oxygenase component; ISP NAP; ND subunit alpha; NDO subunit alpha; doxB DEE76YZ UC NDOB_PSEU8 DEE76YZ RD Isoflavone DEE76YZ E1 1: Oxidoreductase DEE76YZ E2 1.14: Oxygen paired donor oxidoreductase DEE76YZ E3 1.14.12: NADH/NADPH donor oxidoreductase DEE76YZ EC 1.14.12.12 DEE76YZ PD 2HMJ; 2HMK; 2HML; 2HMM; 2HMN; 2HMO; 4HJL; 4HKV; 4HM0; 4HM1; 4HM2; 4HM3; 4HM4; 4HM5; 4HM6 DEE76YZ SQ MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTFGPAGFWESDDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAYQAHVSSSNWAEFEHASSTWHTELTKTTDR DEE76YZ TD Primarily distributed in human gut. DEE76YZ FC This enzyme is a member of the ring-hydroxylating dioxygenase (RHD) family of bacterial enzymes that play a critical role in the degradation of aromatic compounds, such as polycyclic aromatic hydrocarbons, and it requires Fe2+. DEE76YZ KD 2: Bacteria DEE76YZ PL 1224: Proteobacteria DEE76YZ CL 1236: Gammaproteobacteria DEE76YZ OD 72274: Pseudomonadales DEE76YZ FM 135621: Pseudomonadaceae DEE76YZ GE 286: Pseudomonas DEE76YZ SP 1149133: Pseudomonas furukawaii DEL4UKY ID DEL4UKY DEL4UKY DN Methylenetetrahydrofolate dehydrogenase (folD) DEL4UKY GN folD DEL4UKY SN Methenyltetrahydrofolate cyclohydrolase; Bifunctional protein FolD; C3R19_22270; PMF13cell1_04275; folD DEL4UKY UC A0A2S4GHV2_9FIRM DEL4UKY RD ISO-901 DEL4UKY E1 1: Oxidoreductase DEL4UKY E2 1.5: CH-NH donor oxidoreductase DEL4UKY E3 1.5.1: NAD/NADP acceptor oxidoreductase DEL4UKY EC 1.5.1.5 DEL4UKY KG Carbon metabolism:bpro01200; Metabolic pathways:bpro01100; Microbial metabolism in diverse environments:bpro01120; One carbon pool by folate:bpro00670 DEL4UKY SQ MAKRLLGKEVTAALNERIKADVAALEEKGVKPTLCIIRVGENESDISYERGATKRCETLGVACEKILLPADVSQEELLATIDKVNKDDKIHGVLLFRPLPKHLNQSVIENALDPAKDVDCMTDGSMSGVFTGKNVGFPPCTPQACMEILDFYGIDCTGKKAVVVGRSLVVGKPAAMMLIKKNATVTICHTRTVDMPSVVREADIVIVAAGRAGVIDDTYLSAGQTVIDVGINVNAEGKLCGDVDFEKAEPVVDAITPVPGGVGSVTTSVLVGHVVEAAKRKFA DEL4UKY TD Primarily distributed in human gut. DEL4UKY FC This enzyme catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. DEL4UKY KD 2: Bacteria DEL4UKY PL 1239: Firmicutes DEL4UKY CL 186801: Clostridia DEL4UKY OD 186802: Clostridiales DEL4UKY FM 186803: Lachnospiraceae DEL4UKY GE 572511: Blautia DEL4UKY SP 33035: Blautia producta DEIRBUF ID DEIRBUF DEIRBUF DN L-malate:NADP(+) oxidoreductase (maeB) DEIRBUF GN maeB DEIRBUF SN L-malate:NADP oxidoreductase; NADP-dependent malic enzyme; Bacterial NADP-ME DEIRBUF UC MAO2_ECOLI DEIRBUF RD Malate DEIRBUF GI 946947 DEIRBUF E1 1: Oxidoreductase DEIRBUF E2 1.1: CH-OH donor oxidoreductase DEIRBUF E3 1.1.1: NAD/NADP oxidoreductase DEIRBUF EC 1.1.1.40 DEIRBUF KG Carbon metabolism:ecj01200; Metabolic pathways:ecj01100; Microbial metabolism in diverse environments:ecj01120; Pyruvate metabolism:ecj00620 DEIRBUF SQ MDDQLKQSALDFHEFPVPGKIQVSPTKPLATQRDLALAYSPGVAAPCLEIEKDPLKAYKYTARGNLVAVISNGTAVLGLGNIGALAGKPVMEGKGVLFKKFAGIDVFDIEVDELDPDKFIEVVAALEPTFGGINLEDIKAPECFYIEQKLRERMNIPVFHDDQHGTAIISTAAILNGLRVVEKNISDVRMVVSGAGAAAIACMNLLVALGLQKHNIVVCDSKGVIYQGREPNMAETKAAYAVVDDGKRTLDDVIEGADIFLGCSGPKVLTQEMVKKMARAPMILALANPEPEILPPLAKEVRPDAIICTGRSDYPNQVNNVLCFPFIFRGALDVGATAINEEMKLAAVRAIAELAHAEQSEVVASAYGDQDLSFGPEYIIPKPFDPRLIVKIAPAVAKAAMESGVATRPIADFDVYIDKLTEFVYKTNLFMKPIFSQARKAPKRVVLPEGEEARVLHATQELVTLGLAKPILIGRPNVIEMRIQKLGLQIKAGVDFEIVNNESDPRFKEYWTEYFQIMKRRGVTQEQAQRALISNPTVIGAIMVQRGEADAMICGTVGDYHEHFSVVKNVFGYRDGVHTAGAMNALLLPSGNTFIADTYVNDEPDAEELAEITLMAAETVRRFGIEPRVALLSHSNFGSSDCPSSSKMRQALELVRERAPELMIDGEMHGDAALVEAIRNDRMPDSSLKGSANILVMPNMEAARISYNLLRVSSSEGVTVGPVLMGVAKPVHVLTPIASVRRIVNMVALAVVEAQTQPL DEIRBUF TD Primarily distributed in human gut. DEIRBUF FC This enzyme catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP+ and divalent metal ions, and the decarboxylation of oxaloacetate. DEIRBUF KD 2: Bacteria DEIRBUF PL 1239: Firmicutes DEIRBUF CL 186801: Clostridia DEIRBUF OD 186802: Clostridiales DEIRBUF FM 2304686: Hungateiclostridiaceae DEIRBUF GE 2304692: Hungateiclostridium DEIRBUF SP 1515: Hungateiclostridium thermocellum DECXWN8 ID DECXWN8 DECXWN8 DN Kanamycin/gentamycin-resistance enzyme (aacA) DECXWN8 GN aacA DECXWN8 SN Kanamycin/gentamycin-resistance protein; Bifunctional aminoglycoside modifying enzyme AacA-AphD; aacA; aph(2'')-If; aphD DECXWN8 UC J3S7E2_CAMCO DECXWN8 RD Gentamicin DECXWN8 GI 31633730 DECXWN8 E1 2: Transferase DECXWN8 E2 2.7: Kinase DECXWN8 E3 2.7.1: Phosphotransferase DECXWN8 EC 2.7.1.190 DECXWN8 SQ MNIVENEICIRTLIDDDFPLMLKWLTDERVLEFYGGRDKKYTLESLKKHYTEPWEDEVFRVIIEYNNVPIGYGQIYKMYDELYTDYHYPKTDEIVYGMDQFIGEPNYWSKGIGTRYIKLIFEFLKKERNANAVILDPHKNNPRAIRAYQKSGFRIIEDLPEHELHEGKKEDCYLMEYRYDDNATNVKAMKYLIEHYFDNFKVDSIEIIGSGYDSVAYLVNNEYIFKTKFSTNKKKGYAKEKAIYNFLNTNLETNVKIPNIEYSYISDELSILGYKEIKGTFLTPEIYSTMSEEEQNLLKRDIASFLRQMHGLDYTDISECTIDNKQNVLEEYILLRETIYNDLTDIEKDYIESFMERLNATTVFEGKKCLCHNDFSCNHLLLDGNNRLTGIIDFGDSGIIDEYCDFIYLLEDSEEEIGTNFGEDILRMYGNIDIEKAKEYQDIVEEYYPIETIVYGIKNIKQEFIENGRKEIYKRTYKD DECXWN8 TD Primarily distributed in human gut. DECXWN8 FC This enzyme is the most clinically important aminoglycoside-modifying enzyme in Gram-positive bacteria, responsible for high-level resistance in both Enterococci and Staphylococci. And this bacterial enzyme phosphorylates many 4,6-disubstituted aminoglycoside antibiotics that have a hydroxyl group at position 2'', including kanamycin A, kanamycin B, tobramycin, dibekacin, arbekacin, amikacin, gentamicin C, sisomicin and netilmicin. DECXWN8 KD 2: Bacteria DECXWN8 PL 1224: Proteobacteria DECXWN8 CL 29547: Epsilonproteobacteria DECXWN8 OD 213849: Campylobacterales DECXWN8 FM 72294: Campylobacteraceae DECXWN8 GE 194: Campylobacter DECXWN8 SP 195: Campylobacter coli DEQUXZ5 ID DEQUXZ5 DEQUXZ5 DN Fumarate reductase flavoprotein (frdA) DEQUXZ5 GN frdA DEQUXZ5 SN Flavocytochrome c; Methylmenaquinol:fumarate reductase; Flavocytochrome c3; Fcc3; WS0831; Bacterial frdA DEQUXZ5 UC FRDA_WOLSU DEQUXZ5 RD Hydroquinone DEQUXZ5 E1 1: Oxidoreductase DEQUXZ5 E2 1.3: CH-CH donor oxidoreductase DEQUXZ5 E3 1.3.5: Quinone acceptor oxidoreductase DEQUXZ5 EC 1.3.5.4 DEQUXZ5 KG Biosynthesis of secondary metabolites:wsu01110; Butanoate metabolism:wsu00650; Carbon metabolism:wsu01200; Citrate cycle (TCA cycle):wsu00020; Metabolic pathways:wsu01100; Microbial metabolism in diverse environments:wsu01120; Oxidative phosphorylation:wsu00190; Pyruvate metabolism:wsu00620; Two-component system:wsu02020 DEQUXZ5 PD 1E7P; 1QLB; 2BS2; 2BS3; 2BS4 DEQUXZ5 SQ MKVQYCDSLVIGGGLAGLRAAVATQQKGLSTIVLSLIPVKRSHSAAAQGGMQASLGNSKMSDGDNEDLHFMDTVKGSDWGCDQKVARMFVNTAPKAIRELAAWGVPWTRIHKGDRMAIINAQKTTITEEDFRHGLIHSRDFGGTKKWRTCYTADATGHTMLFAVANECLKLGVSIQDRKEAIALIHQDGKCYGAVVRDLVTGDIIAYVAKGTLIATGGYGRIYKNTTNAVVCEGTGTAIALETGIAQLGNMEAVQFHPTPLFPSGILLTEGCRGDGGILRDVDGHRFMPDYEPEKKELASRDVVSRRMIEHIRKGKGVQSPYGQHLWLDISILGRKHIETNLRDVQEICEYFAGIDPAEKWAPVLPMQHYSMGGIRTDYRGEAKLKGLFSAGEAACWDMHGFNRLGGNSVSEAVVAGMIVGEYFAEHCANTQVDLETKTLEKFVKGQEAYMKSLVESKGTEDVFKIKNRMKDVMDDNVGIFRDGPHLEKAVKELEELYKKSKNVGIKNKRLHANPELEEAYRVPMMLKVALCVAKGALDRTESRGAHNREDYPKRDDINWLNRTLASWPNPEQTLPTLEYEALDVNEMEIAPGYRGYGAKGNYIENPLSVKRQEEIDKIQSELEAAGKDRHAIQEALMPYELPAKYKARNERLGDK DEQUXZ5 TD Primarily distributed in human gut. DEQUXZ5 FC This enzyme utilizes low potential quinols, such as menaquinol and rhodoquinol, to reduce fumarate as the final step of an anaerobic respiratory chain. The enzyme is known as complex II of the electron transfer chain, similarly to succinate dehydrogenase (quinone), to which it is closely related. DEQUXZ5 KD 2: Bacteria DEQUXZ5 PL 1224: Proteobacteria DEQUXZ5 CL 29547: Epsilonproteobacteria DEQUXZ5 OD 213849: Campylobacterales DEQUXZ5 FM 72293: Helicobacteraceae DEQUXZ5 GE 843: Wolinella DEQUXZ5 SP 844: Wolinella succinogenes DEBW1FU ID DEBW1FU DEBW1FU DN Fructokinase (scrK) DEBW1FU GN scrK DEBW1FU SN D-fructose(D-mannose)kinase; D-fructose kinase; Fructo kinase; D-fructokinase; cscK, OsFK; scrK; CL6EHI_054510 DEBW1FU UC SCRK_FUSMR DEBW1FU RD M-7403 DEBW1FU E1 2: Transferase DEBW1FU E2 2.7: Kinase DEBW1FU E3 2.7.1: Phosphotransferase DEBW1FU EC 2.7.1.4 DEBW1FU SQ MIIGAVEAGGTKFVDGVGNEKGEIFER DEBW1FU TD Primarily distributed in human gut. DEBW1FU FC This enzyme has fructokinase activity, involved metal ion binding, and cellular carbohydrate catabolic process. DEBW1FU KD 2: Bacteria DEBW1FU PL 32066: Fusobacteria DEBW1FU CL 203490: Fusobacteriia DEBW1FU OD 203491: Fusobacteriales DEBW1FU FM 203492: Fusobacteriaceae DEBW1FU GE 848: Fusobacterium DEBW1FU SP 850: Fusobacterium mortiferum DEBW1FU SU Fusobacterium mortiferum ATCC 25557; Fusobacterium mortiferum ATCC 9817 DE7HL3C ID DE7HL3C DE7HL3C DN Cytochrome P450 101D2 (cyp101) DE7HL3C GN cyp101 DE7HL3C SN Cytochrome P450 family 101 subfamily D member 2; Cytochrome P450-cam D2, Cytochrome P450cam D2; P450 101D2; cyp101D2 DE7HL3C UC Q2G8A2_NOVAD DE7HL3C RD BRN-1907611 DE7HL3C E1 1: Oxidoreductase DE7HL3C E2 1.14: Oxygen paired donor oxidoreductase DE7HL3C E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE7HL3C EC 1.14.15.1 DE7HL3C PD 3NV5; 3NV6; 4DXY DE7HL3C SQ MATNFDEAVRAKVERPANVPEDRVYEIDMYALNGIEDGYHEAWKKVQHPGIPDLIWTPFTGGHWIATNGDTVKEVYSDPTRFSSEVIFLPKEAGEKYQMVPTKMDPPEHTPYRKALDKGLNLAKIRKVEDKVREVASSLIDSFAARGECDFAAEYAELFPVHVFMALADLPLEDIPVLSEYARQMTRPEGNTPEEMATDLEAGNNGFYAYVDPIIRARVGGDGDDLITLMVNSEINGERIAHDKAQGLISLLLLGGLDTVVNFLSFFMIHLARHPELVAELRSDPLKLMRGAEEMFRRFPVVSEARMVAKDQEYKGVFLKRGDMILLPTALHGLDDAANPEPWKLDFSRRSISHSTFGGGPHRCAGMHLARMEVIVTLEEWLKRIPEFSFKEGETPIYHSGIVAAVENVPLVWPIAR DE7HL3C TD Primarily distributed in human gut. DE7HL3C FC This enzyme is a P-450 heme-thiolate protein, and it also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy-1,2-campholide. DE7HL3C KD 2: Bacteria DE7HL3C PL 1224: Proteobacteria DE7HL3C CL 28211: Alphaproteobacteria DE7HL3C OD 204457: Sphingomonadales DE7HL3C FM 41297: Sphingomonadaceae DE7HL3C GE 165696: Novosphingobium DE7HL3C SP 48935: Novosphingobium aromaticivorans DE7HL3C SU Novosphingobium aromaticivorans DSM 12444 DE9JBQK ID DE9JBQK DE9JBQK DN Cytochrome P450 101D1 (cyp101) DE9JBQK GN cyp101 DE9JBQK SN Cytochrome P450 family 101 subfamily D member 1; Cytochrome P450-cam D1, Cytochrome P450cam D1; P450 101D1; cyp101D1 DE9JBQK UC Q2GB12_NOVAD DE9JBQK RD BRN-1907611 DE9JBQK E1 1: Oxidoreductase DE9JBQK E2 1.14: Oxygen paired donor oxidoreductase DE9JBQK E3 1.14.15: Iron-sulfur protein donor oxidoreductase DE9JBQK EC 1.14.15.1 DE9JBQK PD 3LXH; 3LXI; 4C9K; 4C9L; 4C9M; 4C9N; 4C9O; 4C9P DE9JBQK SQ MNAQTSTATQKHRVAPPPHVPGHLIREIDAYDLDGLEQGFHEAWKRVQQPDTPPLVWTPFTGGHWIATRGTLIDEIYRSPERFSSRVIWVPREAGEAYDMVPTKLDPPEHTPYRKAIDKGLNLAEIRKLEDQIRTIAVEIIEGFADRGHCEFGSEFSTVFPVRVFLALAGLPVEDATKLGLLANEMTRPSGNTPEEQGRSLEAANKGFFEYVAPIIAARRGGSGTDLITRILNVEIDGKPMPDDRALGLVSLLLLGGLDTVVNFLGFMMIYLSRHPETVAEMRREPLKLQRGVEELFRRFAVVSDARYVVSDMEFHGTMLKEGDLILLPTALHGLDDRHHDDPMTVDLSRRDVTHSTFAQGPHRCAGMHLARLEVTVMLQEWLARIPEFRLKDRAVPIYHSGIVAAVENIPLEWEPQRVSA DE9JBQK TD Primarily distributed in human gut. DE9JBQK FC This enzyme is a P-450 heme-thiolate protein, and it also acts on (-)-camphor and 1,2-campholide, forming 5-exo-hydroxy-1,2-campholide. DE9JBQK KD 2: Bacteria DE9JBQK PL 1224: Proteobacteria DE9JBQK CL 28211: Alphaproteobacteria DE9JBQK OD 204457: Sphingomonadales DE9JBQK FM 41297: Sphingomonadaceae DE9JBQK GE 165696: Novosphingobium DE9JBQK SP 48935: Novosphingobium aromaticivorans DE9JBQK SU Novosphingobium aromaticivorans DSM 12444 DEGLW18 ID DEGLW18 DEGLW18 DN Cellobiose 2-epimerase (CE) DEGLW18 GN CE DEGLW18 SN Cellobiose epimerase; CS-HRCE; Caob-CE; B15CE; BfCE; CE; CE-NE1; CsCE; ERS852582_01163 DEGLW18 UC A0A173SS24_9FIRM DEGLW18 RD M-7403 DEGLW18 E1 5: Isomerase DEGLW18 E2 5.1: Racemase/epimerase DEGLW18 E3 5.1.3: Carbohydrate racemase/epimerase DEGLW18 EC 5.1.3.11 DEGLW18 SQ MSSIKQAAEEMLLQTIIPFWKGLRDEENGGFYGYMDFDLKLDKKAEKGCILNSRILWFFSEAAMLTGRADLAEDARHAYQFFLKNCYDEANGGVYWSCDYTGKPQDTTKHTYNQGFAIYALSAYYRLTKDPVALTYAKKIFHLIEQHCTDSEGYLEAFTIDWKPESNEKLSENGVMAAKTMNTLLHVFEGYAGLYQASHDPEVGKALRRILDIYEHKIYSPELHRQLVFFDQHYNSIIDLYSYGHDIESSWLIDWGCDLLGDAALSKRIHAINSDLAAHIYKEAYIDHSVVNECDRGKVNTTRVWWVQAESVLGFVNEYNKSGDAKYRDAAADIYHYICNVMVDKRPGSEWFWEVDADGKPSSRKPILEPWKCPYHNGRMCMELIRRNPDVTV DEGLW18 TD Primarily distributed in human gut. DEGLW18 FC This enzyme catalyzes the interconversion between D-glucose and D-mannose residues at the reducing end of beta-1,4-linked disaccharides by epimerizing the hydroxyl group at the C-2 position of the glucose moiety. Besides, it catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). DEGLW18 KD 2: Bacteria DEGLW18 PL 1239: Firmicutes DEGLW18 CL 186801: Clostridia DEGLW18 OD 186802: Clostridiales DEGLW18 FM 541000: Ruminococcaceae DEGLW18 GE 216851: Faecalibacterium DEGLW18 SP 853: Faecalibacterium prausnitzii DENTGJO ID DENTGJO DENTGJO DN Cellobiose 2-epimerase (CE) DENTGJO GN yihS DENTGJO SN Cellobiose epimerase; CS-HRCE; Caob-CE; B15CE; BfCE; CE; CE-NE1; CsCE; ERS852386_01186; yihS DENTGJO UC A0A173Z970_9FIRM DENTGJO RD M-7403 DENTGJO E1 5: Isomerase DENTGJO E2 5.1: Racemase/epimerase DENTGJO E3 5.1.3: Carbohydrate racemase/epimerase DENTGJO EC 5.1.3.11 DENTGJO SQ MRNEIQKELIDAIIPFWEALRDDEYGGFYGYMDYDLNLDKKAEKGCILNSRITWFFASAYKALKDPKLLDEAAHGYEFLKEYCIDREYGGIYWSMNYDGSPKDTTKHTYNQAFSIYALSAYYEASGDSEALDLALQLFHTIEEKCTDEGGYLEAFTREFKPESNDKLSENGVLAERTMNTLLHALEAYTELYKVSKDSKVKERLKWLLDVFADKVYNPELKRQEVFFDKDYNSLIDLYSYGHDIETSWLLDRATEVLGEAEYTEKITKITDILAEQIYEIAFDGHSVLTECEKGVPYTVRVWWVQAESIVGFINAYQKSGDKKYYEAAEKVWEYIKEYFIDKRPGSEWFWDLNADGTPRVGRPIVEPWKCPYHNGRMCLEIMNRLADGK DENTGJO TD Primarily distributed in human gut. DENTGJO FC This enzyme catalyzes the interconversion between D-glucose and D-mannose residues at the reducing end of beta-1,4-linked disaccharides by epimerizing the hydroxyl group at the C-2 position of the glucose moiety. Besides, it catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). DENTGJO KD 2: Bacteria DENTGJO PL 1239: Firmicutes DENTGJO CL 186801: Clostridia DENTGJO OD 186802: Clostridiales DENTGJO FM 186803: Lachnospiraceae DENTGJO GE 33042: Coprococcus DENTGJO SP 33043: Coprococcus eutactus DE4XLDR ID DE4XLDR DE4XLDR DN Cellobiose 2-epimerase (CE) DE4XLDR GN CE DE4XLDR SN Cellobiose epimerase; CS-HRCE; Caob-CE; B15CE; BfCE; CE; CE-NE1; CsCE; ERS852540_00732 DE4XLDR UC A0A174ZCD1_9FIRM DE4XLDR RD Lactose DE4XLDR E1 5: Isomerase DE4XLDR E2 5.1: Racemase/epimerase DE4XLDR E3 5.1.3: Carbohydrate racemase/epimerase DE4XLDR EC 5.1.3.11 DE4XLDR SQ MLARECKKELTEHIIPFWNSLEDNDNGGFYGYVGNDLTLDKNAPKGVILHSRILWFYSNCYLVLKDQNCLKKAKHAYEFLSKYCVDKENGGVYWMMNADGTVNDSMKHTYCQAFFIYAMSSYYDASKDKAALELALDVFATVEEKCRDDVAYLEAFSKDWNIIPNDALSENGLMADKTMNTTLHVMEAYTELYRVSGDKRVLKALRFTLEITLDKIYDKNGGKLFVFFDKNLNEIGDIYSYGHDIEATWLIDRACDVIGDEHLSKRCAEMNKVIVKNIADRALSNGRLNNEVEHGVVNTWHIWWVQAEGVVGFCNAYQRYGDARYLEISRTLWNYIKDKMIDKRPGGEWHSQLDDNDQPADFKPVVDPWKCPYHNGRMCLEIISRM DE4XLDR TD Primarily distributed in human gut. DE4XLDR FC This enzyme catalyzes the interconversion between D-glucose and D-mannose residues at the reducing end of beta-1,4-linked disaccharides by epimerizing the hydroxyl group at the C-2 position of the glucose moiety. Besides, it catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). DE4XLDR KD 2: Bacteria DE4XLDR PL 1239: Firmicutes DE4XLDR CL 186801: Clostridia DE4XLDR OD 186802: Clostridiales DE4XLDR FM 541000: Ruminococcaceae DE4XLDR GE 1730: Eubacterium DE4XLDR SP 39492: Eubacterium siraeum DEGBVKJ ID DEGBVKJ DEGBVKJ DN Cellobiose 2-epimerase (CE) DEGBVKJ GN CE DEGBVKJ SN Cellobiose epimerase; CS-HRCE; Caob-CE; B15CE; BfCE; CE; CE-NE1; CsCE; Cphy_2262 DEGBVKJ UC A9KK53_LACP7 DEGBVKJ RD Lactose DEGBVKJ E1 5: Isomerase DEGBVKJ E2 5.1: Racemase/epimerase DEGBVKJ E3 5.1.3: Carbohydrate racemase/epimerase DEGBVKJ EC 5.1.3.11 DEGBVKJ SQ MGNYKQMKELAKAHLSEVVIPFWNKLKDEENGGFYGYLDYDLQLDKKAVKGCILNSRILWFYSNAYLTLGEEGLLSYAKHAYEFLKNHCYDQTYGGIYWSLNYDGSTYDTTKHTYNQAFAVYALSSYYFATKDEEAINLAKSIIGIMEKKCTDSFGYLEAFDRDFLPIDNELLSENGVIAHKTMNTLLHVFEAYTEYYRVTGDMEIKERLMRMLDIIQIKVYNPNLHRQEVFFDVYMNSILDLHSYGHDIEAAWLIDRGLDVLKEPKYDYLLKPITKDLTNQIYQTAYQDHSLLNESEKGKVNTSRIWWVQAEAVVGFLNGYENDRNETRYYEAATDIFQFILENVHDKRTGSEWFWEVDKEGKPFNKKPIVEPWKCPYHNGRMCFEILRREI DEGBVKJ TD Primarily distributed in human gut. DEGBVKJ FC This enzyme catalyzes the interconversion between D-glucose and D-mannose residues at the reducing end of beta-1,4-linked disaccharides by epimerizing the hydroxyl group at the C-2 position of the glucose moiety. Besides, it catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man). DEGBVKJ KD 2: Bacteria DEGBVKJ PL 1239: Firmicutes DEGBVKJ CL 186801: Clostridia DEGBVKJ OD 186802: Clostridiales DEGBVKJ FM 186803: Lachnospiraceae DEGBVKJ GE 1506553: Lachnoclostridium DEGBVKJ SP 66219: Lachnoclostridium phytofermentans DEDY9F6 ID DEDY9F6 DEDY9F6 DN Cellobiose 2-epimerase (CE) DEDY9F6 GN ce13 DEDY9F6 SN Cellobiose epimerase; CS-HRCE; Caob-CE; B15CE; BfCE; CE; CE-NE1; CsCE; ce13 DEDY9F6 UC CEEP_EUBCE DEDY9F6 RD M-7403 DEDY9F6 E1 5: Isomerase DEDY9F6 E2 5.1: Racemase/epimerase DEDY9F6 E3 5.1.3: Carbohydrate racemase/epimerase DEDY9F6 EC 5.1.3.11 DEDY9F6 SQ MKNEVVYKQLTEKILPFWNAMRDDENGGFYGYMSEDLHIDDHADKGCILNSRILWFYSTAYMYLQDEKLLDNAKHAFEFLKTYCFDPMCGGIFWSVRYNGKPADTTKHTYNQAFAIYALSAYYEATGSIEAIAIAEIIYEKIEDTMRDTKGYLEAFTRDFRPADNDKLSENGVMAERTMNTLLHIIEAYSALVHALRKKVADPAKGDVRDELFMNVVENKLAAALELMRDKFYNSDRHRLDVFFDKEYESLIDLTSYGHDIEASWLLEWAAGILDDEEITESLHPISSDLVEKVYKEAFDGHSIVNECEDGDVNTDRIWWVEAESVLGFLKAFEREGKEEYRKAAHEILAFILDKQVDKREGSEWFEMLKEDGTPCHKPMVREWKCPYHNGRMCLEILKSGIEIG DEDY9F6 TD Primarily distributed in human gut. DEDY9F6 FC This enzyme catalyzes the interconversion between D-glucose and D-mannose residues at the reducing end of beta-1,4-linked disaccharides by epimerizing the hydroxyl group at the C-2 position of the glucose moiety. Besides, it catalyzes the reversible epimerization of cellobiose to 4-O-beta-D-glucopyranosyl-D-mannose (Glc-Man) and epimerizes lactose to epilactose. DEDY9F6 KD 2: Bacteria DEDY9F6 PL 1239: Firmicutes DEDY9F6 CL 186801: Clostridia DEDY9F6 OD 186802: Clostridiales DEDY9F6 FM 186806: Eubacteriaceae DEDY9F6 GE 1730: Eubacterium DEDY9F6 SP 29322: Eubacterium cellulosolvens DEDY9F6 SU Eubacterium cellulosolvens NE13 DEAGY5M ID DEAGY5M DEAGY5M DN Catalase-peroxidase (katG) DEAGY5M GN katG DEAGY5M SN Peroxidase/catalase; Catalase peroxidase; katG; CP; Synpcc7942_1656 DEAGY5M UC KATG_SYNE7 DEAGY5M RD Isoniazid DEAGY5M E1 1: Oxidoreductase DEAGY5M E2 1.11: Peroxidase DEAGY5M E3 1.11.1: Peroxidase DEAGY5M EC 1.11.1.21 DEAGY5M KG Biosynthesis of secondary metabolites:syf01110; Metabolic pathways:syf01100; Phenylalanine metabolism:syf00360; Tryptophan metabolism:syf00380 DEAGY5M PD 1UB2; 3WNU; 3WXO; 3X16; 4PAE DEAGY5M SQ MTATQGKCPVMHGGATTVNISTAEWWPKALNLDILSQHDRKTNPMGPDFNYQEEVKKLDVAALKQDLQALMTDSQDWWPADWGHYGGLMIRLTWHAAGTYRIADGRGGAGTGNQRFAPLNSWPDNTNLDKARRLLWPIKQKYGNKLSWADLIAYAGTIAYESMGLKTFGFAFGREDIWHPEKDIYWGPEKEWVPPSTNPNSRYTGDRELENPLAAVTMGLIYVNPEGVDGNPDPLKTAHDVRVTFARMAMNDEETVALTAGGHTVGKCHGNGNAALLGPEPEGADVEDQGLGWINKTQSGIGRNAVTSGLEGAWTPHPTQWDNGYFRMLLNYDWELKKSPAGAWQWEPINPREEDLPVDVEDPSIRRNLVMTDADMAMKMDPEYRKISERFYQDPAYFADVFARAWFKLTHRDMGPKARYIGPDVPQEDLIWQDPIPAGNRNYDVQAVKDRIAASGLSISELVSTAWDSARTYRNSDKRGGANGARIRLAPQKDWEGNEPDRLAKVLAVLEGIAAATGASVADVIVLAGNVGVEQAARAAGVEIVLPFAPGRGDATAEQTDTESFAVLEPIHDGYRNWLKQDYAATPEELLLDRTQLLGLTAPEMTVLIGGLRVLGTNHGGTKHGVFTDREGVLTNDFFVNLTDMNYLWKPAGKNLYEICDRKTNQVKWTATRVDLVFGSNSILRAYSELYAQDDNKEKFVRDFVAAWTKVMNADRFDLD DEAGY5M TD Primarily distributed in human lung. DEAGY5M FC This enzyme is with both catalase and broad-spectrum peroxidase activity. DEAGY5M KD 2: Bacteria DEAGY5M PL 1117: Cyanobacteria DEAGY5M CL 1890424: Synechococcales DEAGY5M OD 1890424: Synechococcales DEAGY5M FM 1890426: Synechococcaceae DEAGY5M GE 1129: Synechococcus DEAGY5M SP 32046: Synechococcus elongatus DEAGY5M SU Synechococcus elongatus PCC 7942 = FACHB-805 DE9VSLW ID DE9VSLW DE9VSLW DN Cardiac glycoside reductase 2 (cgr2) DE9VSLW GN cgr2 DE9VSLW SN Cardiac glycoside reductase operon protein 2; Cardenolide reductase; Digoxin reductase; cgr2 DE9VSLW UC CGR2_EGGLE DE9VSLW RD Digoxin DE9VSLW GI 40923314 DE9VSLW E1 1: Oxidoreductase DE9VSLW E2 1.3: CH-CH donor oxidoreductase DE9VSLW E3 1.3.2: Quinone acceptor oxidoreductase DE9VSLW EC 1.3.2.- DE9VSLW SQ MEYGKCRGIERGMGRRDFLKAATLLGATAAGAGMLAGCAPKSASEAQAQTAPAATGGLDPADVDWKYETDVVIVGSGSGGTCAAIEAAEAGADVVVFEKDKAMYGGNSALCGGYMLAAGWSTQEEITGYAGDTGEAFANQMLRWSQGLGNQDMIREACLRSGEAVDWMMDTGRTYEGASPLPPVWSCGDTEADVVPRSVYNHNAYGATEGHMATLKKRAESLSNIEIEMGCEVAHILKNAEGSVIGVQLADGSFAKARKGVVMACASVDNNLEMSKDLGLMQNVWGLTLEGAGLLAPGNPDMDSNTGDGVRMLREIGAELCMQQAVCMNDSIYVGGISDWGMSEILGKDVNIHDSSNIDAILVDKTGRRFCQDDAEWGYVMHECAQAAWKQGFTPDDPTTGYIFYVYDATGAPFFEMKGHTPDTCDTTFSADSVDGLAEFIGCDPTALASEVERWNSFCEAGLDADFGRRANMAPIATPPFYCDVVRPGPMGTFAGAKSNVEAEIIGLDGNPIPRLYGAGCIIGGNVSGAFYFGCGWSITNTVVWGREAGRNVAALEPWE DE9VSLW TD Primarily distributed in human gut. DE9VSLW FC This enzyme serves as the terminal electron reductase partner to Cardiac glycoside reductase 1 (Cgr1) by forming an complex with Cgr1 and receiving electrons from Cgr1 at the active site FAD redox cofactor. DE9VSLW KD 2: Bacteria DE9VSLW PL 201174: Actinobacteria DE9VSLW CL 84998: Coriobacteriia DE9VSLW OD 1643822: Eggerthellales DE9VSLW FM 1643826: Eggerthellaceae DE9VSLW GE 84111: Eggerthella DE9VSLW SP 84112: Eggerthella lenta DE84PFW ID DE84PFW DE84PFW DN Cardiac glycoside reductase 1 (cgr1) DE84PFW GN cgr1 DE84PFW SN Cardiac glycoside reductase operon protein 1; Cytochrome c-type protein Cgr1; cgr1 DE84PFW UC CGR1_EGGLE DE84PFW RD Digoxin DE84PFW GI 40923313 DE84PFW E1 1: Oxidoreductase DE84PFW E2 1.3: CH-CH donor oxidoreductase DE84PFW E3 1.3.2: Quinone acceptor oxidoreductase DE84PFW EC 1.3.2.- DE84PFW SQ MAEEPVVIGDPAPRTRKWPIVVGVVVVVLIAAGAGFWVWHEQPSFCAAICHTPMDEYLETYEQEAGTAGVDKWGNEVANTNAMLAVSHKAQGKDCMACHVPTLSEQMSEGMNWVTGNYVYPLEERDTEMLTEARGVDADEFCLNESCHNLTRDDLIKATSDMEFNPHQPQHGEIECSECHKAHRASVMYCTQCHSEAEVPEGWLTVAEANKLSTAA DE84PFW TD Primarily distributed in human gut. DE84PFW FC This enzyme anchors as a dimer in the cytoplasmic membrane and shuttles quinone derived electrons to associated periplasmic nitrite reductases. DE84PFW KD 2: Bacteria DE84PFW PL 201174: Actinobacteria DE84PFW CL 84998: Coriobacteriia DE84PFW OD 1643822: Eggerthellales DE84PFW FM 1643826: Eggerthellaceae DE84PFW GE 84111: Eggerthella DE84PFW SP 84112: Eggerthella lenta DEUX61H ID DEUX61H DEUX61H DN Biphenyl dioxygenase (bphC) DEUX61H GN bphC DEUX61H SN Biphenyl-2,3-diol 1,2-dioxygenase; 2,3-dihydroxybiphenyl dioxygenase; 23OHBP oxygenase; DHBD; bphC DEUX61H UC BPHC_PSEFK DEUX61H RD Isoflavone DEUX61H E1 1: Oxidoreductase DEUX61H E2 1.13: Oxygen single donor oxidoreductase DEUX61H E3 1.13.11: Oxygen single donor oxidoreductase DEUX61H EC 1.13.11.39 DEUX61H SQ MSIRSLGYMGFAVSDVAAWRSFLTQKLGLMEAGTTDNGDLFRIDSRAWRIAVQQGEVDDLAFAGYEVADAAGLAQMADKLKQAGIAVTTGDASLARRRGVTGLITFADPFGLPLEIYYGASEVFEKPFLPGAAVSGFLTGEQGLGHFVRCVPDSDKALAFYTDVLGFQLSDVIDMKMGPDVTVPVYFLHCNERHHTLAIAAFPLPKRIHHFMLEVASLDDVGFAFDRVDADGLITSTLGRHTNDHMVSFYASTPSGVEVEYGWSARTVDRSWVVVRHDSPSMWGHKSVRDKALRATKHEQQPE DEUX61H TD Primarily distributed in human gut. DEUX61H FC This enzyme participates in the degradation pathway of biphenyl and PCB (poly chlorinated biphenyls) and contains Fe2+ or Mn2+ . DEUX61H KD 2: Bacteria DEUX61H PL 1224: Proteobacteria DEUX61H CL 1236: Gammaproteobacteria DEUX61H OD 72274: Pseudomonadales DEUX61H FM 135621: Pseudomonadaceae DEUX61H GE 286: Pseudomonas DEUX61H SP 1149133: Pseudomonas furukawaii DEUX61H SU Pseudomonas furukawaii KF707 DED0TBR ID DED0TBR DED0TBR DN Beta-lactamase (blaB) DED0TBR GN cfxA DED0TBR SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA; DW701_17160 DED0TBR UC A0A414M273_9BACE DED0TBR RD Amoxicillin DED0TBR E1 3: Hydrolases DED0TBR E2 3.5: Carbon-nitrogen hydrolase DED0TBR E3 3.5.2: Cyclic amide hydrolase DED0TBR EC 3.5.2.6 DED0TBR SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADYNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DED0TBR TD Primarily distributed in human gut. DED0TBR FC This enzyme hydrolyzes beta-lactam. DED0TBR KD 2: Bacteria DED0TBR PL 976: Bacteroidetes DED0TBR CL 200643: Bacteroidia DED0TBR OD 171549: Bacteroidales DED0TBR FM 815: Bacteroidaceae DED0TBR GE 816: Bacteroides DED0TBR SP 28111: Bacteroides eggerthii DEX8KJO ID DEX8KJO DEX8KJO DN Beta-lactamase (blaB) DEX8KJO GN blaB DEX8KJO SN Penicillinase; Cephalosporinase; Beta-lactam; BACCAP_02761 DEX8KJO UC A6NX15_9FIRM DEX8KJO RD Amoxicillin DEX8KJO E1 3: Hydrolases DEX8KJO E2 3.5: Carbon-nitrogen hydrolase DEX8KJO E3 3.5.2: Cyclic amide hydrolase DEX8KJO EC 3.5.2.6 DEX8KJO SQ MYTHSAGGKFLILFSFDSTAGRWDNFFEAQGKSRERMNAAMWKKRLSALALTAVMAVSISAPALAAETEAPATRDESAAMAAQYAAQYGGAVSVQYAVWQDGEITVSGHAGVYSKSENRVLLDTDLYGIGSVSKMYVTAAVMQLVEQGKINLDAPVTKYLPEFKMADERYKDITVRMLLNHSSGLMSATHNMLLFADDDRSATENLLETLSTQRLAADPGAYSTYCNTGFTLAELVVEAVSGKTFPEYLHEAILAPNSLENTFTPQDEFDTSRLVKTYLGEDPRALPQDCLGTVGTGGIYANAADLAAFGGLLCSDELLTSASLDAMAAPEYSNGIWPDDADDSLAFGLGWDTVSLAPFGYNDIQALAKGGDTQYYHAALVVLPEYDMAAAVLTSGGVSTYNQMAASRMLIDALAEQGVAVDETVPTLPAATPSQTMPAELMDYSGYYASTLQQFKVDISADGVLTLQSLTVPSAPAQTFYYFDDGSFRDQTGTAAMVKPVVEKNGQTYLWQKAYAFLLGLTVLPTSNYVGQKVEPAQLTEDVQAAWDKWNTTSVLPLNEKYSSQVWLSLGSAAVTELPEYIPGYVGAQKIVDANHTQFAVQVPGNAGRDGSDVTVWEEDGHVWMSAQGLLYADASIAQPIYCGAGAYSTVQPDGYARWYTVGSAAGLTIQVEIEGNGGFYVYDGTGSLAASSVVWGDSTVTLPENGVIAFAGDAGARFHISVVSAE DEX8KJO TD Primarily distributed in human gut. DEX8KJO FC This enzyme hydrolyzes beta-lactam. DEX8KJO KD 2: Bacteria DEX8KJO PL 1239: Firmicutes DEX8KJO CL 186801: Clostridia DEX8KJO OD 186802: Clostridiales DEX8KJO FM 541000: Ruminococcaceae DEX8KJO GE 1017280: Pseudoflavonifractor DEX8KJO SP 106588: Pseudoflavonifractor capillosus DEAYSTX ID DEAYSTX DEAYSTX DN Beta-lactamase (blaB) DEAYSTX GN blaB DEAYSTX SN Penicillinase; Cephalosporinase; Beta-lactam; ACDG_00016 DEAYSTX UC C0W968_9FIRM DEAYSTX RD Cefotaxime DEAYSTX E1 3: Hydrolases DEAYSTX E2 3.5: Carbon-nitrogen hydrolase DEAYSTX E3 3.5.2: Cyclic amide hydrolase DEAYSTX EC 3.5.2.6 DEAYSTX SQ MKKFCFLFLIICGLMVFCLQDCQARQKLNLADLENKYNAVIGVYAVDMENGKKICYKPDTRFSYCSTHKVFTAAELLRQKNTSDLNEIRKFSAEDILSYAPITKDHVADGMTLAEICSASLRWSDNTAANLILQEIGGVENFKVALKNIGDKTTKPARNEPELNLFNPKDNRDTSTPRQMVKNLQVYIFGDILSDDKKKLLIDWMSDNSITDTLIKAETPQGWKVIDKSGSGDYGARNDIAVIYPPNRKPIVMAIMSRRTEKNAKSDDAMIAEAAKRIFDNLVF DEAYSTX TD Primarily distributed in human gut. DEAYSTX FC This enzyme hydrolyzes beta-lactam. DEAYSTX KD 2: Bacteria DEAYSTX PL 1239: Firmicutes DEAYSTX CL 909932: Negativicutes DEAYSTX OD 1843488: Acidaminococcales DEAYSTX FM 909930: Acidaminococcaceae DEAYSTX GE 904: Acidaminococcus DEAYSTX SP 187327: Acidaminococcus intestini DERGEVU ID DERGEVU DERGEVU DN Beta-lactamase (blaB) DERGEVU GN blaB DERGEVU SN Penicillinase; Cephalosporinase; Beta-lactam; Metallo-beta-lactamase domain protein; FMAG_01052 DERGEVU UC C3WC84_FUSMR DERGEVU RD Ticarcillin DERGEVU E1 3: Hydrolases DERGEVU E2 3.5: Carbon-nitrogen hydrolase DERGEVU E3 3.5.2: Cyclic amide hydrolase DERGEVU EC 3.5.2.6 DERGEVU SQ MYFCTEIANGVTWIGVNDRKTERFENYIPLPYGVTYNSYFIDDEKTCVIDAVELGSASTFLDKIVECLDGRKLDYIVINHVEPDHSSGLKEVIRTFPTVKIVGNAKTLGMLQAFSPDFPVENFVTIKEGDILELGNHKLTFAMIPMVHWPESMVTYDLTDKILFSNDAFGSFGALDGGIFDDQVNFEFYQSEMRRYYSNIVGKYGPQVLNAIKKLGGLEIKFICPSHGLIWRKDIAKVVSLYETWAKLEPETEGVVIVYGSMYGNTAKMAEIIGRKLNCCGIKEVKIYDASKTDLSFIISEIWKYKGLIIGSCAHNNSVYPKIQPLLHKLENYGLKNRYVGIFGSMMWSGGGVRGIQCFADALKGVEVVGEAVEVKGTPKAEDVTRLEAIAEEMAAKLIAERI DERGEVU TD Primarily distributed in human gut. DERGEVU FC This enzyme hydrolyzes beta-lactam. DERGEVU KD 2: Bacteria DERGEVU PL 32066: Fusobacteria DERGEVU CL 203490: Fusobacteriia DERGEVU OD 203491: Fusobacteriales DERGEVU FM 203492: Fusobacteriaceae DERGEVU GE 848: Fusobacterium DERGEVU SP 850: Fusobacterium mortiferum DEQMISO ID DEQMISO DEQMISO DN Beta-lactamase (blaB) DEQMISO GN blaB DEQMISO SN Penicillinase; Cephalosporinase; Beta-lactam; Odosp_1620 DEQMISO UC F9Z530_ODOSD DEQMISO RD Ticarcillin DEQMISO GI 41366452 DEQMISO E1 3: Hydrolases DEQMISO E2 3.5: Carbon-nitrogen hydrolase DEQMISO E3 3.5.2: Cyclic amide hydrolase DEQMISO EC 3.5.2.6 DEQMISO SQ MKSRKWKKISALLFLGIALLFLLMPTYMQEALIHWFPDISDTYIFPSDTVGKADSCWEWPVARDANRYRMTDDEEAYLEKYGTVAYLVIQDDSIRYEEYREDWTPQKLSNIFSATKSIVGLLVGIAYDEGFIESLDDKVSKYLPEFGEGDKITIRNLLTMSSGLDWDEAYTALISKTTQAYYGDRIRDLIMDLKVVEEPGKKYSYKSGDTQLLSFVLEAALDKVHKEKEYEWGIFKTEVKVHSPVSISEYAERKLWKPLGACNDALWNLDREDGDEKTYCCFNTTARDLARLGRLILNKGNWNGRQLISETYLNEAITPAGYLENEFGDGSLDYYGFQIWIMHYKEMRFPAFRGLGGQYMFVIPQKNAIVIRLGHKRSDEYIREKTIDMDAYLDIAFKILE DEQMISO TD Primarily distributed in human gut. DEQMISO FC This enzyme hydrolyzes beta-lactam. DEQMISO KD 2: Bacteria DEQMISO PL 976: Bacteroidetes DEQMISO CL 200643: Bacteroidia DEQMISO OD 171549: Bacteroidales DEQMISO FM 1853231: Odoribacteraceae DEQMISO GE 283168: Odoribacter DEQMISO SP 28118: Odoribacter splanchnicus DEHFJ4G ID DEHFJ4G DEHFJ4G DN Beta-lactamase (blaB) DEHFJ4G GN cfxa2 DEHFJ4G SN Penicillinase; Cephalosporinase; Beta-lactam; cfxa2 DEHFJ4G UC Q8KT51_9BACT DEHFJ4G RD Ticarcillin DEHFJ4G E1 3: Hydrolases DEHFJ4G E2 3.5: Carbon-nitrogen hydrolase DEHFJ4G E3 3.5.2: Cyclic amide hydrolase DEHFJ4G EC 3.5.2.6 DEHFJ4G SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKANNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLVTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEHFJ4G TD Primarily distributed in human gut. DEHFJ4G FC This enzyme hydrolyzes beta-lactam. DEHFJ4G KD 2: Bacteria DEHFJ4G PL 976: Bacteroidetes DEHFJ4G CL 200643: Bacteroidia DEHFJ4G OD 171549: Bacteroidales DEHFJ4G FM 171552: Prevotellaceae DEHFJ4G GE 838: Prevotella DEHFJ4G SP 28134: Prevotella oralis DEHPJRC ID DEHPJRC DEHPJRC DN Beta-lactamase (blaB) DEHPJRC GN cfxa2 DEHPJRC SN Penicillinase; Cephalosporinase; Beta-lactam; cfxa2 DEHPJRC UC Q8KT60_9BACT DEHPJRC RD Amoxicillin DEHPJRC E1 3: Hydrolases DEHPJRC E2 3.5: Carbon-nitrogen hydrolase DEHPJRC E3 3.5.2: Cyclic amide hydrolase DEHPJRC EC 3.5.2.6 DEHPJRC SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTKEEMSADHNKAYSNYTSPLGAAMLMNRWFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEHPJRC TD Primarily distributed in human gut. DEHPJRC FC This enzyme hydrolyzes beta-lactam. DEHPJRC KD 2: Bacteria DEHPJRC PL 976: Bacteroidetes DEHPJRC CL 200643: Bacteroidia DEHPJRC OD 171549: Bacteroidales DEHPJRC FM 171552: Prevotellaceae DEHPJRC GE 838: Prevotella DEHPJRC SP 28125: Prevotella bivia DEITMS0 ID DEITMS0 DEITMS0 DN Beta-lactamase (blaB) DEITMS0 GN aci1 DEITMS0 SN Penicillinase; Cephalosporinase; Beta-lactam; aci1 DEITMS0 UC Q9XBM2_ACIFE DEITMS0 RD Cefotaxime DEITMS0 E1 3: Hydrolases DEITMS0 E2 3.5: Carbon-nitrogen hydrolase DEITMS0 E3 3.5.2: Cyclic amide hydrolase DEITMS0 EC 3.5.2.6 DEITMS0 SQ MKKFCFLFLIICGLMVFCLQDCQARQKLNLADLENKYNAVIGVYAVDMENGKKICYKPDTRFSYCSTHKVFTAAELLRQKNTSDLNEIRKFSAEDILSYAPITKDHVADGMTLAEICSASLRWSDNTAANLILQEIGGVENFKVALKNIGDKTTKPARNEPELNLFNPKDNRDTSTPRQMVKNLQVYIFGDILSDDKKKLLIDWMSDNSITDTLIKAETPQGWKVIDKSGSGDYGARNDIAVIYPPNRKPIVMAIMSRRTEKNAKSDDAMIAEAAKRIFDNLVF DEITMS0 TD Primarily distributed in human skin. DEITMS0 FC This enzyme hydrolyzes beta-lactam. DEITMS0 KD 2: Bacteria DEITMS0 PL 1239: Firmicutes DEITMS0 CL 909932: Negativicutes DEITMS0 OD 1843488: Acidaminococcales DEITMS0 FM 909930: Acidaminococcaceae DEITMS0 GE 904: Acidaminococcus DEITMS0 SP 905: Acidaminococcus fermentans DE5HV8P ID DE5HV8P DE5HV8P DN Beta-lactamase (blaB) DE5HV8P GN cfxA DE5HV8P SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA; EAJ00_22575 DE5HV8P UC A0A4Q5I6I2_9BACE DE5HV8P RD Cefoxitin DE5HV8P E1 3: Hydrolases DE5HV8P E2 3.5: Carbon-nitrogen hydrolase DE5HV8P E3 3.5.2: Cyclic amide hydrolase DE5HV8P EC 3.5.2.6 DE5HV8P SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATFIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DE5HV8P TD Primarily distributed in human gut. DE5HV8P FC This enzyme hydrolyzes beta-lactam. DE5HV8P KD 2: Bacteria DE5HV8P PL 976: Bacteroidetes DE5HV8P CL 200643: Bacteroidia DE5HV8P OD 171549: Bacteroidales DE5HV8P FM 815: Bacteroidaceae DE5HV8P GE 816: Bacteroides DE5HV8P SP 47678: Bacteroides caccae DE47ARF ID DE47ARF DE47ARF DN Beta-lactamase (blaB) DE47ARF GN cfxA DE47ARF SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA DE47ARF UC B5WXV2_9BACT DE47ARF RD Cefotaxime DE47ARF E1 3: Hydrolases DE47ARF E2 3.5: Carbon-nitrogen hydrolase DE47ARF E3 3.5.2: Cyclic amide hydrolase DE47ARF EC 3.5.2.6 DE47ARF SQ LVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGCVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DE47ARF TD Primarily distributed in human gut. DE47ARF FC This enzyme hydrolyzes beta-lactam. DE47ARF KD 2: Bacteria DE47ARF PL 976: Bacteroidetes DE47ARF CL 200643: Bacteroidia DE47ARF OD 171549: Bacteroidales DE47ARF FM 2005525: Tannerellaceae DE47ARF GE 375288: Parabacteroides DE47ARF SP 823: Parabacteroides distasonis DEG2PK9 ID DEG2PK9 DEG2PK9 DN Beta-lactamase (blaB) DEG2PK9 GN cfxA DEG2PK9 SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA DEG2PK9 UC B5WXV3_BACOV DEG2PK9 RD Cefotaxime DEG2PK9 E1 3: Hydrolases DEG2PK9 E2 3.5: Carbon-nitrogen hydrolase DEG2PK9 E3 3.5.2: Cyclic amide hydrolase DEG2PK9 EC 3.5.2.6 DEG2PK9 SQ LVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEG2PK9 TD Primarily distributed in human gut. DEG2PK9 FC This enzyme hydrolyzes beta-lactam. DEG2PK9 KD 2: Bacteria DEG2PK9 PL 976: Bacteroidetes DEG2PK9 CL 200643: Bacteroidia DEG2PK9 OD 171549: Bacteroidales DEG2PK9 FM 815: Bacteroidaceae DEG2PK9 GE 816: Bacteroides DEG2PK9 SP 28116: Bacteroides ovatus DEWHJ7A ID DEWHJ7A DEWHJ7A DN Beta-lactamase (blaB) DEWHJ7A GN cfxA DEWHJ7A SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA DEWHJ7A UC B5WXV7_BACT4 DEWHJ7A RD Cefotaxime DEWHJ7A E1 3: Hydrolases DEWHJ7A E2 3.5: Carbon-nitrogen hydrolase DEWHJ7A E3 3.5.2: Cyclic amide hydrolase DEWHJ7A EC 3.5.2.6 DEWHJ7A SQ LVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPCEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEWHJ7A TD Primarily distributed in human gut. DEWHJ7A FC This enzyme hydrolyzes beta-lactam. DEWHJ7A KD 2: Bacteria DEWHJ7A PL 976: Bacteroidetes DEWHJ7A CL 200643: Bacteroidia DEWHJ7A OD 171549: Bacteroidales DEWHJ7A FM 815: Bacteroidaceae DEWHJ7A GE 816: Bacteroides DEWHJ7A SP 818: Bacteroides thetaiotaomicron DEU1RXB ID DEU1RXB DEU1RXB DN Beta-lactamase (blaB) DEU1RXB GN cfxA DEU1RXB SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA DEU1RXB UC BLAC_BACVU DEU1RXB RD Cefoxitin DEU1RXB E1 3: Hydrolases DEU1RXB E2 3.5: Carbon-nitrogen hydrolase DEU1RXB E3 3.5.2: Cyclic amide hydrolase DEU1RXB EC 3.5.2.6 DEU1RXB SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNKSQASQYVAHISAVVYSLLMQTSVKS DEU1RXB TD Primarily distributed in human gut. DEU1RXB FC This enzyme hydrolyze cephalosporins, penicillins and also cefoxitin; but at a slow rate. DEU1RXB KD 2: Bacteria DEU1RXB PL 976: Bacteroidetes DEU1RXB CL 200643: Bacteroidia DEU1RXB OD 171549: Bacteroidales DEU1RXB FM 815: Bacteroidaceae DEU1RXB GE 816: Bacteroides DEU1RXB SP 821: Bacteroides vulgatus DETDS7E ID DETDS7E DETDS7E DN Beta-lactamase (blaB) DETDS7E GN cfxA DETDS7E SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA; C4H12_08600; C4H12_11260; C4H12_12255 DETDS7E UC A0A2S0LB67_9FLAO DETDS7E RD Amoxicillin DETDS7E E1 3: Hydrolases DETDS7E E2 3.5: Carbon-nitrogen hydrolase DETDS7E E3 3.5.2: Cyclic amide hydrolase DETDS7E EC 3.5.2.6 DETDS7E SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DETDS7E TD Primarily distributed in human oral cavity. DETDS7E FC This enzyme hydrolyzes beta-lactam. DETDS7E KD 2: Bacteria DETDS7E PL 976: Bacteroidetes DETDS7E CL 117743: Flavobacteriia DETDS7E OD 200644: Flavobacteriales DETDS7E FM 49546: Flavobacteriaceae DETDS7E GE 1016: Capnocytophaga DETDS7E SP 45243: Capnocytophaga haemolytica DE37FJH ID DE37FJH DE37FJH DN Beta-lactamase (blaB) DE37FJH GN blaB DE37FJH SN Penicillinase; Cephalosporinase; Beta-lactam; Sel1 repeat protein; FVAG_01242 DE37FJH UC C6JIU1_FUSVA DE37FJH RD Ticarcillin DE37FJH E1 3: Hydrolases DE37FJH E2 3.5: Carbon-nitrogen hydrolase DE37FJH E3 3.5.2: Cyclic amide hydrolase DE37FJH EC 3.5.2.6 DE37FJH SQ MKGKNKINVIIYVIILLFSLGNLVFAEDSTEEQVKQGNSYYENGKYDLAEKYWKMAADKGNVDALYALGILYEDADKLDLAEAYYKLAADKGDADAQYNLGVLYDDQKKYDLAEAYYKKAAAQGDVDAQYNLGCLYDTQKNFTEAEKYYKLAADQGDKGAQYNLGCLYDTQKKFALAEQFYRLAANQGDIDAQYNIGILYKNQKKFVLAEKYWKMAADQGDLEAQNNLGILYEEQKKYDLAEIYYKKAADGGLKDAQYNLGLFYSDRGKKDLSKKYSELAENNK DE37FJH TD Primarily distributed in human gut. DE37FJH FC This enzyme hydrolyzes beta-lactam. DE37FJH KD 2: Bacteria DE37FJH PL 32066: Fusobacteria DE37FJH CL 203490: Fusobacteriia DE37FJH OD 203491: Fusobacteriales DE37FJH FM 203492: Fusobacteriaceae DE37FJH GE 848: Fusobacterium DE37FJH SP 856: Fusobacterium varium DEC7JEF ID DEC7JEF DEC7JEF DN Beta-lactamase (blaB) DEC7JEF GN HMPREF3277_11020 DEC7JEF SN Penicillinase; Cephalosporinase; Beta-lactam; HMPREF3277_11020 DEC7JEF UC A0A1S1G219_9NEIS DEC7JEF RD Ampicillin DEC7JEF E1 3: Hydrolases DEC7JEF E2 3.5: Carbon-nitrogen hydrolase DEC7JEF E3 3.5.2: Cyclic amide hydrolase DEC7JEF EC 3.5.2.6 DEC7JEF SQ MKPAQTSLLFALLLGLLPAAYAEDYDDEAYQNLITQCTRNQLDSCVTLGIWTRDYLESPADAYLPLKKACDGKNMKGCNVLANLYLDPYSGLGMDYSKALELYRKACKGGYDNACRNAKETEQEMRSQTAEDRAVKRQERLEALQRSCMGENDAACRALQRELQR DEC7JEF TD Primarily distributed in human oral cavity. DEC7JEF FC This enzyme hydrolyzes 6-aminopenicillinic acid and 7-aminocephalosporanic acid (ACA) derivatives. DEC7JEF KD 2: Bacteria DEC7JEF PL 1224: Proteobacteria DEC7JEF CL 28216: Betaproteobacteria DEC7JEF OD 206351: Neisseriales DEC7JEF FM 481: Neisseriaceae DEC7JEF GE 482: Neisseria DEC7JEF SP 490: Neisseria sicca DEP7MN1 ID DEP7MN1 DEP7MN1 DN Beta-lactamase (blaB) DEP7MN1 GN cfxA2 DEP7MN1 SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA2; CLI70_02470; CTI18_10205; CTM44_04660; CTM46_08920; CTM50_00090; CTM59_09130; CTM61_11025; CTM62_10610; CUB95_12895; CUB97_12180 DEP7MN1 UC Q9X4S7_PREIN DEP7MN1 RD Amoxicillin DEP7MN1 E1 3: Hydrolases DEP7MN1 E2 3.5: Carbon-nitrogen hydrolase DEP7MN1 E3 3.5.2: Cyclic amide hydrolase DEP7MN1 EC 3.5.2.6 DEP7MN1 SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEP7MN1 TD Primarily distributed in human gut. DEP7MN1 FC This enzyme hydrolyzes beta-lactam. DEP7MN1 KD 2: Bacteria DEP7MN1 PL 976: Bacteroidetes DEP7MN1 CL 200643: Bacteroidia DEP7MN1 OD 171549: Bacteroidales DEP7MN1 FM 171552: Prevotellaceae DEP7MN1 GE 838: Prevotella DEP7MN1 SP 28131: Prevotella intermedia DEAILCM ID DEAILCM DEAILCM DN Beta-lactamase (blaB) DEAILCM GN blaB DEAILCM SN Penicillinase; Cephalosporinase; Beta-lactam; CBG57_09675 DEAILCM UC A0A246EJV2_9BACT DEAILCM RD Penicillin G DEAILCM E1 3: Hydrolases DEAILCM E2 3.5: Carbon-nitrogen hydrolase DEAILCM E3 3.5.2: Cyclic amide hydrolase DEAILCM EC 3.5.2.6 DEAILCM SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEAILCM TD Primarily distributed in human gut. DEAILCM FC This enzyme hydrolyzes beta-lactam. DEAILCM KD 2: Bacteria DEAILCM PL 976: Bacteroidetes DEAILCM CL 200643: Bacteroidia DEAILCM OD 171549: Bacteroidales DEAILCM FM 171552: Prevotellaceae DEAILCM GE 838: Prevotella DEAILCM SP 28133: Prevotella nigrescens DET4XFN ID DET4XFN DET4XFN DN Beta-lactamase (blaB) DET4XFN GN cfxa2 DET4XFN SN Penicillinase; Cephalosporinase; Beta-lactam; cfxa2 DET4XFN UC Q8KT59_9BACT DET4XFN RD Amoxicillin DET4XFN E1 3: Hydrolases DET4XFN E2 3.5: Carbon-nitrogen hydrolase DET4XFN E3 3.5.2: Cyclic amide hydrolase DET4XFN EC 3.5.2.6 DET4XFN SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKGSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFVATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DET4XFN TD Primarily distributed in human oral cavity. DET4XFN FC This enzyme hydrolyzes beta-lactam. DET4XFN KD 2: Bacteria DET4XFN PL 976: Bacteroidetes DET4XFN CL 200643: Bacteroidia DET4XFN OD 171549: Bacteroidales DET4XFN FM 171552: Prevotellaceae DET4XFN GE 838: Prevotella DET4XFN SP 28126: Prevotella buccae DEE8742 ID DEE8742 DEE8742 DN Beta-lactamase (blaB) DEE8742 GN bla DEE8742 SN Penicillinase; Cephalosporinase; Beta-lactam; bla TEM-17 DEE8742 UC O32372_CAPOC DEE8742 RD Amoxicillin DEE8742 E1 3: Hydrolases DEE8742 E2 3.5: Carbon-nitrogen hydrolase DEE8742 E3 3.5.2: Cyclic amide hydrolase DEE8742 EC 3.5.2.6 DEE8742 SQ MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVKYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW DEE8742 TD Primarily distributed in human oral cavity. DEE8742 FC This enzyme hydrolyzes beta-lactam. DEE8742 KD 2: Bacteria DEE8742 PL 976: Bacteroidetes DEE8742 CL 117743: Flavobacteriia DEE8742 OD 200644: Flavobacteriales DEE8742 FM 49546: Flavobacteriaceae DEE8742 GE 1016: Capnocytophaga DEE8742 SP 1018: Capnocytophaga ochracea DEY09SU ID DEY09SU DEY09SU DN Beta-lactamase (blaB) DEY09SU GN blaB DEY09SU SN Penicillinase; Cephalosporinase; Beta-lactam; HMPREF0973_01058 DEY09SU UC C9MN73_9BACT DEY09SU RD Amoxicillin DEY09SU E1 3: Hydrolases DEY09SU E2 3.5: Carbon-nitrogen hydrolase DEY09SU E3 3.5.2: Cyclic amide hydrolase DEY09SU EC 3.5.2.6 DEY09SU SQ MIHRSYTLFLIATILLFTSCSVFRGFSLDGFSGPDIYEYQKLERDTIRKGSNVFHFPLVESHRKIRGDFRLKYKDSGRMRLDSLVEQWFGKDNQLLIIHNDSVVYDQWTEPFYPGKNATVFSVSKSLTALLCGIAIDEGYIKSVDDPVTDYIPELAQYNPTFRSLRIIHLLNMQAGFDFKEHYEFTLKSMSSIAKMAQLQYGHDFTRLFRHVKFKYQPGEKYEYNSLTTALLSWIIERATGKNYAHYMSEKVWKPLGMEHDAWVTIDSRKHHHAQGFGGIATNVYDLAKIGRLYLNRGKWEGKQIVREEWINRSLETTSENKGYHYCWYYQYYDDKTDNSSFYAFGVGHQFIYINQKKNVIITRIGNNYNWKWWEMSFFDALCNKLF DEY09SU TD Primarily distributed in human oral cavity. DEY09SU FC This enzyme hydrolyzes beta-lactam. DEY09SU KD 2: Bacteria DEY09SU PL 976: Bacteroidetes DEY09SU CL 200643: Bacteroidia DEY09SU OD 171549: Bacteroidales DEY09SU FM 171552: Prevotellaceae DEY09SU GE 838: Prevotella DEY09SU SP 28137: Prevotella veroralis DEQLVCA ID DEQLVCA DEQLVCA DN Beta-lactamase (blaB) DEQLVCA GN blaB DEQLVCA SN Penicillinase; Cephalosporinase; Beta-lactam; Metallo-beta-lactamase domain protein; GCWU000325_00085 DEQLVCA UC C9LD75_9BACT DEQLVCA RD Amoxicillin DEQLVCA E1 3: Hydrolases DEQLVCA E2 3.5: Carbon-nitrogen hydrolase DEQLVCA E3 3.5.2: Cyclic amide hydrolase DEQLVCA EC 3.5.2.6 DEQLVCA SQ MLKIKRFIFNMVQENCYVLHDETQEGVIIDCGALMPEEEEALRDYIAAEGIQVKHLLHTHSHFDHVFGDQFVYSTYGIKPEMHELEVALYGDVSGQVAMFLHRNISVVVPPLGNVFTGRDEIKFGNHTLEIIETPGHSPGGVCFYCRAEKALFSGDSLFKHEIGRFDFPYGDGAALIDNLKTKILTLPADVNVYPGHGDATSIEEERAYNPYLR DEQLVCA TD Primarily distributed in human oral cavity. DEQLVCA FC This enzyme hydrolyzes beta-lactam. DEQLVCA KD 2: Bacteria DEQLVCA PL 976: Bacteroidetes DEQLVCA CL 200643: Bacteroidia DEQLVCA OD 171549: Bacteroidales DEQLVCA FM 171552: Prevotellaceae DEQLVCA GE 1283313: Alloprevotella DEQLVCA SP 76122: Alloprevotella tannerae DE2IL34 ID DE2IL34 DE2IL34 DN Beta-lactamase (blaB) DE2IL34 GN blaB DE2IL34 SN Penicillinase; Cephalosporinase; Beta-lactam; CAPGI0001_1569 DE2IL34 UC C2M7J0_CAPGI DE2IL34 RD Amoxicillin DE2IL34 E1 3: Hydrolases DE2IL34 E2 3.5: Carbon-nitrogen hydrolase DE2IL34 E3 3.5.2: Cyclic amide hydrolase DE2IL34 EC 3.5.2.6 DE2IL34 SQ MSIFTFFQQLFAQPITQKQIFAEDISKINSLEKAIQQSELVVNYLLQEHYTPSMSICVTKRGFPIWEQGYGYADIENKVGVNPRETLYRIASVSKPLTGMALTKMQEQGWIDWNCSLYDYVPYFPKKQYDFTVKQLAGHLAGIRAYKGKEVFLNRFMSIKEGISVFAEDPLLFEPGTQYYYNSYDINLVSLAMQEARKEPFEWYVTHNVLEPIGMKHTFPDMGGLSPNQSIPYSPDKKKQFKRSTEVNNFFKLGGGGFLSTAYDVNLMGQAILGKAFLKPEYQEQMLTSQQLNTGKDTGYGIGWQTTTDWQGRTYYGHIGNGIGGYAWFYVYPEEEVVFTFLFNTTNPSIADYMHRIMDCMLKGASYKEYTTHNYPVIHNEQ DE2IL34 TD Primarily distributed in human oral cavity. DE2IL34 FC This enzyme hydrolyzes beta-lactam. DE2IL34 KD 2: Bacteria DE2IL34 PL 976: Bacteroidetes DE2IL34 CL 117743: Flavobacteriia DE2IL34 OD 200644: Flavobacteriales DE2IL34 FM 49546: Flavobacteriaceae DE2IL34 GE 1016: Capnocytophaga DE2IL34 SP 1017: Capnocytophaga gingivalis DE1NJIW ID DE1NJIW DE1NJIW DN Beta-lactamase (blaB) DE1NJIW GN ampC DE1NJIW SN Penicillinase; Cephalosporinase; Beta-lactam; PAU_00771; PA-RVA13-1244 DE1NJIW UC B6VMJ3_PHOAA DE1NJIW RD Amoxicillin DE1NJIW E1 3: Hydrolases DE1NJIW E2 3.5: Carbon-nitrogen hydrolase DE1NJIW E3 3.5.2: Cyclic amide hydrolase DE1NJIW EC 3.5.2.6 DE1NJIW KG Two-component system:pay02020; beta-Lactam resistance:pay01501 DE1NJIW SQ MTKRFSVLTGSLLLAASLGVQASNTPDQTRLTNTVDKTIHSLMQEYDIPGMAIAVTFRGQHFFYQYGDASKESNTPVTKETIFELGSVSKTFAGSLISWAQVTGAISFSDKASQHFQPLAGSAFDNINLLNIATYTAGGLPLQFPDEIDNNSKMVDWFQHWQPKYPPGTYRQYSNPSIGLAGYIVAQRLEKPYSILVKNQILSPLGLHHTWFNVPAQEMKNYALGYSKENKPIRINPGVLDEEAYGLKTSAQDLIGFVDANIDPSRVGDSKLAQAIRATHTGYYRTGEMTQGLGWELYHWPVTLEQVLSGNSAEIAYQANKTTELSPPEPPTDALFINKTGSTNGFGAYVAFVPQEQMGIVLLANKNYPNEARIKAAWQILKALK DE1NJIW TD Primarily distributed in human skin. DE1NJIW FC This enzyme hydrolyzes beta-lactam. DE1NJIW KD 2: Bacteria DE1NJIW PL 1224: Proteobacteria DE1NJIW CL 1236: Gammaproteobacteria DE1NJIW OD 91347: Enterobacterales DE1NJIW FM 1903414: Morganellaceae DE1NJIW GE 29487: Photorhabdus DE1NJIW SP 291112: Photorhabdus asymbiotica DEDIMN9 ID DEDIMN9 DEDIMN9 DN Beta-lactamase (blaB) DEDIMN9 GN blaOXA DEDIMN9 SN Penicillinase; Cephalosporinase; Beta-lactam; blaOXA; DXA69_22160 DEDIMN9 UC A0A413GBG0_9BACE DEDIMN9 RD Amoxicillin DEDIMN9 E1 3: Hydrolases DEDIMN9 E2 3.5: Carbon-nitrogen hydrolase DEDIMN9 E3 3.5.2: Cyclic amide hydrolase DEDIMN9 EC 3.5.2.6 DEDIMN9 SQ MKNILFVVFISMIFLFVCCNTTTNKNIIETEISDFDKILDSFQVNGSILIYDNDKNTFYSNDFDWAKNGKFSPASTFKIPNSIIAVELGIIENDTTILKWNGEQRKMDIWEKDLSFKDAFRISCVPCYQEIARKIGTIKMKEYLEKFEYKNMIFDSLTIDNFWLEGNSKISQKQQIDFLRKFYFSKFPISDRTIKIVKNIMEIERTENYILSGKTGLSSIEEKYNGWFVGYVETKSNVYFFATNVIPTDGLNVDDFISSRINVTKNALKQMNIMK DEDIMN9 TD Primarily distributed in human gut. DEDIMN9 FC This enzyme hydrolyzes beta-lactam. DEDIMN9 KD 2: Bacteria DEDIMN9 PL 976: Bacteroidetes DEDIMN9 CL 200643: Bacteroidia DEDIMN9 OD 171549: Bacteroidales DEDIMN9 FM 815: Bacteroidaceae DEDIMN9 GE 816: Bacteroides DEDIMN9 SP 357276: Bacteroides dorei DEJ8X2W ID DEJ8X2W DEJ8X2W DN Beta-lactamase (blaB) DEJ8X2W GN bla DEJ8X2W SN Penicillinase; Cephalosporinase; Beta-lactam; bla; DWW10_06180 DEJ8X2W UC A0A412YFL9_9BACE DEJ8X2W RD Amoxicillin DEJ8X2W E1 3: Hydrolases DEJ8X2W E2 3.5: Carbon-nitrogen hydrolase DEJ8X2W E3 3.5.2: Cyclic amide hydrolase DEJ8X2W EC 3.5.2.6 DEJ8X2W SQ MKAKFFLSCMALAILFSACNTTNRTPKQKIEQQIDSFLKDKKATVGVAVLANDEIVAVYNNQIHFPLLSVFKFHVGLAVLDKMDKDHIGLDSLIEVKSSQLKPDTYSPLRDEFPDQDITISLGELLKYTISKSDNNTCDILIEYVGGIDQVNEYVKSLGIKDCNLAATETLMHTSGDAYLNWSTPEEVVRLLNIADKQPLFATQYKDFLQATMQETSTGKDKLKGQLPADVIVGHKTGSSDRTPEGIKIADNDAGFVILPNGQKYYIAVFVMESQETDADNAAIIASISKIVYDTLNSDIQ DEJ8X2W TD Primarily distributed in human gut. DEJ8X2W FC This enzyme hydrolyzes beta-lactam. DEJ8X2W KD 2: Bacteria DEJ8X2W PL 976: Bacteroidetes DEJ8X2W CL 200643: Bacteroidia DEJ8X2W OD 171549: Bacteroidales DEJ8X2W FM 815: Bacteroidaceae DEJ8X2W GE 816: Bacteroides DEJ8X2W SP 329854: Bacteroides intestinalis DEFEVNH ID DEFEVNH DEFEVNH DN Beta-lactamase (blaB) DEFEVNH GN blaB DEFEVNH SN Penicillinase; Cephalosporinase; Beta-lactam; Beta-lactamase superfamily domain; NCTC12948_00659 DEFEVNH UC A0A381DV31_9FLAO DEFEVNH RD Amoxicillin DEFEVNH E1 3: Hydrolases DEFEVNH E2 3.5: Carbon-nitrogen hydrolase DEFEVNH E3 3.5.2: Cyclic amide hydrolase DEFEVNH EC 3.5.2.6 DEFEVNH SQ MKYTFRTFFCGMGDCIFLMLENGCHTLNIMVDCGKYIDEIDNFVKTELKNKIDYLIVTHIDNDHINGLITMLTKNSDLIIGNIIYNCYQRLIKNAIPWTDKMTENVSRLYGKLPIVIDMISQDINEEKAVTLAECILRKEEWNRTWQREYVTDESPAIQLANNMGRIIFLSPSQAALDQLDKKYRKLFWQQLYKQKEEEYDKEETIYEALMRIAQLDEDEEIKEENVNDCTINEHTLKQYACQSLSKMDDNNMASIAFVWEHQGHRILFMGDADPTQVSKAIEEAYKDETKPIIFDLIKVSHHGSAHSTSKELMNMADSERFFFTGGAKERPSLQTLGRIITNPLPDGIEYRDIRYNRHNVILKKLADLSVEEKNSLHIKVNDNQNSYEFSY DEFEVNH TD Primarily distributed in human oral cavity. DEFEVNH FC This enzyme hydrolyzes beta-lactam. DEFEVNH KD 2: Bacteria DEFEVNH PL 976: Bacteroidetes DEFEVNH CL 117743: Flavobacteriia DEFEVNH OD 200644: Flavobacteriales DEFEVNH FM 49546: Flavobacteriaceae DEFEVNH GE 1016: Capnocytophaga DEFEVNH SP 45242: Capnocytophaga granulosa DEAPGXV ID DEAPGXV DEAPGXV DN Beta-lactamase (blaB) DEAPGXV GN cfxA DEAPGXV SN Penicillinase; Cephalosporinase; Beta-lactam; cfxA; DYJ25_11230 DEAPGXV UC A0A347B2J2_9BACT DEAPGXV RD Amoxicillin DEAPGXV E1 3: Hydrolases DEAPGXV E2 3.5: Carbon-nitrogen hydrolase DEAPGXV E3 3.5.2: Cyclic amide hydrolase DEAPGXV EC 3.5.2.6 DEAPGXV SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEAPGXV TD Primarily distributed in human oral cavity. DEAPGXV FC This enzyme hydrolyzes beta-lactam. DEAPGXV KD 2: Bacteria DEAPGXV PL 976: Bacteroidetes DEAPGXV CL 200643: Bacteroidia DEAPGXV OD 171549: Bacteroidales DEAPGXV FM 171552: Prevotellaceae DEAPGXV GE 838: Prevotella DEAPGXV SP 28129: Prevotella denticola DE0PDVC ID DE0PDVC DE0PDVC DN Beta-lactamase (blaB) DE0PDVC GN blaB DE0PDVC SN Penicillinase; Cephalosporinase; Beta-lactam; CDC50_06275 DE0PDVC UC A0A2A3N1K0_CAPSP DE0PDVC RD Amoxicillin DE0PDVC E1 3: Hydrolases DE0PDVC E2 3.5: Carbon-nitrogen hydrolase DE0PDVC E3 3.5.2: Cyclic amide hydrolase DE0PDVC EC 3.5.2.6 DE0PDVC SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGDVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DE0PDVC TD Primarily distributed in human oral cavity. DE0PDVC FC This enzyme hydrolyzes beta-lactam. DE0PDVC KD 2: Bacteria DE0PDVC PL 976: Bacteroidetes DE0PDVC CL 117743: Flavobacteriia DE0PDVC OD 200644: Flavobacteriales DE0PDVC FM 49546: Flavobacteriaceae DE0PDVC GE 1016: Capnocytophaga DE0PDVC SP 1019: Capnocytophaga sputigena DEQL32N ID DEQL32N DEQL32N DN Beta-lactamase (blaB) DEQL32N GN blaB DEQL32N SN Penicillinase; Cephalosporinase; Beta-lactam; CGC53_04505 DEQL32N UC A0A250F962_9FLAO DEQL32N RD Amoxicillin DEQL32N E1 3: Hydrolases DEQL32N E2 3.5: Carbon-nitrogen hydrolase DEQL32N E3 3.5.2: Cyclic amide hydrolase DEQL32N EC 3.5.2.6 DEQL32N KG beta-Lactam resistance:clk01501 DEQL32N SQ MEKNRKKQIVVLSIALVCIFILVFSLFHKSATKDSANPPLTNVLTDSISQIVSACPGEIGVAVIVNNRDTVKVNNKSVYPMMSVFKVHQALALCNDFDNKGISLDTLVNINRDKLDPKTWSPMLKDYSGPVISLTVRDLLRYTLTQSDNNASNLMFKDMVNVAQTDSFIATLIPRSSFQIAYTEEEMSADHNKAYSNYTSPLGAAMLMNRLFTEGLIDDEKQSFIKNTLKECKTGVDRIAAPLLDKEGVVIAHKTGSGYVNENGVLAAHNDVAYICLPNNISYTLAVFVKDFKGNESQASQYVAHISAVVYSLLMQTSVKS DEQL32N TD Primarily distributed in human oral cavity. DEQL32N FC This enzyme hydrolyzes beta-lactam. DEQL32N KD 2: Bacteria DEQL32N PL 976: Bacteroidetes DEQL32N CL 117743: Flavobacteriia DEQL32N OD 200644: Flavobacteriales DEQL32N FM 49546: Flavobacteriaceae DEQL32N GE 1016: Capnocytophaga DEQL32N SP 327575: Capnocytophaga leadbetteri DE9HF0I ID DE9HF0I DE9HF0I DN Beta-lactamase (blaB) DE9HF0I GN per1 DE9HF0I SN Penicillinase; Cephalosporinase; Beta-lactam; per1; bla; AA415_02475; DXC34_16285 DE9HF0I UC A0A120A1C6_BACSE DE9HF0I RD Amoxicillin DE9HF0I E1 3: Hydrolases DE9HF0I E2 3.5: Carbon-nitrogen hydrolase DE9HF0I E3 3.5.2: Cyclic amide hydrolase DE9HF0I EC 3.5.2.6 DE9HF0I SQ MKLRYTLIGVLCFSINIVLQAQQQALEGKIAGFLKGKKATVGVAVLTDKDETILHNNEVHYPLLSVFKFHVALAVLDKMNREEIPLKHIVHVKASQLQPNTYSPLRQKHSGQDLDISLGELLQYSISLSDNNACDILIEYTGGIGHIHQYIRKLGINDFNLSETEDSMHRNPQKAYANWSTPSEMVRLLKMADEKDLFAPVYRDFLWKTMTETATGSNKLKGLLPSNTVVGHKTGSSDRNLKGVKMADNDAGIVIMPGGKKYYIAVFVTDSSETDEENAAIIAHISRMVYDEMK DE9HF0I TD Primarily distributed in human gut. DE9HF0I FC This enzyme hydrolyzes beta-lactam. DE9HF0I KD 2: Bacteria DE9HF0I PL 976: Bacteroidetes DE9HF0I CL 200643: Bacteroidia DE9HF0I OD 171549: Bacteroidales DE9HF0I FM 815: Bacteroidaceae DE9HF0I GE 816: Bacteroides DE9HF0I SP 46506: Bacteroides stercoris DESHI6O ID DESHI6O DESHI6O DN Beta-lactamase (blaB) DESHI6O GN per1 DESHI6O SN Penicillinase; Cephalosporinase; Beta-lactam; per1; bla; AA416_02797; DHV19_16385 DESHI6O UC A0A108T9G3_9BACE DESHI6O RD Amoxicillin DESHI6O E1 3: Hydrolases DESHI6O E2 3.5: Carbon-nitrogen hydrolase DESHI6O E3 3.5.2: Cyclic amide hydrolase DESHI6O EC 3.5.2.6 DESHI6O SQ MKAKFFLSCMALAILFSACNTANRTPKQKIEQQIDSLLKDKKATVGVAVLANDETVAVYNNQIHFPLLSVFKFHVGLAVLDKMDKGHIALDSLIEVKSSQLKSNTYSPLRDKFPDQDITISLGELLKYSISQSDNNACDILIEYAGGIDQVNEYVKSLGIKDCNLAATEDLMHTSGDAYLNWSTPEEVVRLLNIADKQPLFGTQYKDFLQAIMQETSTGKDKLKGQLPADVIVGHKTGSSDRTPEGIKIADNDAGFVILPNGQKYYIAVFVMESQETDTDNAAIIASISKIVYDTLNSDIQ DESHI6O TD Primarily distributed in human gut. DESHI6O FC This enzyme hydrolyzes beta-lactam. DESHI6O KD 2: Bacteria DESHI6O PL 976: Bacteroidetes DESHI6O CL 200643: Bacteroidia DESHI6O OD 171549: Bacteroidales DESHI6O FM 815: Bacteroidaceae DESHI6O GE 816: Bacteroides DESHI6O SP 246787: Bacteroides cellulosilyticus DEZS3N4 ID DEZS3N4 DEZS3N4 DN Beta-lactamase (blaB) DEZS3N4 GN blaB DEZS3N4 SN Penicillinase; Cephalosporinase; Beta-lactam; HMPREF1991_01269 DEZS3N4 UC A0A069QS91_PRELO DEZS3N4 RD Amoxicillin DEZS3N4 E1 3: Hydrolases DEZS3N4 E2 3.5: Carbon-nitrogen hydrolase DEZS3N4 E3 3.5.2: Cyclic amide hydrolase DEZS3N4 EC 3.5.2.6 DEZS3N4 SQ MFRILFSALCAFALNASANNIPTASPEEVGMSLARLRAADEVILRAIRDHRTPGAVLAVVRHGKMAYLKAYGNRQTYPTTQPMTTQTVFDMASCTKPMATAISAMLLVERGKLRLSDPVSTYLPEFKNWHGEGKDSVTIRVEDLLTHTSGLPPYAPVKTLAEANGKPNPAKLMAYIARCKRDFKPHTDMQYSCLNYITLQNIVERITGQSLRTFAANNIFIPLGMNHTDFLPCAPDKSGKLANTSQPRWVTNGEQASLTPIAPTERQPNGTVKLGQVHDPLACTLNGGVSGNAGLFSSAEDVATLCAMLQNGGEWGGKRILSPLTVKAMRSIPQNFNSFGRSLGWDVSSAYASNQGDLLSDEAYGHTGYTGTSIVIDPVNDLSIILLCNSVHPVDTTNVIRLRAQVANAVAASITNEAAAFPGYYYVRMRTFEAEPPIRSTDIVMLGNSLTEGGRDWAEKLGKPNVRNRGISGDVAMGIDARLFQITPHKPAKIFLLVGINDVSHDLTVDSIVTNIRLLVEHIHAQSPKTKLVLQSLLPIRESTGRWKRLQGKTDMIPQINARLEALAREKGLTFINLFPHFTEPGTNVLRSELTYDGLHLSKAGYDVWVKLLKPHL DEZS3N4 TD Primarily distributed in human oral cavity. DEZS3N4 FC This enzyme hydrolyzes beta-lactam. DEZS3N4 KD 2: Bacteria DEZS3N4 PL 976: Bacteroidetes DEZS3N4 CL 200643: Bacteroidia DEZS3N4 OD 171549: Bacteroidales DEZS3N4 FM 171552: Prevotellaceae DEZS3N4 GE 838: Prevotella DEZS3N4 SP 840: Prevotella loescheii DE5NSUX ID DE5NSUX DE5NSUX DN Beta-lactamase (blaB) DE5NSUX GN HMPREF1639_06800 DE5NSUX SN Penicillinase; Cephalosporinase; Beta-lactam; HMPREF1639_06800 DE5NSUX UC A0A095XPV0_9FIRM DE5NSUX RD Amoxicillin DE5NSUX E1 3: Hydrolases DE5NSUX E2 3.5: Carbon-nitrogen hydrolase DE5NSUX E3 3.5.2: Cyclic amide hydrolase DE5NSUX EC 3.5.2.6 DE5NSUX SQ MKKIVILSCFIAFAFVVLFPRSFIFAAEETEHYETVIDKVADAYIGKSVPGACVIVSEHGEIVFSKAYGYADLEKNIPMDPENTVFEWGSISKTFIWVGVMQLNEEGKIDLDADIRNYLPKGFLKNLHYDTPITMRHLMNHTAGFEEQLINLRYFESDKEFTLAEVLSSHQPEQVFSPGKVSAYSNWGAALAAFIVERVSGQNYKEYVNEHILKPLDMNNTSIGPFQNDNPTILARKAVGYSFFEKGFRKEPNMYLRMYPAGGMNGSAGDLLNYAQELAKNNDKDNLLFNNPHTKKEMFTETYRSYGANSGLSHGFWQYANNPEMHGHEGGTYGFKTQIWVEPKNERAILILTNVMETEFCSEIMEKIAYTEADEKKIKENLDLKMLSGDYLPARSALKNVGKIQGKKQMISIRVTDGNRLCLTMPFEDKKQYYEQIDSNIFFCKDASPEEKILAFNINDGKVHSMSFRLAHDYIPATNTQGKIAFLFSLGTYISTTLLFLTLLIICIISTLQRWKRCMRHHIYLYICGAMLGISGITGMAHWFSIYEILAHELMIIIIAGWCFSIIGILCGGYAIFKERSIKNSGLLLIFIAQIFSAYYLGFLTVV DE5NSUX TD Primarily distributed in human oral cavity. DE5NSUX FC This enzyme hydrolyzes beta-lactam. DE5NSUX KD 2: Bacteria DE5NSUX PL 1239: Firmicutes DE5NSUX CL 186801: Clostridia DE5NSUX OD 186802: Clostridiales DE5NSUX FM 186804: Peptostreptococcaceae DE5NSUX GE 1257: Peptostreptococcus DE5NSUX SP 1261: Peptostreptococcus anaerobius DEQ1CTE ID DEQ1CTE DEQ1CTE DN Beta-lactamase (blaB) DEQ1CTE GN C7120_10955 DEQ1CTE SN Penicillinase; Cephalosporinase; Beta-lactam; C7120_10955 DEQ1CTE UC A0A2T4TNV5_9BACT DEQ1CTE RD Amoxicillin DEQ1CTE E1 3: Hydrolases DEQ1CTE E2 3.5: Carbon-nitrogen hydrolase DEQ1CTE E3 3.5.2: Cyclic amide hydrolase DEQ1CTE EC 3.5.2.6 DEQ1CTE SQ MKLKRLVFLIPIWLIALCSFGQAGHVSARLTLDGKMQALAERLLEGKQGSIVAIEPSTGEVKCLVSKSFLSDTINRAIGQAYSPGSTFKVAQALALVSEGIVNKDSKFTCSEGFWKNNMHIGCHKHSSPQDLIGAIAHSCNSWFCKAFMNMIRDRVKYKNKLEAINKWKEYMSSLGLGRPLGIDMEGETDGEMPDSEMLERLYSGRWNEATIMWVGMGQGEVLATPLQLCNLAAIIANKGYYYIPHIHKDVDTTYTTRRLSTASPEAFELIRKGMRKAVTTGTATAIQHPDWQICGKTGTAENPGEDHSVFIGYAPMNNPKIAVSVYVENAGFGADLAAPLAQLMIEQYLTGKLSERSERKARQWYDFLVVPHDPTEVTEKETPTKIPMPTQPASPSTSPKGKS DEQ1CTE TD Primarily distributed in human oral cavity. DEQ1CTE FC This enzyme hydrolyzes beta-lactam. DEQ1CTE KD 2: Bacteria DEQ1CTE PL 976: Bacteroidetes DEQ1CTE CL 200643: Bacteroidia DEQ1CTE OD 171549: Bacteroidales DEQ1CTE FM 171552: Prevotellaceae DEQ1CTE GE 838: Prevotella DEQ1CTE SP 165179: Prevotella copri DEX0NP3 ID DEX0NP3 DEX0NP3 DN Beta-glucosidase (bglA) DEX0NP3 GN bglA DEX0NP3 SN Periplasmic beta-glucosidase; Glucan endo-1 3-beta-D-glucosidase; Beta-D-glucosidase; BGK71_01895 DEX0NP3 UC A0A249DCH3_LACRH DEX0NP3 RD Esculin DEX0NP3 E1 3: Hydrolases DEX0NP3 E2 3.2: Glycosylase DEX0NP3 E3 3.2.1: O/S-glycosyl compound glycosidase DEX0NP3 EC 3.2.1.21 DEX0NP3 SQ MTQQQLYTPKGFPKNFLWGGAIAANQAEGAWQTDGRGPSQADIMLLPEKYSRLGSFGEHVTRADIERALADKSGNYPRRRGIDFFHTYDSDLDLMKEMGFNTFRTSFSWSRIFPNGDEKEPNEKGLKFYDKLIQKMLDLDITPVMTISHYEMPLNLITKYGGWENPEMINFFNRFAQVLLDRYHDKVKYWIVFNQVNDVYGWGEFAGLGILKENQPNEKQAKFQAVHHQFIANAQTVKYGHQIDNDIKIGMMLGLTNVYPASTKPQDVMATYKRWNKDTFFFSDVLARGEYPGYMLRYFEDNNIQLSIDQKELDLIKNNPVDFIAFSYYSSSLISADTPDSLLPNPELEESIWGWSFDPIGFRYGFNVLWDRYHLPLFVAENGLGALDTVEDNKIHDAYRIKYLKAHIKQMKEAIKDGVHIFGYAAWGPIDIVSYSQAEMSKRYGFVYVDLDDKGNGTGKRIRKDSFYWYQKVIESNGDQI DEX0NP3 TD Primarily distributed in human skin. DEX0NP3 FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DEX0NP3 KD 4751: Fungi DEX0NP3 PL 5204: Basidiomycota DEX0NP3 CL 1538075: Malasseziomycetes DEX0NP3 OD 162474: Malasseziales DEX0NP3 FM 742845: Malasseziaceae DEX0NP3 GE 55193: Malassezia DEX0NP3 SP 55194: Malassezia furfur DESLN2J ID DESLN2J DESLN2J DN Beta-glucosidase (bglA) DESLN2J GN bglA DESLN2J SN Periplasmic beta-glucosidase; Glucan endo-1 3-beta-D-glucosidase; Beta-D-glucosidase; BGK71_01895 DESLN2J UC A0A249DCH3_LACRH DESLN2J RD Esculin DESLN2J E1 3: Hydrolases DESLN2J E2 3.2: Glycosylase DESLN2J E3 3.2.1: O/S-glycosyl compound glycosidase DESLN2J EC 3.2.1.21 DESLN2J SQ MTQQQLYTPKGFPKNFLWGGAIAANQAEGAWQTDGRGPSQADIMLLPEKYSRLGSFGEHVTRADIERALADKSGNYPRRRGIDFFHTYDSDLDLMKEMGFNTFRTSFSWSRIFPNGDEKEPNEKGLKFYDKLIQKMLDLDITPVMTISHYEMPLNLITKYGGWENPEMINFFNRFAQVLLDRYHDKVKYWIVFNQVNDVYGWGEFAGLGILKENQPNEKQAKFQAVHHQFIANAQTVKYGHQIDNDIKIGMMLGLTNVYPASTKPQDVMATYKRWNKDTFFFSDVLARGEYPGYMLRYFEDNNIQLSIDQKELDLIKNNPVDFIAFSYYSSSLISADTPDSLLPNPELEESIWGWSFDPIGFRYGFNVLWDRYHLPLFVAENGLGALDTVEDNKIHDAYRIKYLKAHIKQMKEAIKDGVHIFGYAAWGPIDIVSYSQAEMSKRYGFVYVDLDDKGNGTGKRIRKDSFYWYQKVIESNGDQI DESLN2J TD Primarily distributed in human skin. DESLN2J FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DESLN2J KD 4751: Fungi DESLN2J PL 5204: Basidiomycota DESLN2J CL 1538075: Malasseziomycetes DESLN2J OD 162474: Malasseziales DESLN2J FM 742845: Malasseziaceae DESLN2J GE 55193: Malassezia DESLN2J SP 76777: Malassezia sympodialis DEAZSKX ID DEAZSKX DEAZSKX DN Beta-glucosidase (bglA) DEAZSKX GN bglA DEAZSKX SN Periplasmic beta-glucosidase; Glucan endo-1 3-beta-D-glucosidase; Beta-D-glucosidase; BG; H109_07780 DEAZSKX UC A0A059IXB8_TRIIM DEAZSKX RD Esculin DEAZSKX E1 3: Hydrolases DEAZSKX E2 3.2: Glycosylase DEAZSKX E3 3.2.1: O/S-glycosyl compound glycosidase DEAZSKX EC 3.2.1.21 DEAZSKX SQ MLFRWCPLVALAIASGTAATEQSWESPPYYPSPWTKGEGEWEDAYQKAVSFVSQLTLAEKVNLTTGVGWMQESCVGQVGSIPRLGFRSLCMQDGPLGIRFGDYVTAFPAGINVAATWSRELAYLRGKAMGEEFHGKGADVILGPAIGPIGRAPEGGRNWEGFGPDPVLAGRLVAETIKGMQKTGVIACAKHFIANEQERFRIAAEAQGYGFDIAESISSNVDDVTMHEIYLWPFADAVKAGVGSIMCSYNQINNSYGCGNSYTQNKLLKGELGFRGFIMSDWQAHHSGVGSAFAGLDMSMPGDTLFGTGVSFWGANLTIAVANGTIPEWRVDDMAVRIMAAYYKVGRDKVQVPINFNSWTTDVEGYQHALVKEGYGVVNQRVNVRDHHARIARRMASDSIVLLKNEGVLPLTGTEQFTAIIGEDAGPNINGPNSCPDRGCDNGTLAMGWGSGTTNFPYLVTPDDAIQREIVAKGVGNVMSVLQNGDFKNIQSVAGQANVALVFINSDSGEGYISVDGNEGDRKNLTTWKGGDEMVKQVTSVCNNTVLVIHSSGPILAGQWHDNPNITAILWAGLPGQESGNALVDVLYGKVNPGGKSPFTWGRTAEDYGTTILREPNNGKGAPQHQFSEGIMFEYRHFDQQNITPVYEFGYGLSYTTFSYSNLRVRPMRANKYVPATGMTKPAPRLGHSSTKYADYLFPGGFKGVTKYVYPWLTSTDPKEASGDKNYGMPLEDYVPPNANNGDAQPVLPASGVPGGNPGLFEDLYKVSAVITNDGDRVGEEVPQLYISLGGDRNAKVVLRGFDRIRLAPRQRFRWRTTITRRDISNWDPASQDWVMTEHPKIVYVGSSSRNLPLQAPLPPPNLA DEAZSKX TD Primarily distributed in human skin. DEAZSKX FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DEAZSKX KD 4751: Fungi DEAZSKX PL 4890: Ascomycota DEAZSKX CL 147545: Eurotiomycetes DEAZSKX OD 33183: Onygenales DEAZSKX FM 34384: Arthrodermataceae DEAZSKX GE 5550: Trichophyton DEAZSKX SP 101480: Trichophyton interdigitale DEAZSKX SU Trichophyton interdigitale NCPF 0335 DE3UF6Z ID DE3UF6Z DE3UF6Z DN Azoreductase (azoR) DE3UF6Z GN BSIG_4687 DE3UF6Z SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; BSIG_4687; Btheta7330_01816 DE3UF6Z UC A0A0P0ETC6_BACT4 DE3UF6Z RD Sulfasalazine DE3UF6Z E1 1: Oxidoreductase DE3UF6Z E2 1.7: Cytochrome acceptor oxidoreductase DE3UF6Z E3 1.7.1: NAD/NADP acceptor oxidoreductase DE3UF6Z EC 1.7.1.6 DE3UF6Z SQ MDRKGFLKSTMIATGSLLLGGAGICRFLNDKEPADGPFPRTIEKIHCGNMKKVLVIMSAGTKLGNTDRLTDAYIKGLVERGHSVTKVYLGSMRIEGCRGCGVCQRLAHQCAVRDGMQDIYPLFAECDTVVMASPLYFWTITSQLKAFIDRLYAISADDKYPQKDTVLLMTAGDDNENTFDQPKQYFRLLSQALGWNEVGIYCAGGCTGCEKLARQIDKVHLENVYKMGLEL DE3UF6Z TD Primarily distributed in human gut. DE3UF6Z FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. DE3UF6Z KD 2: Bacteria DE3UF6Z PL 976: Bacteroidetes DE3UF6Z CL 200643: Bacteroidia DE3UF6Z OD 171549: Bacteroidales DE3UF6Z FM 815: Bacteroidaceae DE3UF6Z GE 816: Bacteroides DE3UF6Z SP 818: Bacteroides thetaiotaomicron DE6GHJ5 ID DE6GHJ5 DE6GHJ5 DN Azoreductase (azoR) DE6GHJ5 GN azoR DE6GHJ5 SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; BSIG_4687; Btheta7330_01816 DE6GHJ5 UC A0A0P0ETC6_BACT4 DE6GHJ5 RD Sulfasalazine DE6GHJ5 E1 1: Oxidoreductase DE6GHJ5 E2 1.7: Cytochrome acceptor oxidoreductase DE6GHJ5 E3 1.7.1: NAD/NADP acceptor oxidoreductase DE6GHJ5 EC 1.7.1.6 DE6GHJ5 SQ MDRKGFLKSTMIATGSLLLGGAGICRFLNDKEPADGPFPRTIEKIHCGNMKKVLVIMSAGTKLGNTDRLTDAYIKGLVERGHSVTKVYLGSMRIEGCRGCGVCQRLAHQCAVRDGMQDIYPLFAECDTVVMASPLYFWTITSQLKAFIDRLYAISADDKYPQKDTVLLMTAGDDNENTFDQPKQYFRLLSQALGWNEVGIYCAGGCTGCEKLARQIDKVHLENVYKMGLEL DE6GHJ5 TD Primarily distributed in human gut. DE6GHJ5 FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. DE6GHJ5 KD 2: Bacteria DE6GHJ5 PL 201174: Actinobacteria DE6GHJ5 CL 1760: Actinobacteria DE6GHJ5 OD 85004: Bifidobacteriales DE6GHJ5 FM 31953: Bifidobacteriaceae DE6GHJ5 GE 1678: Bifidobacterium DE6GHJ5 SP 1689: Bifidobacterium dentium DETEMAH ID DETEMAH DETEMAH DN Azoreductase (azoR) DETEMAH GN azoR DETEMAH SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; DCW31_09905 DETEMAH UC A0A349MYB4_9LACO DETEMAH RD Sulfasalazine DETEMAH E1 1: Oxidoreductase DETEMAH E2 1.7: Cytochrome acceptor oxidoreductase DETEMAH E3 1.7.1: NAD/NADP acceptor oxidoreductase DETEMAH EC 1.7.1.6 DETEMAH SQ MAKILVIKAHPLTIEHSRTLKILDAFMTQYKVSNPEDTIETRDLYAEEFPDIDRSMMTAWGQLQNGVGFPDLTTQQQQQLSAYDSTTQQYIDADKVILANPMWNLSIPAKLQAWIDTICVAGKTFQYTETAEIPLVPGKKVLHIQTAGGFYDGKDFGAKYISGIMHFLGASDVQELAVEGMDHFPEKAEAFMQDGLERATALATKF DETEMAH TD Primarily distributed in human gut. DETEMAH FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. And it requires NADH, but not NADPH, as an electron donor for its activity. DETEMAH KD 2: Bacteria DETEMAH PL 1239: Firmicutes DETEMAH CL 91061: Bacilli DETEMAH OD 186826: Lactobacillales DETEMAH FM 33958: Lactobacillaceae DETEMAH GE 1578: Lactobacillus DETEMAH SP 1581: Lactobacillus buchneri DEIKZOU ID DEIKZOU DEIKZOU DN Azoreductase (azoR) DEIKZOU GN azoR DEIKZOU SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; BSIG_4687; Btheta7330_01816 DEIKZOU UC A0A0P0ETC6_BACT4 DEIKZOU RD Sulfasalazine DEIKZOU E1 1: Oxidoreductase DEIKZOU E2 1.7: Cytochrome acceptor oxidoreductase DEIKZOU E3 1.7.1: NAD/NADP acceptor oxidoreductase DEIKZOU EC 1.7.1.6 DEIKZOU SQ MDRKGFLKSTMIATGSLLLGGAGICRFLNDKEPADGPFPRTIEKIHCGNMKKVLVIMSAGTKLGNTDRLTDAYIKGLVERGHSVTKVYLGSMRIEGCRGCGVCQRLAHQCAVRDGMQDIYPLFAECDTVVMASPLYFWTITSQLKAFIDRLYAISADDKYPQKDTVLLMTAGDDNENTFDQPKQYFRLLSQALGWNEVGIYCAGGCTGCEKLARQIDKVHLENVYKMGLEL DEIKZOU TD Primarily distributed in human gut. DEIKZOU FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. DEIKZOU KD 2: Bacteria DEIKZOU PL 976: Bacteroidetes DEIKZOU CL 200643: Bacteroidia DEIKZOU OD 171549: Bacteroidales DEIKZOU FM 815: Bacteroidaceae DEIKZOU GE 816: Bacteroides DEIKZOU SP 817: Bacteroides fragilis DEIKZOU SU Bacteroides fragilis str. 3397 T10 DENLBG3 ID DENLBG3 DENLBG3 DN Azoreductase (azoR) DENLBG3 GN azoR DENLBG3 SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; azoR; BSIG_4687; Btheta7330_01816 DENLBG3 UC A0A0P0ETC6_BACT4 DENLBG3 RD Sulfasalazine DENLBG3 E1 1: Oxidoreductase DENLBG3 E2 1.7: Cytochrome acceptor oxidoreductase DENLBG3 E3 1.7.1: NAD/NADP acceptor oxidoreductase DENLBG3 EC 1.7.1.6 DENLBG3 SQ MDRKGFLKSTMIATGSLLLGGAGICRFLNDKEPADGPFPRTIEKIHCGNMKKVLVIMSAGTKLGNTDRLTDAYIKGLVERGHSVTKVYLGSMRIEGCRGCGVCQRLAHQCAVRDGMQDIYPLFAECDTVVMASPLYFWTITSQLKAFIDRLYAISADDKYPQKDTVLLMTAGDDNENTFDQPKQYFRLLSQALGWNEVGIYCAGGCTGCEKLARQIDKVHLENVYKMGLEL DENLBG3 TD Primarily distributed in human gut. DENLBG3 FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. DENLBG3 KD 2: Bacteria DENLBG3 PL 201174: Actinobacteria DENLBG3 CL 1760: Actinobacteria DENLBG3 OD 85004: Bifidobacteriales DENLBG3 FM 31953: Bifidobacteriaceae DENLBG3 GE 1678: Bifidobacterium DENLBG3 SP 28025: Bifidobacterium animalis DENLBG3 SU Bifidobacterium animalis subsp. lactis B94 DEXCQTM ID DEXCQTM DEXCQTM DN Arylamine N-acetyltransferase (NAT) DEXCQTM GN nat DEXCQTM SN N-hydroxyarylamine O-acetyltransferase; nhoA; nat; NCTC10741_01829; SAMEA1712962_01653 DEXCQTM UC A0A3P8LE58_TSUPA DEXCQTM RD Isoniazid DEXCQTM E1 2: Transferase DEXCQTM E2 2.3: Acyltransferase DEXCQTM E3 2.3.1: Acyltransferase DEXCQTM EC 2.3.1.5 DEXCQTM SQ MNDDAAWGAPALDLPRYLHRIGLQAPPAPDLAGLSTLVRAHALTLPWENFDAVRGIPGELTIDALQRRMIEGRRGYGCTGHVPLLAAALQRTGFRFGAASGRVLVDGGPSASTHALLIVEVDGAPHLAEVGFGAVPLAPLRLESGLEQDAGGWRYRLTAEAVGFGEEWRLDFLDPSSGQWRPQYRFALADRTWSDLRMTNFYVATSPHSPFRGRLMAVVNRPGERHVLTRDAVISTRPDGFRETVPYVAADRRAILAESFAIDLPEDEAAALAAVSGS DEXCQTM TD Primarily distributed in human lung. DEXCQTM FC This enzyme is wide specificity for aromatic amines, including serotonin and it also catalyses acetyl-transfer between arylamines without CoA. DEXCQTM KD 2: Bacteria DEXCQTM PL 201174: Actinobacteria DEXCQTM CL 1760: Actinobacteria DEXCQTM OD 85007: Corynebacteriales DEXCQTM FM 85028: Tsukamurellaceae DEXCQTM GE 2060: Tsukamurella DEXCQTM SP 2061: Tsukamurella paurometabola DEV01ZI ID DEV01ZI DEV01ZI DN Arginine dihydrolase (arcA) DEV01ZI GN arcA DEV01ZI SN Arginine deiminase; arcA; AD; ADI; BJR09_08810; E2557_01300; NCTC13830_00349 DEV01ZI UC A0A380FWY5_9STAP DEV01ZI RD L-arginine DEV01ZI E1 3: Hydrolases DEV01ZI E2 3.5: Carbon-nitrogen hydrolase DEV01ZI E3 3.5.3: Linear amidine hydrolase DEV01ZI EC 3.5.3.6 DEV01ZI SQ MTQGPIQVNSEIGKLKTVLLKRPGKELENLVPDHLSGLLFDDIPYLKVAQEEHDKFAQTLRDEGVEVVYLEKLAAEAIADKAVREQFIDDILAESQKTILGHEEEIKKFFETLSDQELIDKIMAGVRKEEIELETTHLVEYLDDRYPFYLDPMPNLYFTRDPQASVGRGMTINRMYWRARRRESLFITYILKHHPRFKDADVPVWLDRNSPFNIEGGDELILSKEALAIGISERTSAQAIERLARNIFKDESTTFKKVIAIEIPNSRSFMHLDTVFTMIDYDKFTVHSAIFKEENNMNIFTIEYDEAKDDIKITHSHKLRETLADVLGVDHIDFIPTGNGDVIDGAREQWNDGSNTLCIRPGVVVTYDRNYVSNQLLRDKGIKVIEITGSELVRGRGGPRCMSQPLFREDI DEV01ZI TD Primarily distributed in human blood. DEV01ZI FC This enzyme acts on canavanine. DEV01ZI KD 2: Bacteria DEV01ZI PL 1239: Firmicutes DEV01ZI CL 91061: Bacilli DEV01ZI OD 1385: Bacillales DEV01ZI FM 90964: Staphylococcaceae DEV01ZI GE 1279: Staphylococcus DEV01ZI SP 1276936: Staphylococcus petrasii DEV01ZI SU Staphylococcus petrasii subsp. Jettensis DEST6E5 ID DEST6E5 DEST6E5 DN Alpha-glucosidase (aglA) DEST6E5 GN malL_1 DEST6E5 SN Oligo-1,6-glucosidase; 6-phospho-alpha-glucosidase 1; DW040_17105; ERS852394_00764; malL_1 DEST6E5 UC A0A173ZA10_9FIRM DEST6E5 RD M-7403 DEST6E5 GI 42449350 DEST6E5 E1 3: Hydrolases DEST6E5 E2 3.2: Glycosylase DEST6E5 E3 3.2.1: O/S-glycosyl compound glycosidase DEST6E5 EC 3.2.1.20 DEST6E5 SQ MEKKWWKESVVYQIYPKSFKDSNGDGVGDIRGIIQKLDYLKELGVNVLWISPMLESPQDDNGYDISDYRRIYKEYGTMEDYEELLSEAHKRDIRILMDLVVNHTSDEHNWFIESRKSKDNPYRDYYIWKDPVNGKEPNNWGGVFGGSAWEYDAQTQMYYLHLFSKKQPDLNWENEKVRQEVYDMMTFWCEKGIDGFRMDVISMISKDQAFPDGKMNNSLYGDFGPYCVHGPRIHEFLQEMNREVLSRYDIMTVGETSGVTIEEAQKYAGEAGKELNMVFQFEHVDNGSGDYGKWTTEKYDFKEFKRIMIKWQEELQGKAWNSLFLGNHDQPRSVSRFGNDNPAYRETSAKMLATCLHMMQGTPYVYQGEELGMTNVYFDKLEDYRDIESINFFTELTESGLMTPEYMMKCLMLRSRDNARTPMQWDDSEQAGFTDGESWIKVNPNYKEINAAQQLKDPNSIFHYYQKLISLRKEKDIIVYGEFEPLYRDDEQIFAYTRKLDQEKLLTVCNFSDKNAEMEIPEEFKGAECLITNLDRTVFEGKIVLKPYEAFVLYKK DEST6E5 TD Primarily distributed in human gut. DEST6E5 FC This enzyme is probably involved in the catabolism of alpha-glycosides accumulated via a phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). And it hydrolyzes a wide variety of 6-phospho-alpha-D-glucosides including the five isomeric derivatives of sucrose, i.e. trehalulose-6'-phosphate, turanose-6'-phosphate, maltulose-6'-phosphate, leucrose-6'-phosphate, and palatinose-6'-phosphate, but is not active on sucrose-6-phosphate. Moreover, it can also hydrolyze maltose-6'-phosphate and methyl-alpha-glucose-6-phosphate, and poorly, trehalose-6-phosphate. However, it fails to hydrolyze beta-O-linked phosphorylated disaccharides such as cellobiose-6'-phosphate and gentiobiose-6'-phosphate. DEST6E5 KD 2: Bacteria DEST6E5 PL 1239: Firmicutes DEST6E5 CL 186801: Clostridia DEST6E5 OD 186802: Clostridiales DEST6E5 FM 186803: Lachnospiraceae DEST6E5 GE 572511: Blautia DEST6E5 SP 40520: Blautia obeum DE19C8A ID DE19C8A DE19C8A DN L,D-carboxypeptidase A (ldcA) DE19C8A GN b1192 DE19C8A SN Carboxypeptidase; LD-carboxypeptidase; Murein tetrapeptide carboxypeptidase; AC789_1c12840; ACN002_1829; ACU90_08670; AM270_04255; AMK83_26425; BANRA_01764; BB545_18240; BN17_10381; BON69_25620; BON71_20135; BON72_24745; BON76_11630; BON94_22610; BON95_19240; BVL39_22290; BvCms28BK_02847; BvCmsNSNP036_02737; BvCmsNSP006_02167; BvCmsOUP014_03493; BvCmsSIP019_04003; BvCmsSIP044_03891; C6669_23480; C7235_14540; C7B02_00395; C9114_05805; C9162_18910; C9Z28_09785; C9Z37_17470; COD46_20425; CR538_15200; CRD98_02440; CWS33_11925; D2184_25220; D6T60_03840; D9K48_17225; DEN89_04765; DEO04_08505; DL545_14375; DQF57_19545; DS732_10945; DXT69_15460; E0I42_05850; EHH55_11410; EJC75_04705; ERS085374_03985; ERS085379_03097; EXX24_08925; EXX78_01285; EYY78_23060; F0312_19185; F1E03_16650; F1E13_06740; F7F29_12315; FQ915_22760; FQR64_13480; HW43_09665; HmCmsJML079_01442; NCTC8009_03749; NCTC8179_03095; NCTC8622_05704; NCTC9055_04762; NCTC9111_02948; NCTC9703_02151; RG28_17325; RX35_02911; SAMEA3472043_03661; SAMEA3472055_01267; SAMEA3472070_03304; SAMEA3472114_00072; SAMEA3752553_01826; SAMEA3753064_00071; SAMEA3753290_01164; UN86_12510; b1192; ldcA DE19C8A UC J7R060_ECOLX DE19C8A RD Dithiazoline DE19C8A E1 3: Hydrolases DE19C8A E2 3.4: Peptidase DE19C8A E3 3.4.17: Metallocarboxypeptidase DE19C8A EC 3.4.17.13 DE19C8A SQ MSLFHLIAPSGYCIKQHAALRGIHRLTDEGHQVNNVEVIARRCERFAGTETERLEDLNSLARLTTPNTIVLAVRGGYGASRLLADIDWQALVARQQHDPLLICGHSDFTAIQCGLLAQGNVITFSGPMLVANFGADELNAFTEHHFWLALRNKTFTIEWQGEGPTCQTEGTLWGGNLAMLISLIGTPWMPKIENGILVLEDINEHPFRVERMLLQLYHAGILPRQKAIILGSFSGSTPNDYDAGYNLESVYAFLRSRLSIPLITGLDFGHEQRTVTLPLGAHAILNNTREGTQLTISGHPVLKM DE19C8A TD Primarily distributed in human gut. DE19C8A FC This enzyme hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains. DE19C8A KD 2: Bacteria DE19C8A PL 1224: Proteobacteria DE19C8A CL 1236: Gammaproteobacteria DE19C8A OD 91347: Enterobacterales DE19C8A FM 543: Enterobacteriaceae DE19C8A GE 561: Escherichia DE19C8A SP 562: Escherichia coli DEH2VKT ID DEH2VKT DEH2VKT DN Glycoside hydrolase (cscA) DEH2VKT GN cscA DEH2VKT SN Sucrose-6-phosphate hydrolase A; Invertase A; Sucrase A; cscA DEH2VKT UC CSCA_ECOLX DEH2VKT RD LS-69767 DEH2VKT E1 3: Hydrolases DEH2VKT E2 3.2: Glycosylase DEH2VKT E3 3.2.1: O/S-glycosyl compound glycosidase DEH2VKT EC 3.2.1.26 DEH2VKT SQ MTQSRLHAAQNALAKLHERRGNTFYPHFHLAPPAGWMNDPNGLIWFNDRYHAFYQHHPMSEHWGPMHWGHATSDDMIHWQHEPIALAPGDENDKDGCFSGSAVDDNGVLSLIYTGHVWLDGAGNDDAIREVQCLATSRDGIHFEKQGVILTPPEGIMHFRDPKVWREADTWWMVVGAKDPGNTGQILLYRGSSLREWTFDRVLAHADAGESYMWECPDFFSLGDQHYLMFSPQGMNAEGYSYRNRFQSGVIPGMWSPGRLFAQSGHFTELDNGHDFYAPQSFVAKDGRRIVIGWMDMWESPMPSKREGWAGCMTLARELSESNGKLLQRPVHEAESLRQQHQSISPRTISNKYVLQENAQAVEIQLQWALKNSDAEHYGLQLGAGMRLYIDNQSERLVLWRYYPHENLDGYRSIPLPQGDMLALRIFIDTSSVEVFINDGEAVMSSRIYPQPEERELSLYASHGVAVLQHGALWQLG DEH2VKT TD Primarily distributed in human gut. DEH2VKT FC This enzyme takes part in glucuronoside catabolic process. Substrates include sucrose. DEH2VKT KD 2: Bacteria DEH2VKT PL 1224: Proteobacteria DEH2VKT CL 1236: Gammaproteobacteria DEH2VKT OD 91347: Enterobacterales DEH2VKT FM 543: Enterobacteriaceae DEH2VKT GE 561: Escherichia DEH2VKT SP 562: Escherichia coli DEH2VKT SU Escherichia coli BEN2908 DECY6JG ID DECY6JG DECY6JG DN D-Lactate dehydrogenase (ldhA) DECY6JG GN ldhA DECY6JG SN Glycolate dehydrogenase; D-lactate ferricytochrome C oxidoreductase; Fermentative lactate dehydrogenase; D-LDH; JW1375; b1380; hslI; htpH; ldhA DECY6JG UC LDHD_ECOLI DECY6JG RD DB-053072 DECY6JG GI 946315 DECY6JG E1 1: Oxidoreductase DECY6JG E2 1.1: CH-OH donor oxidoreductase DECY6JG E3 1.1.1: NAD/NADP oxidoreductase DECY6JG EC 1.1.1.28 DECY6JG KG Metabolic pathways:ecj01100; Microbial metabolism in diverse environments:ecj01120; Pyruvate metabolism:ecj00620 DECY6JG PD 5Z1Z DECY6JG SQ MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSRPVLEELKKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFEQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEKGETCPNELV DECY6JG TD Primarily distributed in human gut. DECY6JG FC This enzyme has D-lactate dehydrogenase activity. DECY6JG KD 2: Bacteria DECY6JG PL 1224: Proteobacteria DECY6JG CL 1236: Gammaproteobacteria DECY6JG OD 91347: Enterobacterales DECY6JG FM 543: Enterobacteriaceae DECY6JG GE 561: Escherichia DECY6JG SP 562: Escherichia coli DEMIUB2 ID DEMIUB2 DEMIUB2 DN Beta-lactamase (blaB) DEMIUB2 GN bla DEMIUB2 SN Penicillinase; Cephalosporinase; Beta-lactam; Beta-lactamase TEM; IRT-4; TEM-1; TEM-16/CAZ-7; TEM-2; TEM-24/CAZ-6; TEM-3; TEM-4; TEM-5; TEM-6; TEM-8/CAZ-2; and; bla; blaT-3; blaT-4; blaT-5; blaT-6 DEMIUB2 UC BLAT_ECOLX DEMIUB2 RD Cefotaxime DEMIUB2 GI 10076131 DEMIUB2 E1 3: Hydrolases DEMIUB2 E2 3.5: Carbon-nitrogen hydrolase DEMIUB2 E3 3.5.2: Cyclic amide hydrolase DEMIUB2 EC 3.5.2.6 DEMIUB2 PD 1AXB; 1BT5; 1BTL; 1CK3; 1ERM; 1ERO; 1ERQ; 1ESU; 1FQG; 1JTD; 1JTG; A/C=24-286; 1JVJ; 1JWP; 1LI0; 1LI9; 1M40; 1NXY; 1NY0; 1NYM; 1NYY; 1PZO; 1PZP; 1S0W; 1TEM; 1XPB; 1XXM; 1YT4; 1ZG4; 1ZG6; 2B5R; 2V1Z; 2V20; 3C7U; 3C7V; 3CMZ; 3DTM; 3JYI; 3TOI; 4DXB; 4DXC; 4GKU; 4IBR; 4IBX; 4ID4; 4MEZ; 4QY5; 4QY6; 4R4R; 4R4S; 4RVA; 4RX2; 4RX3; 4ZJ1; 4ZJ2; 4ZJ3; 5HVI; 5HW1; 5HW5; 5I52; 5I63; 5IQ8; 5KKF; 5KPU; 5NPO; 6APA; 6AYK; 6B2N DEMIUB2 SQ MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW DEMIUB2 TD Primarily distributed in human gut. DEMIUB2 FC This enzyme is the most prevalent beta-lactamase in enterobacteria. It hydrolyzes the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors. DEMIUB2 KD 2: Bacteria DEMIUB2 PL 1224: Proteobacteria DEMIUB2 CL 1236: Gammaproteobacteria DEMIUB2 OD 91347: Enterobacterales DEMIUB2 FM 543: Enterobacteriaceae DEMIUB2 GE 561: Escherichia DEMIUB2 SP 562: Escherichia coli DEWU03P ID DEWU03P DEWU03P DN Sorbitol dehydrogenase (SORD) DEWU03P GN SORD DEWU03P SN Ribitol dehydrogenase; Xylitol dehydrogenase; Polyol dehydrogenase; (R,R)-butanediol dehydrogenase; L-iditol 2-dehydrogenase; RDH; SDH; SORD DEWU03P UC DHSO_HUMAN DEWU03P RD Sorbitol DEWU03P GI 6652 DEWU03P E1 1: Oxidoreductase DEWU03P E2 1.1: CH-OH donor oxidoreductase DEWU03P E3 1.1.1: NAD/NADP oxidoreductase DEWU03P EC 1.1.1.14 DEWU03P RC Formation of xylulose-5-phosphate:R-HSA-5661270; Fructose biosynthesis:R-HSA-5652227 DEWU03P KG Fructose and mannose metabolism:hsa00051; Metabolic pathways:hsa01100; Pentose and glucuronate interconversions:hsa00040 DEWU03P PD 1PL6; 1PL7; 1PL8 DEWU03P SQ MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNFIVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFCATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCGAGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGQLGCKPEVTIECTGAEASIQAGIYATRSGGNLVLVGLGSEMTTVPLLHAAIREVDIKGVFRYCNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP DEWU03P TD Primarily distributed in cervix, uterine, liver and thyroid gland. DEWU03P FC This enzyme catalyzes the reversible NAD(+)- dependent oxidation of various sugar alcohols. It is mostly active with D- sorbitol (D-glucitol), L-threitol, xylitol and ribitol as substrates, leading to the C2-oxidized products D-fructose, L-erythrulose, D- xylulose, and D-ribulose, respectively. It is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism. It also catalyzes the stereospecific oxidation of (2R,3R)-2,3-butanediol. And to a lesser extent, it can also oxidize L-arabinitol, galactitol and D-mannitol and glycerol in vitro. DEWU03P KD 33208: Metazoa DEWU03P PL 7711: Chordata DEWU03P CL 40674: Mammalia DEWU03P OD 9443: Primates DEWU03P FM 9604: Hominidae DEWU03P GE 9605: Homo DEWU03P SP 9606: Homo sapiens DEXHBCR ID DEXHBCR DEXHBCR DN S-methyl-5'-thioadenosine phosphorylase (MTAP) DEXHBCR GN MTAP DEXHBCR SN MTA phosphorylase; 5'-methylthioadenosine phosphorylase; MTAPase; MSAP; MTAP DEXHBCR UC MTAP_HUMAN DEXHBCR RD Methylthioadenosine DEXHBCR GI 4507 DEXHBCR E1 2: Transferase DEXHBCR E2 2.4: Glycosyltransferases DEXHBCR E3 2.4.2: Pentosyltransferase DEXHBCR EC 2.4.2.28 DEXHBCR RC Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation:R-HSA-8950505; Methionine salvage pathway:R-HSA-1237112 DEXHBCR KG Cysteine and methionine metabolism:hsa00270; Metabolic pathways:hsa01100 DEXHBCR PD 1K27; 1SD1; 1SD2; 3LN5; 3OZC; 3OZD; 3OZE; 5EUB; 5TC5 DEXHBCR SQ MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH DEXHBCR TD Low tissue/organ specificity. DEXHBCR FC This enzyme catalyzes the reversible phosphorylation of S-methyl-5'-thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. It is involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. And it is responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Additionally, it has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. DEXHBCR KD 33208: Metazoa DEXHBCR PL 7711: Chordata DEXHBCR CL 40674: Mammalia DEXHBCR OD 9443: Primates DEXHBCR FM 9604: Hominidae DEXHBCR GE 9605: Homo DEXHBCR SP 9606: Homo sapiens DER0EN5 ID DER0EN5 DER0EN5 DN Phosphoglucomutase 3 (PGM3) DER0EN5 GN PGM3 DER0EN5 SN Acetylglucosamine phosphomutase; N-acetylglucosamine-phosphate mutase; Phosphoacetylglucosamine mutase; Phosphoglucomutase-3; AGM1; PAGM; PGM 3; PGM3 DER0EN5 UC AGM1_HUMAN DER0EN5 RD NA-alpha-D-glucosamine DER0EN5 GI 5238 DER0EN5 E1 5: Isomerase DER0EN5 E2 5.4: Mutase DER0EN5 E3 5.4.2: Phosphomutase DER0EN5 EC 5.4.2.3 DER0EN5 RC Synthesis of UDP-N-acetyl-glucosamine:R-HSA-446210 DER0EN5 KG Amino sugar and nucleotide sugar metabolism:hsa00520; Metabolic pathways:hsa01100 DER0EN5 SQ MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRVLIDISEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELLVEIGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKQSAEQLEDKKRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIGERPQPGF DER0EN5 TD Primarily distributed in pancreas, heart, liver and placenta. DER0EN5 FC This enzyme catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O- glycosylation. DER0EN5 KD 33208: Metazoa DER0EN5 PL 7711: Chordata DER0EN5 CL 40674: Mammalia DER0EN5 OD 9443: Primates DER0EN5 FM 9604: Hominidae DER0EN5 GE 9605: Homo DER0EN5 SP 9606: Homo sapiens DE0K52I ID DE0K52I DE0K52I DN Methionine-tRNA ligase cytoplasmic (MARS) DE0K52I GN MARS1 DE0K52I SN Methionyl-tRNA synthetase; Cytoplasmic methionine--tRNA ligase; MARS; MARS1; MetRS DE0K52I UC SYMC_HUMAN DE0K52I RD Methionine DE0K52I GI 4141 DE0K52I E1 6: Ligase DE0K52I E2 6.1: Carbon-oxygen ligase DE0K52I E3 6.1.1: Aminoacyl tRNA synthetase DE0K52I EC 6.1.1.10 DE0K52I RC Cytosolic tRNA aminoacylation:R-HSA-379716; Selenoamino acid metabolism:R-HSA-2408522 DE0K52I KG Aminoacyl-tRNA biosynthesis:hsa00970; Metabolic pathways:hsa01100; Selenocompound metabolism:hsa00450 DE0K52I PD 2DJV; 4BL7; 4BVX; 4BVY; 5GL7; 5GOY; 5Y6L DE0K52I SQ MRLFVSDGVPGCLPVLAAAGRARGRAEVLISTVGPEDCVVPFLTRPKVPVLQLDSGNYLFSTSAICRYFFLLSGWEQDDLTNQWLEWEATELQPALSAALYYLVVQGKKGEDVLGSVRRALTHIDHSLSRQNCPFLAGETESLADIVLWGALYPLLQDPAYLPEELSALHSWFQTLSTQEPCQRAAETVLKQQGVLALRPYLQKQPQPSPAEGRAVTNEPEEEELATLSEEEIAMAVTAWEKGLESLPPLRPQQNPVLPVAGERNVLITSALPYVNNVPHLGNIIGCVLSADVFARYSRLRQWNTLYLCGTDEYGTATETKALEEGLTPQEICDKYHIIHADIYRWFNISFDIFGRTTTPQQTKITQDIFQQLLKRGFVLQDTVEQLRCEHCARFLADRFVEGVCPFCGYEEARGDQCDKCGKLINAVELKKPQCKVCRSCPVVQSSQHLFLDLPKLEKRLEEWLGRTLPGSDWTPNAQFITRSWLRDGLKPRCITRDLKWGTPVPLEGFEDKVFYVWFDATIGYLSITANYTDQWERWWKNPEQVDLYQFMAKDNVPFHSLVFPCSALGAEDNYTLVSHLIATEYLNYEDGKFSKSRGVGVFGDMAQDTGIPADIWRFYLLYIRPEGQDSAFSWTDLLLKNNSELLNNLGNFINRAGMFVSKFFGGYVPEMVLTPDDQRLLAHVTLELQHYHQLLEKVRIRDALRSILTISRHGNQYIQVNEPWKRIKGSEADRQRAGTVTGLAVNIAALLSVMLQPYMPTVSATIQAQLQLPPPACSILLTNFLCTLPAGHQIGTVSPLFQKLENDQIESLRQRFGGGQAKTSPKPAVVETVTTAKPQQIQALMDEVTKQGNIVRELKAQKADKNEVAAEVAKLLDLKKQLAVAEGKPPEAPKGKKKK DE0K52I TD Low tissue/organ specificity. DE0K52I FC This enzyme catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. DE0K52I KD 33208: Metazoa DE0K52I PL 7711: Chordata DE0K52I CL 40674: Mammalia DE0K52I OD 9443: Primates DE0K52I FM 9604: Hominidae DE0K52I GE 9605: Homo DE0K52I SP 9606: Homo sapiens DEB4JZV ID DEB4JZV DEB4JZV DN Gamma-glutamylcyclotransferase 2 (CHAC2) DEB4JZV GN CHAC2 DEB4JZV SN Glutathione-specific gamma-glutamylcyclotransferase 2; Cation transport regulator-like protein 2; Gamma-GCG 2; CHAC2 DEB4JZV UC CHAC2_HUMAN DEB4JZV RD ANW-43980 DEB4JZV GI 494143 DEB4JZV E1 4: Lyases DEB4JZV E2 4.3: Carbon-nitrogen lyase DEB4JZV E3 4.3.2: Amidine-lyase DEB4JZV EC 4.3.2.7 DEB4JZV RC Glutathione synthesis and recycling:R-HSA-174403 DEB4JZV KG Glutathione metabolism:hsa00480; Metabolic pathways:hsa01100 DEB4JZV SQ MWVFGYGSLIWKVDFPYQDKLVGYITNYSRRFWQGSTDHRGVPGKPGRVVTLVEDPAGCVWGVAYRLPVGKEEEVKAYLDFREKGGYRTTTVIFYPKDPTTKPFSVLLYIGTCDNPDYLGPAPLEDIAEQIFNAAGPSGRNTEYLFELANSIRNLVPEEADEHLFALEKLVKERLEGKQNLNCI DEB4JZV TD Low tissue/organ specificity. DEB4JZV FC This enzyme catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide and acts specifically on glutathione, but not on other gamma-glutamyl peptides. DEB4JZV KD 33208: Metazoa DEB4JZV PL 7711: Chordata DEB4JZV CL 40674: Mammalia DEB4JZV OD 9443: Primates DEB4JZV FM 9604: Hominidae DEB4JZV GE 9605: Homo DEB4JZV SP 9606: Homo sapiens DEYIEO5 ID DEYIEO5 DEYIEO5 DN Beta-lactamase (blaB) DEYIEO5 GN ampC DEYIEO5 SN Penicillinase; Cephalosporinase; Beta-lactam; PAU_00771; PA-RVA13-1244 DEYIEO5 UC AMPC_SERMA DEYIEO5 RD Cefotaxime DEYIEO5 E1 3: Hydrolases DEYIEO5 E2 3.5: Carbon-nitrogen hydrolase DEYIEO5 E3 3.5.2: Cyclic amide hydrolase DEYIEO5 EC 3.5.2.6 DEYIEO5 SQ MTKMNRCAALIAALILPTAHAAQQQDIDAVIQPLMKKYGVPGMAIAVSVDGKQQIYPYGVASKQTGKPITEQTLFEVGSLSKTFTATLAVYAQQQSKLSFKDPASHYLPDVRGSAFDGVSLLNLATHTSGLPLFVPDDVTNNAQLMAYYRAWQPKHPAGSYRVYSNLGIGMLGMIAAKSLDQPFIQAMEQGMLPALGMSHTYVQVPAAQMANYAQGYSKDDKPVRVNPGPLDAESYGIKSNARDLIRYLDANLQQVKVASVARRWPRRTSVITSAGAFTQDLMWENYPYPVKLSRLIEGNNAGMIMNGTPATAITPPQPELRAGWYNKTGSTGGFSTYAVFIPAKNIAVEMLANKWFPNDDRVEAAYHIIQALEKR DEYIEO5 TD Primarily distributed in human gut. DEYIEO5 FC This enzyme hydrolyzes beta-lactam with a substrate specificity for cephalosporins. DEYIEO5 KD 2: Bacteria DEYIEO5 PL 1224: Proteobacteria DEYIEO5 CL 1236: Gammaproteobacteria DEYIEO5 OD 91347: Enterobacterales DEYIEO5 FM 1903411: Yersiniaceae DEYIEO5 GE 613: Serratia DEYIEO5 SP 615: Serratia marcescens DEB90AL ID DEB90AL DEB90AL DN Carbapenemase (cphA) DEB90AL GN cphA DEB90AL SN Versatile beta-lactamase; Versatile hydrolytic beta-lactamase; Beta-lactamase II; Carbapenem-hydrolyzing metallo-beta-lactamase; Metallo-beta-lactamase type 2b; Metallo-beta-lactamase type IIb; cphA DEB90AL UC BLAB_AERHY DEB90AL RD Meropenem DEB90AL E1 3: Hydrolases DEB90AL E2 3.5: Carbon-nitrogen hydrolase DEB90AL E3 3.5.2: Cyclic amide hydrolase DEB90AL EC 3.5.2.6 DEB90AL PD 1X8G; 1X8H; 1X8I; 2GKL; 2QDS; 3F9O; 3FAI; 3IOF; 3IOG; 3SW3; 3T9M DEB90AL SQ MMKGWMKCGLAGAVVLMASFWGGSVRAAGMSLTQVSGPVYVVEDNYYVQENSMVYFGAKGVTVVGATWTPDTARELHKLIKRVSRKPVLEVINTNYHTDRAGGNAYWKSIGAKVVSTRQTRDLMKSDWAEIVAFTRKGLPEYPDLPLVLPNVVHDGDFTLQEGKVRAFYAGPAHTPDGIFVYFPDEQVLYGNCILKEKLGNLSFADVKAYPQTLERLKAMKLPIKTVIGGHDSPLHGPELIDHYEALIKAAPQS DEB90AL TD Primarily distributed in human gut. DEB90AL FC This enzyme confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. It is able to hydrolyze penicillin and imipenem, but is much less active against cephalothin, cefotaxime, meropenem and ceftazidime. DEB90AL KD 2: Bacteria DEB90AL PL 1224: Proteobacteria DEB90AL CL 1236: Gammaproteobacteria DEB90AL OD 135624: Aeromonadales DEB90AL FM 84642: Aeromonadaceae DEB90AL GE 642: Aeromonas DEB90AL SP 644: Aeromonas hydrophila DES378D ID DES378D DES378D DN Methylthioribose kinase (mtnK) DES378D GN mtnK DES378D SN MTR kinase; 5-deoxyribose disposal kinase; 5-deoxyribose kinase; mtnK; mtrK DES378D UC MTNK_KLEPN DES378D RD 5-Methylthioribose 1-phosphate DES378D E1 2: Transferase DES378D E2 2.7: Kinase DES378D E3 2.7.1: Phosphotransferase DES378D EC 2.7.1.100 DES378D SQ MSQYHTFTAHDAVAYAQQFAGIDNPSELVSAQEVGDGNLNLVFKVFDRQGVSRAIVKQALPYVRCVGESWPLTLDRARLEAQTLVAHYQHSPQHTVKIHHFDPELAVMVMEDLSDHRIWRGELIANVYYPQAARQLGDYLAQVLFHTSDFYLHPHEKKAQVAQFINPAMCEITEDLFFNDPYQIHERNNYPAELEADVAALRDDAQLKLAVAALKHRFFAHAEALLHGDIHSGSIFVAEGSLKAIDAEFGYFGPIGFDIGTAIGNLLLNYCGLPGQLGIRDAAAAREQRLNDIHQLWTTFAERFQALAAEKTRDAALAYPGYASAFLKKVWADAVGFCGSELIRRSVGLSHVADIDTIQDDAMRHECLRHAITLGRALIVLAERIDSVDELLARVRQYS DES378D TD Primarily distributed in human gut. DES378D FC This enzyme catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate. DES378D KD 2: Bacteria DES378D PL 1224: Proteobacteria DES378D CL 1236: Gammaproteobacteria DES378D OD 91347: Enterobacterales DES378D FM 543: Enterobacteriaceae DES378D GE 570: Klebsiella DES378D SP 573: Klebsiella pneumoniae DEOWDK1 ID DEOWDK1 DEOWDK1 DN Oxygen-insensitive NADPH nitroreductase B (nfsB) DEOWDK1 GN nfsB DEOWDK1 SN Oxygen-insensitive NAD(P)H nitroreductase B; Dihydropteridine reductase; FMN-dependent nitroreductase; STM0578; pnrB DEOWDK1 UC NFSB_SALTY DEOWDK1 RD AI3-23606 DEOWDK1 GI 1252098 DEOWDK1 E1 1: Oxidoreductase DEOWDK1 E2 1.5: CH-NH donor oxidoreductase DEOWDK1 E3 1.5.1: NAD/NADP acceptor oxidoreductase DEOWDK1 EC 1.5.1.34 DEOWDK1 KG Microbial metabolism in diverse environments:stm01120; Nitrotoluene degradation:stm00633 DEOWDK1 PD 3HZN DEOWDK1 SQ MDIVSVALQRYSTKAFDPSKKLTAEEADKIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGNYTFNERKMLDASHVVVFCAKTAMDDAWLERVVDQEDADGRFATPEAKAANDKGRRFFADMHRVSLKDDHQWMAKQVYLNVGNFLLGVAAMGLDAVPIEGFDAEVLDAEFGLKEKGYTSLVVVPVGHHSVEDFNAGLPKSRLPLETTLTEV DEOWDK1 TD Primarily distributed in human gut. DEOWDK1 FC This enzyme can reduce a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. And it also can reduce nitrofurazone. DEOWDK1 KD 2: Bacteria DEOWDK1 PL 1224: Proteobacteria DEOWDK1 CL 1236: Gammaproteobacteria DEOWDK1 OD 91347: Enterobacterales DEOWDK1 FM 543: Enterobacteriaceae DEOWDK1 GE 590: Salmonella DEOWDK1 SP 28901: Salmonella enterica DEOWDK1 SU Salmonella enterica subsp. enterica serovar Typhimurium TA100 DEYWTIQ ID DEYWTIQ DEYWTIQ DN Aminoglycoside adenylyltransferase (aadA1a) DEYWTIQ GN aadA1a DEYWTIQ SN Streptomycin 3''-adenylyltransferase; Aminoglycosideadenylyl transferase; aadA; aadA1; aadA1a; ASQ14_26245; ASQ14_27545; FJR52_24735 DEYWTIQ UC Q6YLD2_SALER DEYWTIQ RD Spectinomycin DEYWTIQ GI 39727563 DEYWTIQ E1 2: Transferase DEYWTIQ E2 2.7: Kinase DEYWTIQ E3 2.7.7: Nucleotidyltransferase DEYWTIQ EC 2.7.7.46 DEYWTIQ SQ MREAVIAEVSTQLSEVVGVIERHLEPTLLAVHLYGSAVDGGLKPHSDIDLLVTVTVRLDETTRRALINDLLETSASPGESEILRAVEVTIVVHDDIIPWRYPAKRELQFGEWQRNDILAGIFEPATIDIDLAILLTKAREHSVALVGPAAEELFDPVPEQDLFEALNETLTLWNSPPDWAGDERNVVLTLSRIWYSAVTGKIAPKDVAADWAMERLPAQYQPVILEARQAYLGQEEDRLASRADQLEEFVHYVKGEITKVVGK DEYWTIQ TD Primarily distributed in human gut. DEYWTIQ FC This enzyme can use ATP, dATP, CTP, ITP and GTP as donors and kanamycin, tobramycin and sisomicin as acceptors. And it mediates bacterial resistance to the antibiotics streptomycin and spectomycin. DEYWTIQ KD 2: Bacteria DEYWTIQ PL 1224: Proteobacteria DEYWTIQ CL 1236: Gammaproteobacteria DEYWTIQ OD 91347: Enterobacterales DEYWTIQ FM 543: Enterobacteriaceae DEYWTIQ GE 590: Salmonella DEYWTIQ SP 28901: Salmonella enterica DEBKS91 ID DEBKS91 DEBKS91 DN Beta-lactamase (blaB) DEBKS91 GN blaIMP DEBKS91 SN Penicillinase; Cephalosporinase; Beta-lactam; blaIMP DEBKS91 UC A0A1B1FBM9_ACIBA DEBKS91 RD Meropenem DEBKS91 GI 8458023 DEBKS91 E1 3: Hydrolases DEBKS91 E2 3.5: Carbon-nitrogen hydrolase DEBKS91 E3 3.5.2: Cyclic amide hydrolase DEBKS91 EC 3.5.2.6 DEBKS91 SQ MSKLSVFFIFLFCSIATAAESLPDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLISRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLEQAVKGLNESKKPSKPSN DEBKS91 TD Primarily distributed in human gut. DEBKS91 FC This enzyme hydrolyzes beta-lactam. DEBKS91 KD 2: Bacteria DEBKS91 PL 1224: Proteobacteria DEBKS91 CL 1236: Gammaproteobacteria DEBKS91 OD 72274: Pseudomonadales DEBKS91 FM 468: Moraxellaceae DEBKS91 GE 469: Acinetobacter DEBKS91 SP 470: Acinetobacter baumannii DEBKS91 SU Acinetobacter baumannii ST25; Acinetobacter baumannii ST79 DER7KFQ ID DER7KFQ DER7KFQ DN VanB ligase (vanB) DER7KFQ GN vanB DER7KFQ SN Vancomycin B-type resistance protein VanB; D-alanylalanine synthetase VanB; D-alanine--D-alanine ligase VanB; D-Ala-D-Ala ligase VanB; vanB; vanB2; EF_2294 DER7KFQ UC VANB_ENTFA DER7KFQ RD Vancomycin DER7KFQ GI 1201166 DER7KFQ E1 6: Ligase DER7KFQ E2 6.3: Carbon-nitrogen ligase DER7KFQ E3 6.3.2: Peptide synthase DER7KFQ EC 6.3.2.4 DER7KFQ KG Two-component system:efa02020; Vancomycin resistance:efa01502 DER7KFQ SQ MNKIKVAIIFGGCSEEHDVSVKSAIEIAANINTEKFDPHYIGITKNGVWKLCKKPCTEWEADSLPAIFSPDRKTHGLLVMKEREYETRRIDVAFPVLHGKCGEDGAIQGLFELSGIPYVGCDIQSSAACMDKSLAYILTKNAGIAVPEFQMIEKGDKPEARTLTYPVFVKPARSGSSFGVTKVNSTEELNAAIEAAGQYDGKILIEQAISGCEVGCAVMGNEDDLIVGEVDQIRLSHGIFRIHQENEPEKGSENAMIIVPADIPVEERNRVQETAKKVYRVLGCRGLARVDLFLQEDGGIVLNEVNTLPGFTSYSRYPRMAAAAGITLPALIDSLITLAIER DER7KFQ TD Primarily distributed in human gut. DER7KFQ FC This enzyme is required for high-level resistance to glycopeptides antibiotics. D-Ala--D-Ala ligase of altered specificity catalyzes ester bond formation between D-Ala and various D-hydroxy acids and produce a peptidoglycan which does not terminate in D-alanine but in D-lactate, thus preventing vancomycin binding. DER7KFQ KD 2: Bacteria DER7KFQ PL 1239: Firmicutes DER7KFQ CL 91061: Bacilli DER7KFQ OD 186826: Lactobacillales DER7KFQ FM 81852: Enterococcaceae DER7KFQ GE 1350: Enterococcus DER7KFQ SP 1351: Enterococcus faecalis DEZLFV5 ID DEZLFV5 DEZLFV5 DN Beta-lactamase (blaB) DEZLFV5 GN penB1 DEZLFV5 SN Penicillinase; Cephalosporinase; Beta-lactam; penB1; blaA; F01_480029 DEZLFV5 UC B8R6A5_9BURK DEZLFV5 RD Cefotaxime DEZLFV5 E1 3: Hydrolases DEZLFV5 E2 3.5: Carbon-nitrogen hydrolase DEZLFV5 E3 3.5.2: Cyclic amide hydrolase DEZLFV5 EC 3.5.2.6 DEZLFV5 SQ MTYSSKRRTLLLAAATAPLVLTATACASRQAAAPDPATAAAAAAADAMAPAAAAATLADLERDAGGRLGVCAIDTASGRVIEHRAGERFPFCSTFKAMLSAAVLAQSVERPGLLQQRVKYTKADLVNYSPVSEKHVGAGMTVAALCEATIQYSDNSAANLLMKLIGGPSAVTAYARSIGDDAFRLDRWETELNTALPGDPRDTTTPAAMAASIRVLTLGDALPAAQRAQLVAWLRGNKVGDKRIRAGVPAGWTVGDKTGTGDYGTTNDAGVIWPTSRAPIVLAVYYTQTRADARAKDDVIASVARIVAQTFG DEZLFV5 TD Primarily distributed in human lung. DEZLFV5 FC This enzyme hydrolyzes beta-lactam. DEZLFV5 KD 2: Bacteria DEZLFV5 PL 1224: Proteobacteria DEZLFV5 CL 28216: Betaproteobacteria DEZLFV5 OD 80840: Burkholderiales DEZLFV5 FM 119060: Burkholderiaceae DEZLFV5 GE 32008: Burkholderia DEZLFV5 SP 95486: Burkholderia cenocepacia DEZLFV5 SU Burkholderia cenocepacia J2315 DE0TCN3 ID DE0TCN3 DE0TCN3 DN Ampc beta-lactamase (ampC) DE0TCN3 GN ampC DE0TCN3 SN Beta-lactamase ampC; Bacterial burkholderia beta-lactamase ampC; ampC; BCAS0156 DE0TCN3 UC B4EPS2_BURCJ DE0TCN3 RD Cefotaxime DE0TCN3 E1 3: Hydrolases DE0TCN3 E2 3.5: Carbon-nitrogen hydrolase DE0TCN3 E3 3.5.2: Cyclic amide hydrolase DE0TCN3 EC 3.5.2.6 DE0TCN3 KG Two-component system:bcj02020; beta-Lactam resistance:bcj01501 DE0TCN3 PD 5E2G DE0TCN3 SQ MRFNATRFAATLLVAACATATAGRAAAVTQDDLRDTVTRQIAPLMKQYAIPGMAIGIVADGKPYVFDYGVMSKQTGKPVTGDTLFEIGSVSKTLTATLASDAQEGGELSLADPAGKYLPELQGKPFGVVTLLQLGTHTPGGTPLQVPDSIRDDAGLIRYLDAWRPAYAPGTHRKYSNVAIGMLGWLTAKAMHQDFATLMEQRLFPAIGMTHTYINVPAARMADYAQGYTKDGKPVRMTEGMLWQPAYGVRTTAADLLRFVQANMGMIHTAPRLQRAIERTHTGYFRAGPLTQDLIWEQYPYPVALPTLLAGNAPKMLFDAVPASAIQPPLAPNPATWINKTGSTGGFSTYVAFVPAKRIGIVMLANGNVPIEERVKAAYRILGSLGDAR DE0TCN3 TD Primarily distributed in human lung. DE0TCN3 FC This enzyme hydrolyzes beta-lactam. DE0TCN3 KD 2: Bacteria DE0TCN3 PL 1224: Proteobacteria DE0TCN3 CL 28216: Betaproteobacteria DE0TCN3 OD 80840: Burkholderiales DE0TCN3 FM 119060: Burkholderiaceae DE0TCN3 GE 32008: Burkholderia DE0TCN3 SP 95486: Burkholderia cenocepacia DE0TCN3 SU Burkholderia cenocepacia J2315 DERI7LO ID DERI7LO DERI7LO DN AmpC beta-lactamase (ampC) DERI7LO GN ampC DERI7LO SN Beta-lactamase ampC; Bacterial burkholderia beta-lactamase ampC; ampC; BMULJ_05519 DERI7LO UC A0A0H3KQ39_BURM1 DERI7LO RD Cephalothin DERI7LO E1 3: Hydrolases DERI7LO E2 3.5: Carbon-nitrogen hydrolase DERI7LO E3 3.5.2: Cyclic amide hydrolase DERI7LO EC 3.5.2.6 DERI7LO KG Two-component system:bmj02020; beta-Lactam resistance:bmj01501 DERI7LO SQ MRITVTRVVATLLVATAAIATTGRAAELTQAHIRQIVTQQVAPAMKQYAIPGVAIGVIVDGKRYVFDYGVMSKDTGKPVTADTLFEIGSVSKTLTATLAADAQEGGELSLSDPVARYVPALNGKPAGALTLLELGTHTAGGLPQQVPDAIHDDATLIGYFDAWRPASVPGTQRVYSNVGIGTLGWITAKAMKRDFAELMERRLFPALGMTHTYIDVPDARRADYAQGYTTDGTPIRMKPGGLWQPAYGVRTTATDLLRFVQANMGGIDIAPRLQRAIERTHTGYFRAGPLTQDLIWEQYPYPVALPTLLEGNASKMLSDAVPAVALTPPLAPQRNVWINKTGSTNGFSTYVAFVPAKRIGFVMLANRRVPNEVRVEIAYRILASLGGAR DERI7LO TD Primarily distributed in human lung. DERI7LO FC This enzyme hydrolyzes beta-lactam. DERI7LO KD 2: Bacteria DERI7LO PL 1224: Proteobacteria DERI7LO CL 28216: Betaproteobacteria DERI7LO OD 80840: Burkholderiales DERI7LO FM 119060: Burkholderiaceae DERI7LO GE 32008: Burkholderia DERI7LO SP 87883: Burkholderia multivorans DERI7LO SU Burkholderia multivorans ATCC 17616 DEUGFHC ID DEUGFHC DEUGFHC DN Azoreductase (azoR) DEUGFHC GN azr_2 DEUGFHC SN Azo-dye reductase; FMN-dependent NADH-azo compound oxidoreductase; FMN-dependent NADH-azoreductase; Flavin reductase; NAD(P)H-dependent oxidoreductase; NADPH azoreductase; azoR; A6J87_06095; CKU37_01320; CQA85_07565; D8867_01950; DL07_01170; DWV94_10025; DWY30_01550; DWZ07_06240; FBF48_06605; NCTC8618_04344; azr_2; azr_4 DEUGFHC UC A0A074IU04_STRSL DEUGFHC RD Prontosil DEUGFHC GI 29398535 DEUGFHC E1 1: Oxidoreductase DEUGFHC E2 1.7: Cytochrome acceptor oxidoreductase DEUGFHC E3 1.7.1: NAD/NADP acceptor oxidoreductase DEUGFHC EC 1.7.1.6 DEUGFHC SQ MKFVGLVGANYDQSYNRKLLEFIRRHFKIKFELEVLEIDEVPMFNQDEKWDESFQLRLLNNKITRADGVIIATPEHNHTISAALKSVLEWLSFEVHPFENKPVMIVGASYYDQGTSRAQVHLRKILEAPGVNAYTLPGNEFLLGKAKEAFDLEGNITNEGTINFLEQCLDNFIQYVGVVSKLKKPKPIEPEDLDCNNPIATTVTEVDPDDPEWVEKVAEITGAVSGDTYVKLDHGILTVNQIDMFLKAMPFELTYADDNNQFLYYNNAHQDPDTMFAKRVPPQSGSRMSTVHGSLPPARMKNVEWVIGTLRNGNQEYVRTIVPGSPEGVINTHNYQAMYYDDGSYAGINEIVFNFKPWLDWYLETTGQRLVGGSGPFAPAAASHGGSDATSGASDAGGHGGDAAPAADATSGASSY DEUGFHC TD Primarily distributed in human gut. DEUGFHC FC This enzyme catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. DEUGFHC KD 2: Bacteria DEUGFHC PL 1239: Firmicutes DEUGFHC CL 91061: Bacilli DEUGFHC OD 186826: Lactobacillales DEUGFHC FM 1300: Streptococcaceae DEUGFHC GE 1301: Streptococcus DEUGFHC SP 1314: Streptococcus pyogenes DEWYT5M ID DEWYT5M DEWYT5M DN Beta-lactamase (blaB) DEWYT5M GN blaB DEWYT5M SN Penicillinase; Cephalosporinase; Beta-lactam; HMPREF0675_4578 DEWYT5M UC D4HFC4_CUTAS DEWYT5M RD Ampicillin DEWYT5M GI 2932324 DEWYT5M E1 3: Hydrolases DEWYT5M E2 3.5: Carbon-nitrogen hydrolase DEWYT5M E3 3.5.2: Cyclic amide hydrolase DEWYT5M EC 3.5.2.6 DEWYT5M SQ MTDSVLDVTADALEQAGAHPHRLVVRQHGQVVGRRRWAPWSPDVPSLVYSCSKTFTSAAVGIAVNRGAFGYDDTLADLWPQACTANTGPVAKSMTVRNALSMSTGHSPEQLLEPTLMSRRLPDLNTARILLATEPEGRPGIDFAYNNLATWMLSRLVAQHTGEDVDTIITKEVLDPIGAGPHTWVRDADGIPMGFSGLHIDAEDLSLFGQLLLDDGVHEGARLLPEEWIRQHRVRQVNCDSETDPEWGMGYGWQTWMSSHGYRLDGAFGQYVLIVPEVDAVITMTNEASEGPGDKQAILQAVWDHLLPALADGFQPQPEEIVRTVPTVTGEFDSARSVQGIAPDGSYIVVSPHKESRTWAMSWRCPGTFSHPTDETLDIAVGYEEWQTSHCRVGDDAIDIATSGGWQGETFVARLCVISTPHTLTLRMTPEATTTEWDNEPLNPGGLLGLVHPELRR DEWYT5M TD Primarily distributed in human oral cavity. DEWYT5M FC This enzyme hydrolyzes beta-lactam. DEWYT5M KD 2: Bacteria DEWYT5M PL 201174: Actinobacteria DEWYT5M CL 1760: Actinobacteria DEWYT5M OD 85009: Propionibacteriales DEWYT5M FM 31957: Propionibacteriaceae DEWYT5M GE 1912216: Cutibacterium DEWYT5M SP 1747: Corynebacterium acnes DE2ARDZ ID DE2ARDZ DE2ARDZ DN PenA beta-lactamase (penA1) DE2ARDZ GN penA DE2ARDZ SN Beta-lactamase penA; Penicillinase penA; Cephalosporinase penA; penA DE2ARDZ UC O08350_BURCE DE2ARDZ RD Oxacillin DE2ARDZ E1 3: Hydrolases DE2ARDZ E2 3.5: Carbon-nitrogen hydrolase DE2ARDZ E3 3.5.2: Cyclic amide hydrolase DE2ARDZ EC 3.5.2.6 DE2ARDZ SQ MTHSSQRRILLLAAATAPLALSLGACAARDATVSDAASPVGAAPASFAALERAAGGRLGVCAIDTATGRRALHRADERFPFCSTFKAMLGAAVLAQSVAHPGLLQQRVTYGRSDLVNYSPVTERHVDTGMTVAELCAATIQYSDNTAANELMKRIGGPAAVTAYARSIGDDTFRLDRWETELNTALPGDLRDTTTPAAMAANLRVLVLGDALPPAQRAQLIEWLRGNKVGDKRIRAGVPTGWRVGDKTGTGDYGTTNDVGVLWPPSRAPIVLAVYYTQTRADAKAKDDVIAAATRIASATLA DE2ARDZ TD Primarily distributed in human lung. DE2ARDZ FC This enzyme hydrolyzes beta-lactam. DE2ARDZ KD 2: Bacteria DE2ARDZ PL 1224: Proteobacteria DE2ARDZ CL 28216: Betaproteobacteria DE2ARDZ OD 80840: Burkholderiales DE2ARDZ FM 119060: Burkholderiaceae DE2ARDZ GE 32008: Burkholderia DE2ARDZ SP 292: Burkholderia cepacia DE2ARDZ SU Burkholderia cepacia 249 DED6V8P ID DED6V8P DED6V8P DN Oxygen-insensitive NADPH nitroreductase A (nfsA) DED6V8P GN pnrA DED6V8P SN Oxygen-insensitive NAD(P)H nitroreductase A; Modulator of drug activity A; nfsA; pnrA DED6V8P UC Q7B4Y3_PSEPU DED6V8P RD Nitrobenzoate DED6V8P E1 1: Oxidoreductase DED6V8P E2 1.5: CH-NH donor oxidoreductase DED6V8P E3 1.5.1: NAD/NADP acceptor oxidoreductase DED6V8P EC 1.5.1.38 DED6V8P SQ MSLQDEALKAWQARYGEPANLPAADTVIAQMLQHRSVRAYSDLPVDEQMLSWAIAAAQSASTSSNLQAWSVLAVRDRERLARLARLSGNQRHVEQAPLFLVWLVDWSRLRRLARTLQAPTAGIDYLESYTVGVVDAALAAQNAALAFEAQGLGIVYIGGMRNHPEAMSEELGLPNDTFAVFGMCVGHPDPAQPAEIKPRLAQSVVLHRERYEATEAEAVSVAAYDRRMSDFQHRQQRENRSWSSQAVERVKGADSLSGRHRLRDALNTLGFGLR DED6V8P TD Primarily distributed in human skin. DED6V8P FC This enzyme can catalyze FMN and also can catalyze FAD and riboflavin with lower activity. DED6V8P KD 2: Bacteria DED6V8P PL 1224: Proteobacteria DED6V8P CL 1236: Gammaproteobacteria DED6V8P OD 72274: Pseudomonadales DED6V8P FM 135621: Pseudomonadaceae DED6V8P GE 286: Pseudomonas DED6V8P SP 303: Pseudomonas putida DED6V8P SU Pseudomonas putida JLR11 DEPB9C2 ID DEPB9C2 DEPB9C2 DN Glycosyl hydrolase (glyH) DEPB9C2 GN bglB DEPB9C2 SN Glycosidase; Glycoside hydrolase; Furcatin hydrolase; Isoflavonoid 7-O-apiosylglucosidase; NCTC7914_04276; bglB DEPB9C2 UC A0A379KQ43_PSEPU DEPB9C2 RD Lactulose DEPB9C2 E1 3: Hydrolases DEPB9C2 E2 3.2: Glycosylase DEPB9C2 E3 3.2.1: O/S-glycosyl compound glycosidase DEPB9C2 EC 3.2.1.18 DEPB9C2 SQ MKHFKQAVSLMALGVMQASGALAAGPATGNEVEARVSSILDNMNQAEKINFTRVNDGHMIPSLLKWGIQGTVAYDSSMGVHVNNATFGAQYPSQSALAATWSINRAKEFGLAIAYETRISGGQQMLSPGVNLYRTPYNGRSAEYVSGEDPFLGAVLAPAIVNGIQAQGIQASGKHYLANEQEANRQAVNVVADERTLRELYLPGFESMVKNANVASIMCGFNKVNGDYACENHHLITEVLKGEWGYQGTVISDFNAIHDPFKGAWAGTDLDMPSGLQFTEANLLPYLWSGQLTQNVIDDKVKRNLRAVVSYDFQENLNTAKTLEHTEYGQRASLNAAREGIVLLRNADTAAGKPLLPLARTARIAVIGDWANQAPASPFGTANSPPNSYVTELSGLQQLASNSANVTYLSALSLNPKAAVWYQPTSSGSGVSNAGVKAEYFSNTSLSGDPVLTRIEPGVNLNWTTSTNETSTGTTAVSGFSPTAGAFSARFSATIKPTVSGAHVFKVRADGPYKLWVDGKLVVQSDGVPYSSDVVNALTTSGKSAALVAGKSYNVKLEYRRVQGNFTPALGGLAGVQMSWASLRPPKDIASYDAVVIAAGTNYENEGEGSDHGYALPDQQAELIKFVTKANPNTIVVTHGGGVADMQPWAKKVGAALHAWFPGQQGGQALAEILYGKVNPSGKLPVTIDKKIEDNPSYASYPDPAAYRGDNPLTEIDYSEGLYMGYRGYDKKHAKPLYPFGFGLSYTTFGYSDLKLSTNVMTPGNTVNATFTLTNTGDKAGFEVAQLYIQPIAPQVDRPKKELKGFTKVYLEPGQSKTVSLPIDSRSLAYFVQNTDSWDVDAGKFKVWVGPDSENLTLQRTLVTLMPQHLTTRDSNPLPAPLQAAVQVSDSQAY DEPB9C2 TD Primarily distributed in human gut. DEPB9C2 FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DEPB9C2 KD 2: Bacteria DEPB9C2 PL 1224: Proteobacteria DEPB9C2 CL 1236: Gammaproteobacteria DEPB9C2 OD 72274: Pseudomonadales DEPB9C2 FM 135621: Pseudomonadaceae DEPB9C2 GE 286: Pseudomonas DEPB9C2 SP 303: Pseudomonas putida DERPJ4F ID DERPJ4F DERPJ4F DN Beta-lactamase (blaB) DERPJ4F GN penA DERPJ4F SN Penicillinase; Cephalosporinase; Beta-lactam; C5615_23680 DERPJ4F UC A0A2S8IKB0_BURCE DERPJ4F RD Penicillin G DERPJ4F E1 3: Hydrolases DERPJ4F E2 3.5: Carbon-nitrogen hydrolase DERPJ4F E3 3.5.2: Cyclic amide hydrolase DERPJ4F EC 3.5.2.6 DERPJ4F SQ MTYSSKRRTLLLAAATAPLALTVAACASSQAAAPNEAATPDVAAAAAAAALAHLERDAGGRLGVCAIDTASGRRVAHRAAERFPFCSTFKAMLSAAVLAQSVARPGLLQQRVTYGKADLVNYSPVTEKHVGAGMTVAELCEATIQYSDNSAANLLMKLIGGPSAVTAYARSIGDDTFRLDRWETELNTALPGDLRDTTTPAAMAASMRVLTLGDALPAAQRAQLVTWLRGNKVGDKRIRAGVPAGWTVGDKTGTGDYGTTNDAGVVWAPSRAPIVLAVYYTQARADARAKDDVIADVARVVVAAFG DERPJ4F TD Primarily distributed in human lung. DERPJ4F FC This enzyme hydrolyzes beta-lactam. DERPJ4F KD 2: Bacteria DERPJ4F PL 1224: Proteobacteria DERPJ4F CL 28216: Betaproteobacteria DERPJ4F OD 80840: Burkholderiales DERPJ4F FM 119060: Burkholderiaceae DERPJ4F GE 32008: Burkholderia DERPJ4F SP 292: Burkholderia cepacia DENZLGX ID DENZLGX DENZLGX DN Beta-lactamase (blaB) DENZLGX GN ybxI DENZLGX SN Penicillinase; Cephalosporinase; Beta-lactam; ybxI; AIDNDMCJ_13045 DENZLGX UC A0A498U5Y1_BACPU DENZLGX RD Ceftiofur DENZLGX E1 3: Hydrolases DENZLGX E2 3.5: Carbon-nitrogen hydrolase DENZLGX E3 3.5.2: Cyclic amide hydrolase DENZLGX EC 3.5.2.6 DENZLGX SQ MKKKHMKWLFSGLMLMALCIGQPSSSEGTSPAWSVDEFIKDREGTFVIQEVKEKSPWVYNKKRANERFAPQSTFKVANALIGLQTGAVRDEYDIKYWDGVKREIDNWNKDHTLGSGMRDSVVWYYQAMARDIGEERMNHWVKAIHYGNEDISGGIDQFWLSSSLRISPVEQVHFLKQLYEESLPFDLSVMRTVKRMMIQEEEKHATLYGKTGSGSGIGWYVGFIKHENKTYIFATNIEGTGLEAKEITYRILKKYHLIEASV DENZLGX TD Primarily distributed in human gut. DENZLGX FC This enzyme hydrolyzes beta-lactam. DENZLGX KD 2: Bacteria DENZLGX PL 1239: Firmicutes DENZLGX CL 91061: Bacilli DENZLGX OD 1385: Bacillales DENZLGX FM 186817: Bacillaceae DENZLGX GE 1386: Bacillus DENZLGX SP 1408: Bacillus pumilus DE27YVU ID DE27YVU DE27YVU DN VanB ligase (vanB) DE27YVU GN vanB DE27YVU SN Vancomycin B-type resistance protein VanB; D-alanylalanine synthetase VanB; D-alanine--D-alanine ligase VanB; D-Ala-D-Ala ligase VanB; vanB DE27YVU UC Q58F99_ENTFC DE27YVU RD Vancomycin DE27YVU E1 6: Ligase DE27YVU E2 6.3: Carbon-nitrogen ligase DE27YVU E3 6.3.2: Peptide synthase DE27YVU EC 6.3.2.4 DE27YVU SQ MNRIKVAIIFGGCSEEHDVSVKSAIEIAANIDTEKFDPHYIGITKNGVWKLCKKPCTEWEADSLPAILSPDRKTHGLLVMKESEYETRRIDVAFPVLHGKCGEDGAIQGLFVLSGIPYVGCDIQSSAACMDKSLAYILTKNAGIAVPEFQMIDKGDKPEAGALTYPVFVKPARSGSSFGVTKVNGTEELNAAIEAAGQYDGKILIEQAISGCEVGCAVMGNEDDLIVGEVDQIRLSHGIFRIHQENEPEKGSENAMITVPADIPVEERNRVQETAKKVYRVLGCRGLARVDLFLQEDGGIVLNEVNTLPGFTSYSRYPRMMAAAGITLPALIDSLITLALKR DE27YVU TD Primarily distributed in human gut. DE27YVU FC This enzyme is involved with UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase (EC 6.3.2.7) or UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase (EC 6.3.2.13), UDP-N-acetylmuramate---L-alanine ligase (EC 6.3.2.8), UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase (EC 6.3.2.9) and UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase (EC 6.3.2.10) in the synthesis of a cell-wall peptide. DE27YVU KD 2: Bacteria DE27YVU PL 1239: Firmicutes DE27YVU CL 91061: Bacilli DE27YVU OD 186826: Lactobacillales DE27YVU FM 81852: Enterococcaceae DE27YVU GE 1350: Enterococcus DE27YVU SP 1352: Enterococcus faecium DEX542K ID DEX542K DEX542K DN Dipeptidylpeptidase IV (DPP4) DEX542K GN DPP4 DEX542K SN Bacterial dipeptidyl peptidase 4; Adenosine deaminase binding protein; Adenosine deaminase complexing protein; Adenosine deaminase-binding protein; Amino acyl-prolyl dipeptidyl aminopeptidase; Bacterial DPP4; E8L09_04090 DEX542K UC A0A4T2GYT7_STRSU DEX542K RD PR-39 DEX542K E1 3: Hydrolases DEX542K E2 3.4: Peptidase DEX542K E3 3.4.14: Di/tripeptidyl peptidase DEX542K EC 3.4.14.5 DEX542K SQ MKKTFVRIATFLMLVCLFPVQLVQACSGFIIGKGLTTDGSILYGRTEDYPYPPNNGAHNKNYIVVPAATYAKGDMLVDESFGFTAPHLANEFKYTSTPDAARGDGSNGNFGAHGFNEKGVSMTATVTAIPNKKILAVDPLVTAGGLGEAILIDYVLPRVTSAREGIELIAKTIDEKGSAEGNIIVIADKNEVWYMEILSGHQYVAIKFPEDKYAIFANTYYLGHVDFTDTENVIASAKVEEVAKQAENYMMVDGKFHIAKSYGPENYADGDRSRTYAGIKLLDPASSVTYEDAVYDLLRQPTDPSRRFSLQDTFALQRNRFEHLPEFRPDDEAGKVKQGDNGANDQAADATYKYALGNENVIDAHVYQINSSLPSAFGGTVWLGLAQTRNTPYVPFYGIVTDTYEAFKNRSASYDANSWYWTVQNIDKMAISHPELFGTSIQEKWIALEKEWIAAQAALDAQYAGLSEDAAVALAPTVTEATLARSAEIFAQLKAVEAEMMAKIEVVTTPSSSGTETSTSTSQSTSTSDTGGATDTSSSSGTVVSSDKKVTPTNKKGKSNLPSTGEQVSILLVALGVAGILTAIFLHRKKSNKE DEX542K TD Primarily distributed in human blood. DEX542K FC This enzyme cleaves X-proline or X-alanine dipeptides from the N-terminus of polypeptides. DEX542K KD 2: Bacteria DEX542K PL 1239: Firmicutes DEX542K CL 91061: Bacilli DEX542K OD 186826: Lactobacillales DEX542K FM 1300: Streptococcaceae DEX542K GE 1301: Streptococcus DEX542K SP 1307: Streptococcus suis DEVSF75 ID DEVSF75 DEVSF75 DN Cytochrome P450 monooxygenase 51A (cyp51A) DEVSF75 GN cyp51A DEVSF75 SN Sterol 14-alpha demethylase; Ergosterol biosynthesis protein cyp51A; AFUA_4G06890; cyp51A; erg11A DEVSF75 UC CP51A_ASPFU DEVSF75 RD Lanosterol DEVSF75 GI 3509526 DEVSF75 E1 1: Oxidoreductase DEVSF75 E2 1.14: Oxygen paired donor oxidoreductase DEVSF75 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEVSF75 EC 1.14.14.154 DEVSF75 KG Biosynthesis of secondary metabolites:afm01110; Metabolic pathways:afm01100; Steroid biosynthesis:afm00100 DEVSF75 SQ MVPMLWLTAYMAVAVLTAILLNVVYQLFFRLWNRTEPPMVFHWVPYLGSTISYGIDPYKFFFACREKYGDIFTFILLGQKTTVYLGVQGNEFILNGKLKDVNAEEVYSPLTTPVFGSDVVYDCPNSKLMEQKKFIKYGLTQSALESHVPLIEKEVLDYLRDSPNFQGSSGRVDISAAMAEITIFTAARALQGQEVRSKLTAEFADLYHDLDKGFTPINFMLPWAPLPHNKKRDAAHARMRSIYVDIITQRRLDGEKDSQKSDMIWNLMNCTYKNGQQVPDKEIAHMMITLLMAGQHSSSSISAWIMLRLASQPKVLEELYQEQLANLGPAGPDGSLPPLQYKDLDKLPFHQHVIRETLRIHSSIHSIMRKVKSPLPVPGTPYMIPPGRVLLASPGVTALSDEHFPNAGCWDPHRWENQATKEQENDKVVDYGYGAVSKGTSSPYLPFGAGRHRCIGEKFAYVNLGVILATIVRHLRLFNVDGKKGVPETDYSSLFSGPMKPSIIGWEKRSKNTSK DEVSF75 TD Primarily distributed in human lung. DEVSF75 FC This enzyme is involved in the biosynthesis of ergosterol, and as a cytochrome P-450 (heme-thiolate) protein acts on a range of steroids with a 14alpha-methyl group, such as obtusifoliol and lanosterol. And it catalyses a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond. DEVSF75 KD 4751: Fungi DEVSF75 PL 4890: Ascomycota DEVSF75 CL 147545: Eurotiomycetes DEVSF75 OD 5042: Eurotiales DEVSF75 FM 1131492: Aspergillaceae DEVSF75 GE 5052: Aspergillus DEVSF75 SP 746128: Aspergillus fumigatus DE49HWX ID DE49HWX DE49HWX DN CDP-alcohol phosphatidyltransferase (pgsA) DE49HWX GN pgsA DE49HWX SN CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase; pgsA; AXK38_10040; CYK18_09100; D8842_08295; FBF73_01305; SK1126_1848; SK642_1900 DE49HWX UC A0A081Q830_STRMT DE49HWX RD Daptomycin DE49HWX E1 2: Transferase DE49HWX E2 2.7: Kinase DE49HWX E3 2.7.8: Phosphotransferase DE49HWX EC 2.7.8.5 DE49HWX SQ MKKEQIPNLLTIGRILFIPIFIFILTVGNSIESHIVAAIIFAIASITDYLDGYLARKWNVVSNFGKFADPMADKLLVMSAFIMLIELGMAPAWIVAVIICRELAVTGLRLLLVETGGTVLAAAMPGKIKTFSQMFAIIFLLLHWTLIGQVLLYVALFFTIYSGYDYFKGSAYVFKGTFGSK DE49HWX TD Primarily distributed in human oral cavity. DE49HWX FC This enzyme catalyzes the committed step in the biosynthesis of acidic phospholipids known by the common names phophatidylglycerols and cardiolipins. DE49HWX KD 2: Bacteria DE49HWX PL 1239: Firmicutes DE49HWX CL 91061: Bacilli DE49HWX OD 186826: Lactobacillales DE49HWX FM 1300: Streptococcaceae DE49HWX GE 1301: Streptococcus DE49HWX SP 28037: Streptococcus mitis DETRKSD ID DETRKSD DETRKSD DN Carbapenemase (cphA) DETRKSD GN axc DETRKSD SN Versatile beta-lactamase; Versatile hydrolytic beta-lactamase; Beta-lactamase II; Carbapenem-hydrolyzing metallo-beta-lactamase; Metallo-beta-lactamase type 2b; Metallo-beta-lactamase type IIb; axc DETRKSD UC A0A3G1JAD7_ALCXX DETRKSD RD Imipenem DETRKSD E1 3: Hydrolases DETRKSD E2 3.5: Carbon-nitrogen hydrolase DETRKSD E3 3.5.2: Cyclic amide hydrolase DETRKSD EC 3.5.2.6 DETRKSD SQ MLTRRTFIASAVLAGWIPALAHARTDKKTRWTRESLAAFQQGLAQVEAASRGRLGVALLDVGSGQAAGYRADERFLMLSSFKTLSAAYVLARADRGEDQLSRRIPITDADVREYSPVTRLHVGPRGMTLAELCEATITTSDNAAVNLMHKSYGGPQALTRYLRSLGDTVTRHDRYEPELNRPHPSEPQDTTTPQAMARTLDTLLFGDALKPQSRQQLQSWLLANTTGGKRLRAGMPADWKIGEKTGTYSKVGCNDAGFAQPPGAAPIIIAAYLETTAVPMEERDRCIAEVGRLVAALG DETRKSD TD Primarily distributed in human stomach. DETRKSD FC This enzyme hydrolyzes beta-lactam. DETRKSD KD 2: Bacteria DETRKSD PL 1224: Proteobacteria DETRKSD CL 28216: Betaproteobacteria DETRKSD OD 80840: Burkholderiales DETRKSD FM 506: Alcaligenaceae DETRKSD GE 222: Achromobacter DETRKSD SP 85698: Achromobacter xylosoxidans DECWSA9 ID DECWSA9 DECWSA9 DN Beta-lactamase (blaB) DECWSA9 GN ampC DECWSA9 SN Penicillinase; Cephalosporinase; Beta-lactam; PAU_00771; PA-RVA13-1244 DECWSA9 UC AMPC_MORMO DECWSA9 RD Ertapenem DECWSA9 E1 3: Hydrolases DECWSA9 E2 3.5: Carbon-nitrogen hydrolase DECWSA9 E3 3.5.2: Cyclic amide hydrolase DECWSA9 EC 3.5.2.6 DECWSA9 SQ MKKSLSATLISALLAFSAPGFSAADNVAAVVDSTIKPLMAQQDIPGMAVAVSVKGKPYYFNYGFADVQAKQPVTENTLFELGSVSKTFTGVLGAVSVAKKEMTLNDPAEKYQPELALPQWKGITLLDLATYTAGGLPLQVPDAVKSRADLLHFYQQWQPSRKPGDMRLYANSSIGLFGALTANAAGMPYEQLLTARILAPLGLSHTFITVPESAQSQYAYGYKNKKPVRVSPGQLDAESYGVKSASKDMLRWAEMNMEPSRAGNADLEMAMYLAQTRYYKTAAINQGLGWEMYDWPQQKDMIINGVTNEVALQPHPVTDNQVQPYNRASWVHKTGATTGFGAYVAFIPEKQVAIVILANKNYPNTERVKAAQAILSALE DECWSA9 TD Primarily distributed in human gut. DECWSA9 FC This enzyme hydrolyzes beta-lactam with a substrate specificity for cephalosporins. DECWSA9 KD 2: Bacteria DECWSA9 PL 1224: Proteobacteria DECWSA9 CL 1236: Gammaproteobacteria DECWSA9 OD 91347: Enterobacterales DECWSA9 FM 1903414: Morganellaceae DECWSA9 GE 581: Morganella DECWSA9 SP 582: Morganella morganii DE235K6 ID DE235K6 DE235K6 DN Beta-glucosidase (bglA) DE235K6 GN bglH DE235K6 SN Periplasmic beta-glucosidase; Glucan endo-1 3-beta-D-glucosidase; Beta-D-glucosidase; HMPREF0351_10377; bglH DE235K6 UC Q3Y0M8_ENTFD DE235K6 RD Lactulose DE235K6 GI 12999036 DE235K6 E1 3: Hydrolases DE235K6 E2 3.2: Glycosylase DE235K6 E3 3.2.1: O/S-glycosyl compound glycosidase DE235K6 EC 3.2.1.21 DE235K6 KG Glycolysis / Gluconeogenesis:efu00010; Starch and sucrose metabolism:efu00500 DE235K6 SQ MDQEIFPENFLWGGAVAANQCEGAWLEDGKLPNVTDTLIGIMNQHPSIQWNEEKKIWEIALDESLHYLSHEAIDFYHRFEEDIRLLKELGLKAFRTSISWARIFPRGDEQKPNEAGLVFYDRLINTLNRYDIEPVITLSHYETPLALVGEYGGWQNRKLIDFFEFYAQTVFERYQGKVKYWMTFNEINNAFRMPYAAAGLVTFPARDKLEPIATLTKKVIYQACHHMFLANARATQLLKKIDPNAKMGIMCSFSALATYAYDCDPENVFGSLQFKRNSWFFSDVMCRGHYPAYIYRTWKEEDCAPVMLDGDEQCLQANTADYIAFSYYRSAVYKKEAEMRVDTGGANGFDNPFLKEKSPEPWSWPIDPLGFRYVMNELTDRYELPLFIVENGIGLDEAPDELNRIHDPKRCEYLKIHLQEIAEAIKDGCQIIGYLWWGPIDIVSAGTGEMRKRYGFIYVDRQNDGSGSFRRLKKDSFEYYKQIIQSNGKNLEYRSFFK DE235K6 TD Primarily distributed in human gut. DE235K6 FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DE235K6 KD 2: Bacteria DE235K6 PL 1239: Firmicutes DE235K6 CL 91061: Bacilli DE235K6 OD 186826: Lactobacillales DE235K6 FM 81852: Enterococcaceae DE235K6 GE 1350: Enterococcus DE235K6 SP 1352: Enterococcus faecium DEIEY19 ID DEIEY19 DEIEY19 DN Beta-galactosidase (bgaB) DEIEY19 GN lacZ DEIEY19 SN Beta-galactosidase/glucuronidase; Beta-galactosidase BgaBeta; Beta-Gal II; Beta-gal; ESA_02977; Lactase; lacZ DEIEY19 UC BGAL_CROS8 DEIEY19 RD Lactulose DEIEY19 E1 3: Hydrolases DEIEY19 E2 3.2: Glycosylase DEIEY19 E3 3.2.1: O/S-glycosyl compound glycosidase DEIEY19 EC 3.2.1.23 DEIEY19 KG Galactose metabolism:esa00052; Metabolic pathways:esa01100; Other glycan degradation:esa00511; Sphingolipid metabolism:esa00600 DEIEY19 SQ MTENPTTTAFNELQTRPLATILARNDWQNPAITSVNRLPSHTPLHGWRDADRARRGEPSDAVLSLDGEWQFSFFASPHQVPEVWLAADLSDARATPVPSNWQMEGYDTPIYTNVRYPIPVNPPFVPDDNPTGCYSRDIEVPQAWLETGRTRIIFGGVNSAFYLWCNGQWVGYSQDSRLPAEFDLTGVLHAGRNRLCVLVLRWSDGTYLEDQDMWRMSGIFRPVSLLHLPEQALADVRVHTELAPSLRHATLFSEVEVTPAACGLSVTLALWHGENEIASQTLPLGSAPIDERGNYAERVTLSLDVDNPLLWSAETPHLYRAVVTLLDADGMPLVSEAHDVGFRRVEINNGLLTLNGQPLLIRGVNRHEHHPEKGQAVDEAAMVQDILLMKQNNFNAVRCSHYPNQPRWYELCSRYGLYVVDEANIETHGMEPMSRLSDDPVWLGAYSERVTRMVKCNRNHPSIIIWSLGNESGNGATHTALYNWIKHQDPTRPVQYEGGGADTRATDIICPMYARVETDQLIPAVPKWSIKKWISMPGETRPLILCEYAHAMGNSLGNFADYWAAFRQYPRLQGGFIWDWADQAITRVEPDGSRWWAYGGDFGDTPNDRQFCMNGLVFPDRTPHPALFEAKHQQQFFQFRLVSENPLQIEVTSEYLFRESDNERLLWSIEVRGETRLSGELTLELGPQASRVLTLSDTGFSARAGDEEIWLHVRVEQPQATPWSPEGHLSAWAQWPLAAPLALPEPVAAGDAPQLEITDAEFVIRHGCQTWRVSRASGQLIQWSDDGVDQILTPLADQFIRAPIDNDIGVSEVERIDPNAWVERWKAAGLYNTEHRCLACDAQTTRDGVEIVAQHAYFVKGVADGPAILSRWRMVVDNQGALHCDIDIARSAALPPLPRVGVVCQLRGGEETASWLGLGPHENYPDRLSSACFSRWTLPLSELTTPYIFPGENGLRCNTRELNWNGWQAEGEFHFSLSPYGTRQLMETSHWHKLQPEAGIWLTIDGFHMGVGGDDSWTPSVHPEYLLTAREYRYRFTLRRRQG DEIEY19 TD Primarily distributed in human gut. DEIEY19 FC This enzyme hydrolyzes alpha-L-arabinoside and beta-D-fucosides and beta-D-glucosides. DEIEY19 KD 2: Bacteria DEIEY19 PL 1224: Proteobacteria DEIEY19 CL 1236: Gammaproteobacteria DEIEY19 OD 91347: Enterobacterales DEIEY19 FM 543: Enterobacteriaceae DEIEY19 GE 413496: Cronobacter DEIEY19 SP 28141: Cronobacter sakazakii DESGYWE ID DESGYWE DESGYWE DN Aminoglycoside O-phosphotransferase (aphA6) DESGYWE GN aphA6 DESGYWE SN Aminoglycoside 3'-phosphotransferase; Kanamycin kinase, type VI; Neomycin-kanamycin phosphotransferase type VI; APH(3')VI; AphA6; aphA-6; aphA6 DESGYWE UC G9FRK8_PROST DESGYWE RD Plazomicin DESGYWE E1 2: Transferase DESGYWE E2 2.7: Kinase DESGYWE E3 2.7.1: Phosphotransferase DESGYWE EC 2.7.1.95 DESGYWE SQ GNSVLEPNKIGQSPSDVYSFNRNNETFFLKRSSTLYTETTYSVSREAKMLSWLSDKLKVPELIMTFQDEQFEFMITKAINAKPISALFLTEQELLAIYKETLNQLNAVAIIDCPFISSIDHRLKESKFFIDNQLLDEIDQDDLDAELWGDHKTYISLWNELNETRVEERLVFSHGDITDSNIFIDKSGEIYFLDLGRAGLADEFVDISFVERCLREDVSEETAKIFLKHLKNDRPDKR DESGYWE TD Primarily distributed in human gut. DESGYWE FC This enzyme acts on the antibiotics neomycin, paromomycin, neamine, paromamine, vistamycin and gentamicin A. DESGYWE KD 2: Bacteria DESGYWE PL 1224: Proteobacteria DESGYWE CL 1236: Gammaproteobacteria DESGYWE OD 91347: Enterobacterales DESGYWE FM 1903414: Morganellaceae DESGYWE GE 586: Providencia DESGYWE SP 588: Providencia stuartii DE69QHT ID DE69QHT DE69QHT DN Aminoglycoside acetyltransferase (aac) DE69QHT GN aac DE69QHT SN Aminoglycoside 2'-N-acetyltransferase; AAC(2')-Ia; aac DE69QHT UC AAC2_PROST DE69QHT RD Plazomicin DE69QHT GI 31518288 DE69QHT E1 2: Transferase DE69QHT E2 2.3: Acyltransferase DE69QHT E3 2.3.1: Acyltransferase DE69QHT EC 2.3.1.59 DE69QHT PD 5US1 DE69QHT SQ MGIEYRSLHTSQLTLSEKEALYDLLIEGFEGDFSHDDFAHTLGGMHVMAFDQQKLVGHVAIIQRHMALDNTPISVGYVEAMVVEQSYRRQGIGRQLMLQTNKIIASCYQLGLLSASDDGQKLYHSVGWQIWKGKLFELKQGSYIRSIEEEGGVMGWKADGEVDFTASLYCDFRGGDQW DE69QHT TD Primarily distributed in human gut. DE69QHT FC This enzyme catalyzes the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. DE69QHT KD 2: Bacteria DE69QHT PL 1224: Proteobacteria DE69QHT CL 1236: Gammaproteobacteria DE69QHT OD 91347: Enterobacterales DE69QHT FM 1903414: Morganellaceae DE69QHT GE 586: Providencia DE69QHT SP 588: Providencia stuartii DE86CHA ID DE86CHA DE86CHA DN Xylose isomerase (xylA) DE86CHA GN xylA DE86CHA SN Xylose isomerase xylA; Isomerase xylA; Enzyme xylA; xylA; BAD_0422 DE86CHA UC XYLA_BIFAA DE86CHA RD Xylose DE86CHA GI 4556760 DE86CHA E1 5: Isomerase DE86CHA E2 5.3: Intramolecular oxidoreductase DE86CHA E3 5.3.1: Aldose/ketose isomerase DE86CHA EC 5.3.1.5 DE86CHA KG Fructose and mannose metabolism:bad00051; Metabolic pathways:bad01100; Pentose and glucuronate interconversions:bad00040 DE86CHA SQ MGLWDIDKIPYVGREKGPQEGLAFHYYDADKVVAGKKMKDWLRFGVAWWHTFDQQLVDPFGTGTAQRPWYGKYSDPEDEALAKVDYAFEFFQKLGVEYFCFHDRDIAPEGDTLRETDKNLDKVVDKIEENMKSTGIKLLWNTSSLFTNPRFVSGASTSPFADIYAYAGGQLKHSLEIAKRLGAENYVFWGGREGYENLWNTQMKREQEHMAKFFHMCHDYAKEIGLDAQFLIEPKAKEPTMFQYDFDAATAINFLRTYDLMDVFKLNLEGNHANLAGHTYQHEIRTAREAGVLGSLDANQGDKLIGWDMDEFPTDLYETSTVMWEVLAEGQIGPHGGLNFDAKPRRTSFTAEDLFRSHIAGMDSFAAGLLVAAKMHEDKVIENLQAERYSSFDSGIGATVENGTASLASLEEYALDIPQSKLIEATKSDHLESVKATINNYMIDALAEA DE86CHA TD Primarily distributed in human gut. DE86CHA FC This enzyme catalyzes the interconversion of aldose and ketose sugars with broad substrate specificity. It binds the closed form of its sugar substrate (in the case of glucose, only the alpha anomer) and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. DE86CHA KD 2: Bacteria DE86CHA PL 201174: Actinobacteria DE86CHA CL 1760: Actinobacteria DE86CHA OD 85004: Bifidobacteriales DE86CHA FM 31953: Bifidobacteriaceae DE86CHA GE 1678: Bifidobacterium DE86CHA SP 1680: Bifidobacterium adolescentis DEPN8F9 ID DEPN8F9 DEPN8F9 DN VanG ligase (vanG) DEPN8F9 GN vanG DEPN8F9 SN Vancomycin G-type resistance protein VanG; D-alanylalanine synthetase VanG; D-alanine--D-alanine ligase VanG; D-Ala-D-Ala ligase VanG; vanG DEPN8F9 UC A0A076YRI6_STRAG DEPN8F9 RD Vancomycin DEPN8F9 E1 6: Ligase DEPN8F9 E2 6.3: Carbon-nitrogen ligase DEPN8F9 E3 6.3.2: Peptide synthase DEPN8F9 EC 6.3.2.4 DEPN8F9 SQ MQNKKIAVIFGGNSTEYEVSLQSASAVFENINTNKFDIIPIGITRSGEWYHYTGEKEKILNNTWFEDSKNLCPVVVSQNRSVKGFLEIASDKYRIIKVDLVFPVLHGKNGEDGTLQGIFELAGIPVVGCDTLSSALCMDKDRAHKLVSLAGISVPKSVTFKRFNEEAAMKEIEANLTYPLFIKPVRAGSSFGITKVIEKQELDAAIELAFEHDTEVIVEETINGFEVGCAVLGIDELIVGRVDEIELSSGFFDYTEKYTLKSSKIYMPARIDAEAEKRIQEAAVTIYKALGCSGFSRVDMFYTPSGEIVFNEVNTIPGFTSHSRYPNMMKGIGLSFSQMLDKLIGLYVE DEPN8F9 TD Primarily distributed in human gut. DEPN8F9 FC This enzyme is involved with UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---L-lysine ligase (EC 6.3.2.7) or UDP-N-acetylmuramoyl-L-alanyl-D-glutamate---2,6-diaminopimelate ligase (EC 6.3.2.13), UDP-N-acetylmuramate---L-alanine ligase (EC 6.3.2.8), UDP-N-acetylmuramoyl-L-alanine---D-glutamate ligase (EC 6.3.2.9) and UDP-N-acetylmuramoyl-tripeptide---D-alanyl-D-alanine ligase (EC 6.3.2.10) in the synthesis of a cell-wall peptide. DEPN8F9 KD 2: Bacteria DEPN8F9 PL 1239: Firmicutes DEPN8F9 CL 91061: Bacilli DEPN8F9 OD 186826: Lactobacillales DEPN8F9 FM 1300: Streptococcaceae DEPN8F9 GE 1301: Streptococcus DEPN8F9 SP 1311: Streptococcus agalactiae DEIF4P9 ID DEIF4P9 DEIF4P9 DN VanC2 ligase (vanC) DEIF4P9 GN vanC DEIF4P9 SN Vancomycin C-type resistance protein VanC; VanC ligase; vanC DEIF4P9 UC VANC_ENTGA DEIF4P9 RD Vancomycin DEIF4P9 E1 6: Ligase DEIF4P9 E2 6.3: Carbon-nitrogen ligase DEIF4P9 E3 6.3.2: Peptide synthase DEIF4P9 EC 6.3.2.4 DEIF4P9 SQ MKKIAVLFGGNSPEYSVSLTSAASVIQAIDPLKYEVMTIGIAPTMDWYWYQGNLANVRNDTWLEDHKNCHQLTFSSQGFILGEKRIVPDVLFPVLHGKYGEDGCIQGLLELMNLPYVGCHVAASALCMNKWLLHQLADTMGIASAPTLLLSRYENDPATIDRFIQDHGFPIFIKPNEAGSSKGITKVTDKTALQSALTTAFAYGSTVLIQKAIAGIEIGCGILGNEQLTIGACDAISLVDGFFDFEEKYQLISATITVPAPLPLALESQIKEQAQLLYRNLGLTGLARIDFFVTNQGAIYLNEINTMPGFTGHSRYPAMMAEVGLSYEILVEQLIALAEEDKR DEIF4P9 TD Primarily distributed in human gut. DEIF4P9 FC This enzyme is required for low-level resistance to the glycopeptide antibiotic vancomycin and it may synthesize a dipeptide or a depsipeptide which is incorporated into peptidoglycan precursors and not recognized by vancomycin. DEIF4P9 KD 2: Bacteria DEIF4P9 PL 1239: Firmicutes DEIF4P9 CL 91061: Bacilli DEIF4P9 OD 186826: Lactobacillales DEIF4P9 FM 81852: Enterococcaceae DEIF4P9 GE 1350: Enterococcus DEIF4P9 SP 1353: Enterococcus gallinarum DEIF4P9 SU Enterococcus gallinarum BM4174 DEIZ2D9 ID DEIZ2D9 DEIZ2D9 DN Tripeptidase (pepT) DEIZ2D9 GN pepT DEIZ2D9 SN Aminotripeptidase; Tripeptide aminopeptidase; Peptidase T; L9PepTR; pepT DEIZ2D9 UC PEPT_LACLL DEIZ2D9 RD Glypromate DEIZ2D9 E1 3: Hydrolases DEIZ2D9 E2 3.4: Peptidase DEIZ2D9 E3 3.4.11: Aminopeptidase DEIZ2D9 EC 3.4.11.4 DEIZ2D9 SQ MKYEKLLPRFLEYVKVNTRSDENSTTTPSTQALVEFAHKMGEDMKALGLKDVHYLESNGYVIGTIPANTDKKVRKIGLLAHLDTADFNAEGVNPQILENYDGESVIKLGDTEFTLDPKDFPNLKNYKGQTLVHTDGTTLLGSDDKSGVAEIMTLADYLLNINPDFEHGEIRVGFGPDEEIGVGADKFDVADFDVDFAYTVDGGPLGELQYETFSAAGAVIEFQGKNVHPGTAKNTMVNALQLAIDYHNALPEFDRPEKTEGREGFFHLLKLDGTPEEARAQYIIRDHEEGKFNERKALMQEIADKMNAELGQNRVKPVIKDQYYNMAQIIEKDMSIIDIAKKAMENLDIVPIIEPIRGGTDGSKISFMGLPTPNLFAGGENMHGRFEFVSVQTMEKAVDTLLEIIRLNNEVVK DEIZ2D9 TD Primarily distributed in human gut. DEIZ2D9 FC This enzyme catalyzes release of the N-terminal residue from a tripeptide. DEIZ2D9 KD 2: Bacteria DEIZ2D9 PL 1239: Firmicutes DEIZ2D9 CL 91061: Bacilli DEIZ2D9 OD 186826: Lactobacillales DEIZ2D9 FM 1300: Streptococcaceae DEIZ2D9 GE 1357: Lactococcus DEIZ2D9 SP 1358: Lactococcus lactis DEIZ2D9 SU Lactococcus lactis subsp. lactis (L9); Lactococcus lactis subsp. hordniae (hT); Lactococcus lactis subsp. cremoris (L6) DEJ4FO2 ID DEJ4FO2 DEJ4FO2 DN Sucrose phosphorylase (Spase) DEJ4FO2 GN treY DEJ4FO2 SN Sucrose glucosyltransferase; Glucosyltransferase-A; SPase; GTF-A; SP; treY; BBG7_0104; CE169_10215 DEJ4FO2 UC A0A0M4N1J6_BIFLN DEJ4FO2 RD Kestose DEJ4FO2 E1 2: Transferase DEJ4FO2 E2 2.4: Glycosyltransferases DEJ4FO2 E3 2.4.1: Hexosyltransferase DEJ4FO2 EC 2.4.1.7 DEJ4FO2 SQ MKNKVQLITYADRLGDGTLSSMTDILRTRFDGVYDGVHILPFFTPFDGADAGFDPIDHTKVDERLGSWDDVAELSKTHNIMVDAIVNHMSWESKQFQDVLEKGEESEYYPMFLTMSSVFPNGATEEDLAGIYRPRPGLPFTHYNLGGKTRLVWVSFTPQQVDIDTDSAKGWEYLMSIFDQMAASHVRYIRLDAVGYGAKEAGTSCFMTPKTFKLISRLREEGVKRGLEILIEVHSYYKKQVEIASKVDRVYDFALPPLLLHSLFTGHVEPVAHWTEIRPNNAVTVLDTHDGIGVIDIGSDQLDRSLKGLVPDEDVDNLVNTIHANTHGESQAATGAAASNLDLYQVNSTYYSALGCNDQHYLAARAVQFFLPGVPQVYYVGALAGRNDMELLRRTNNGRDINRHYYSTAEIDENLERPVVKALNALAKFRNELSAFDGEFSYEVDGDTSITFRWTAADGASTAALTFEPGRGLGTDNATPVASLAWSDAAGDHETHDLLANPPIADID DEJ4FO2 TD Primarily distributed in human oral cavity. DEJ4FO2 FC This enzyme catalyzes the conversion of sucrose to D-fructose and alpha-D-glucose-1-phosphate. DEJ4FO2 KD 2: Bacteria DEJ4FO2 PL 201174: Actinobacteria DEJ4FO2 CL 1760: Actinobacteria DEJ4FO2 OD 85004: Bifidobacteriales DEJ4FO2 FM 31953: Bifidobacteriaceae DEJ4FO2 GE 1678: Bifidobacterium DEJ4FO2 SP 216816: Bifidobacterium longum DE4IPGZ ID DE4IPGZ DE4IPGZ DN Sucrose phosphorylase (Spase) DE4IPGZ GN gtfA DE4IPGZ SN Sucrose glucosyltransferase; Glucosyltransferase-A; SPase; GTF-A; SP; treY; D7H66_05705; gtfA DE4IPGZ UC Q7WWQ5_LACAI DE4IPGZ RD Raffinose DE4IPGZ E1 2: Transferase DE4IPGZ E2 2.4: Glycosyltransferases DE4IPGZ E3 2.4.1: Hexosyltransferase DE4IPGZ EC 2.4.1.7 DE4IPGZ KG Metabolic pathways:laf01100; Starch and sucrose metabolism:laf00500 DE4IPGZ SQ MKLQNKAILITYPDSLGHNLKDLDHVMDRYFNKTIGGIHLLPFFPSNGDRGFSPTRYDVVEPKFGSWEDVEKLSQKYYLMFDFMINHLSKKSSYFEDFEAKHDKSKYSDLFLSWDKFWPKGRPTKEDIDLIYKRKDKAPYQNIKFEDGTHEKMWNTFGPDQMDLDVRTKTTQDFIKHNLQNLSKHGASLIRLDAFAYAIKKLDTNDFFVEPEIWNLLEKVNDYLKDTPTTILPEIHEHYTMPFKVAEHGYFIYDFALPMVLLYSLYSGNSTQLAAWLKKCPMKQFTTLDTHDGLGVVDAKDILTDDQISYTTNELYKIGANVKKKYSSAEYHNLDIYQINTTYYSALGNDDKKYFIARLLQIFAPGIPQIYYVGLLAGENDIQLLEKTKEGRDINRHYYDLDEIAEQVQRPVVKSLIKLLEFRNSVPAFDLEGSIKVETPSEHEIIVTRSNKAGTEVASTYVDFKNLDYQVKYNDQVFNF DE4IPGZ TD Primarily distributed in human gut. DE4IPGZ FC This enzyme catalyzes the conversion of sucrose to D-fructose and alpha-D-glucose-1-phosphate. DE4IPGZ KD 2: Bacteria DE4IPGZ PL 1239: Firmicutes DE4IPGZ CL 91061: Bacilli DE4IPGZ OD 186826: Lactobacillales DE4IPGZ FM 33958: Lactobacillaceae DE4IPGZ GE 1578: Lactobacillus DE4IPGZ SP 1579: Lactobacillus acidophilus DEKVGPX ID DEKVGPX DEKVGPX DN Retro-nitroreductase (rNR) DEKVGPX GN rNR DEKVGPX SN Retro-FMN reductase (NAD(P)H); Retro-FMN reductase NADPH; ECL_03157 DEKVGPX UC A0A0H3CM55_ENTCC DEKVGPX RD AI3-23606 DEKVGPX GI 9125636 DEKVGPX E1 1: Oxidoreductase DEKVGPX E2 1.5: CH-NH donor oxidoreductase DEKVGPX E3 1.5.1: NAD/NADP acceptor oxidoreductase DEKVGPX EC 1.5.1.34 DEKVGPX KG Microbial metabolism in diverse environments:enc01120; Nitrotoluene degradation:enc00633 DEKVGPX SQ MDIISVALKRHSTKAFDPAKKLTADEAEKIKTLLQYSPSSTNSQPWHFIVASTEEGKARVAKSAAGTYVFNERKMLDASHVVVFCAKTAMDDAWLERVVDQEEADGRFNTPEAKAANHKGRTYFADMHRVDLKDDDQWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDEEFGLKEKGFTSLVVVPVGHHSVEDFNATLPKSRLPLSTIVTEC DEKVGPX TD Primarily distributed in human gut. DEKVGPX FC This enzyme uses NADH as source of reducing equivalents to reduce of a variety of nitroaromatic compounds. DEKVGPX KD 2: Bacteria DEKVGPX PL 1224: Proteobacteria DEKVGPX CL 1236: Gammaproteobacteria DEKVGPX OD 91347: Enterobacterales DEKVGPX FM 543: Enterobacteriaceae DEKVGPX GE 547: Enterobacter DEKVGPX SP 550: Enterobacter cloacae DE6QXYP ID DE6QXYP DE6QXYP DN Pyruvate oxidase (pyrO) DE6QXYP GN pyrO DE6QXYP SN Pyruvate dehydrogenase; Pyruvic oxidase; POX; AAW28_13255; AUQ39_11915 DE6QXYP UC A0A0H0YI92_LACCA DE6QXYP RD DB-053072 DE6QXYP E1 1: Oxidoreductase DE6QXYP E2 1.2: Aldehyde/oxo donor oxidoreductase DE6QXYP E3 1.2.3: Oxygen acceptor oxidoreductase DE6QXYP EC 1.2.3.3 DE6QXYP SQ MATKAADQLVSVLMDWQVKHVFGLPGDSIDTTVDALRRHQDKIKFVQVRHEEVAALAASATAKLTGGLGVCLSIGGPGAIHLLNGLYDAKMDHAPVLALLGQVTTSNLNEGFFQEVNTPKLFDDVAVYNKTVMASDNLGQIVDTAIRTAFTEKGVAVLTIPDDLPDQKETTSYRDSAAAFALNVPEVDPKQLDDVASLLQKSQKPLALIGRGAEHAGEQVQKFVEANHIPFIQTMPAKGTVADDHPNSLGNVGKLGTKPAYEAMKATDLLFMIGTNYPYTPYLPDEGQAKCVQIDTQPENLGKRYSVDVAVDGDVETFLTELNAKGSLRDDDRFLKACQKNMESWDKWMAEKRLLTTNPASPEAVFATIDQTAPKDAVYSVDVGTSTSWGARFLNVQPTQKYTISAWLGTMGCGLPGAIAGAEAFPKRQNISVAGDGAFAMVMQDFVTAVKYKLPIIMVVLNNQKLAFIEYEQQSAGQLNYEIDLADMDYAKIAEAAGGVGYTAHSNDEFKEALTKAYQETEKPVLINTYVQDDAPLPGKIVGEEAKGYMKYGSQYLENYWKIPSMPPLKDIMRQFF DE6QXYP TD Primarily distributed in human gut. DE6QXYP FC This enzyme is a flavoprotein (FAD) requiring thiamine diphosphate. Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. DE6QXYP KD 2: Bacteria DE6QXYP PL 1239: Firmicutes DE6QXYP CL 91061: Bacilli DE6QXYP OD 186826: Lactobacillales DE6QXYP FM 33958: Lactobacillaceae DE6QXYP GE 1578: Lactobacillus DE6QXYP SP 1582: Lactobacillus casei DEXCHR2 ID DEXCHR2 DEXCHR2 DN Phosphotransferase enzyme strB (strB) DEXCHR2 GN strB DEXCHR2 SN Streptomycin phosphotransferase strB; Bacterial phosphotransferase strB; strB DEXCHR2 UC Q57204_ERWAM DEXCHR2 RD Streptomycin DEXCHR2 E1 2: Transferase DEXCHR2 E2 2.7: Kinase DEXCHR2 E3 2.7.3: Phosphotransferase DEXCHR2 EC 2.7.3.9 DEXCHR2 SQ MFMPPVFPAHWHVSQPVLIADTFSSLVWKVSLPDGTPAIVKGLKPIEDIADELRGADYLVWRNGRGAVRLLGRENNLMLLEYAGERMLSHIVAEHGDYQATEIAAELMAKLYAASEEPLPSALLPIRDRFAALFQRARDDQNAGCQTDYVHAAIIADQMMSNASELRGLHGDLHHENIMFSSRGWLVIDPVGLVGEVGFGAANMFYDPADRDDLCLDPRRIAQMADAFSRALDVDPRRLLDQAYAYGCLSAAWNADGEEEQRDLAIAAAIKQVRQTSY DEXCHR2 TD Primarily distributed in human gut. DEXCHR2 FC This enzyme is enzyme I of the phosphotransferase system, and it acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. DEXCHR2 KD 2: Bacteria DEXCHR2 PL 1224: Proteobacteria DEXCHR2 CL 1236: Gammaproteobacteria DEXCHR2 OD 91347: Enterobacterales DEXCHR2 FM 1903409: Erwiniaceae DEXCHR2 GE 551: Erwinia DEXCHR2 SP 552: Erwinia amylovora DEI2XLV ID DEI2XLV DEI2XLV DN Phosphoenolpyruvate carboxykinase (pckG) DEI2XLV GN pckG DEI2XLV SN GTP-dependent phosphoenolpyruvate carboxykinase; PEP carboxykinase; GTP-PEPCK; PEPCK; SAMN04487832_102103; pckG DEI2XLV UC A0A1K1UGV6_RUMFL DEI2XLV RD FT-0624878 DEI2XLV E1 4: Lyases DEI2XLV E2 4.1: Carbon-carbon lyase DEI2XLV E3 4.1.1: Carboxy-lyase DEI2XLV EC 4.1.1.32 DEI2XLV SQ MSLTKNPNVLKWVDEMVALCKPDNVVWIDGSKEQIDSLIEEVTSLPDDSWDKMYKLNPEKYPNCLYHRTRANDVARVEDRTFICSKEKSGAGPTNNWMAPDEMKALLTPMYDGVMKGRTMYVIPYSMGPIGSPLAKVGVEVTDSIYVVLNMNIMTRMGKQAFENLGDTSDDFVRGLHSKADVDPEKRYIVQFPEENTIWSINSAYGGNVLLGKKCFALRIASFQGKNEAWMAEHMLILGVKKPNGDVKYITAAFPSACGKTNLAMLIPPEGYKKEGYEVFTVGDDIAWMKPGKDGRLYAINPENGFFGVAPGTNEKSNYNALACTKNGAIFTNVALDNSDNTPWWEKLTENPPKDATEWKGEKVDGEAYTAAGNKLAHPNSRFTAPAQNCPCISPEFNNPEGVPVSAIIFGGRRATTAPLVYQSFDWTHGTYIGSAVSSETTAAATGAVGVLRHDPMAMKPFIGYNVGDYWAHWLEMGARLGSKAPKIFNVNWFRTDDEGNFLWPGFGDNMRVIDWIIKRVENEVDAVETPIGYLPKPEDINLKGIEDEVSADALKLLLTVNKDEWKKEIAEMRRYYDEDIKAKGGNIPQALYDELDMIEANLNK DEI2XLV TD Primarily distributed in human gut. DEI2XLV FC This enzyme catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. DEI2XLV KD 2: Bacteria DEI2XLV PL 1239: Firmicutes DEI2XLV CL 186801: Clostridia DEI2XLV OD 186802: Clostridiales DEI2XLV FM 541000: Ruminococcaceae DEI2XLV GE 1263: Ruminococcus DEI2XLV SP 1265: Ruminococcus flavefaciens DEFKVZD ID DEFKVZD DEFKVZD DN Phospho-beta-glucosidase (LBA1706) DEFKVZD GN LBA1706 DEFKVZD SN Beta-glucosidase phospho; 6-phospho-beta-glucosidase; LBA1706 DEFKVZD UC Q5FIF6_LACAC DEFKVZD RD Salicin DEFKVZD GI 3251293 DEFKVZD E1 3: Hydrolases DEFKVZD E2 3.2: Glycosylase DEFKVZD E3 3.2.1: O/S-glycosyl compound glycosidase DEFKVZD EC 3.2.1.86 DEFKVZD KG Glycolysis / Gluconeogenesis:lac00010; Starch and sucrose metabolism:lac00500 DEFKVZD SQ MNTYHVPHVFLWGVATSANQVEGAWNEEGKGISIADCERFNPNQDLDDYRKVNDMTTAEIESAMQDKSSKSWGKRHGVDFYHYYQSDLELLAKMGINSMRTSIAWSRIFPNGDDARPNQKGLEFYDRLFTKMHELGIQPVVTLSHYEMPLNLVLNYDSWYDPKIIDYFYRFSKTVIDRYHDKVKYWLPINEIDSIIRHPYSSAGLVEDRFPNKNFKEVIYQSMHHQFVAAAKVTKYIHENYLGHKVGSMITSTMVYPYNSDPRNMLKATQIMRESYNFSDVQLRGKYPQVLLKQMMEMGIHVKMSDKDLQLIKENTADFVAFSYYSSICTAHDTEGLQITKANRTIGVYNKYLPTSEWGWQIDPVGLRLIMINLYDRYQKPVFIVENGLGARDRLTYDFKIHDQYRIDYLRAHINEMLRSLTEDGIELMGYMIWGTTDMVSASTTQMSKRYGLIYVDLDDEGKGTCKRYLKDSYYWYQKLLSFKADIPVDYLN DEFKVZD TD Primarily distributed in human gut. DEFKVZD FC This enzyme hydrolyzes several other phospho-beta-D-glucosides, but not their non-phosphorylated forms. DEFKVZD KD 2: Bacteria DEFKVZD PL 1239: Firmicutes DEFKVZD CL 91061: Bacilli DEFKVZD OD 186826: Lactobacillales DEFKVZD FM 33958: Lactobacillaceae DEFKVZD GE 1578: Lactobacillus DEFKVZD SP 1579: Lactobacillus acidophilus DEQ3EWA ID DEQ3EWA DEQ3EWA DN Maltose phosphorylase (malP) DEQ3EWA GN malP DEQ3EWA SN Glycoside hydrolase 65 protein; Glycoside hydrolase family 65; Glycoside hydrolase family 65 protein; Kojibiose phosphorylase; LbDm2_0970 DEQ3EWA UC A0A0C1MAP6_LACBR DEQ3EWA RD Ortho-phosphate DEQ3EWA E1 2: Transferase DEQ3EWA E2 2.4: Glycosyltransferases DEQ3EWA E3 2.4.1: Hexosyltransferase DEQ3EWA EC 2.4.1.8 DEQ3EWA SQ MKRIFEVQPWNVITHTFDPKDKRLQESMTSLGNGYMGMRGDFEEGYSGDSLQGIYLGGVWYPDKTRVGWWKNGYPKYFGKVVNAVNFIKLPIEINGEPVDLAKDKISDFTLDLDMHQGVLNRSFVVERGAVRVALNFQRFLSVAQPELSVQKVTVKNLSDAEVDVTLKPSIDADVMNEEANYDERFWDVLATDQQADRGSIVAKTTPNPFGTPRFTSGMEMRLVTDLKNVAITQPNEKEVTTAYTGKLAPQASAELEKRVIVVTSRDYDTQESLTAAMHQLSDKVAQSSYEDLLNAHTAIWAQRWEKSDVVIQGDDESQQGIRFNLFQLFSTYYGDDARLNIGPKGFTGEKYGGATYWDTEAFAFPVYLGITDPKVTRNLLMYRYKQLDGAYINAQEQGLKGALFPMVTFDGIECHNEWEITFEEIHRNGDIAFAIYNYTRYTGDDSYVLHEGAKVLTEISRFWADRVHFSKRNNQYMIHGVTGADEYENNVDNNWDTNMLAQWTLKYTLEILGKVDQDTAKQLDVSDEEKTKWQDIVDRMYLPYDKDLNIFVQHDGFLDKDIEPVSSIPADQRPINQNWSWDKILRSPYIKQGDVLQGIWDFIDDYTPEQKKANFDFYEPLTVHESSLSPAIHSVLAADLHYEDKAVELYSRTARLDLDNYNNDTTDGLHITAMTGGWIAVVQGFAGMRVRDGQLHYAPFLPKTWTSYTFRQVFRDRLIEVSVHADGPHFKLLSGEPLTIDVAGEKVELTQNVTA DEQ3EWA TD Primarily distributed in human gut. DEQ3EWA FC This enzyme catalyzes the conversion of maltose to D-glucose and beta-D-glucose 1-phosphate. DEQ3EWA KD 2: Bacteria DEQ3EWA PL 1239: Firmicutes DEQ3EWA CL 91061: Bacilli DEQ3EWA OD 186826: Lactobacillales DEQ3EWA FM 33958: Lactobacillaceae DEQ3EWA GE 1578: Lactobacillus DEQ3EWA SP 1580: Lactobacillus brevis DESR17C ID DESR17C DESR17C DN L-Lactate dehydrogenase (ldh) DESR17C GN ldh DESR17C SN L-lactate ferricytochrome C oxidoreductase; Cytochrome b2 mitochondrial; L-LCR; L-LDH; ldh DESR17C UC LDH_LACCA DESR17C RD DB-053072 DESR17C GI 31583240 DESR17C E1 1: Oxidoreductase DESR17C E2 1.1: CH-OH donor oxidoreductase DESR17C E3 1.1.1: NAD/NADP oxidoreductase DESR17C EC 1.1.1.27 DESR17C PD 1LLC; 2ZQY; 2ZQZ; 6J9S; 6J9T; 6J9U DESR17C SQ MASITDKDHQKVILVGDGAVGSSYAYAMVLQGIAQEIGIVDIFKDKTKGDAIDLSNALPFTSPKKIYSAEYSDAKDADLVVITAGAPQKPGETRLDLVNKNLKILKSIVDPIVDSGFNGIFLVAANPVDILTYATWKLSGFPKNRVVGSGTSLDTARFRQSIAEMVNVDARSVHAYIMGEHGDTEFPVWSHANIGGVTIAEWVKAHPEIKEDKLVKMFEDVRDAAYEIIKLKGATFYGIATALARISKAILNDENAVLPLSVYMDGQYGLNDIYIGTPAVINRNGIQNILEIPLTDHEEESMQKSASQLKKVLTDAFAKNDIETRQ DESR17C TD Primarily distributed in human gut. DESR17C FC This enzyme catalyzes the conversion of lactate to pyruvate, and it also oxidizes other (S)-2-hydroxymonocarboxylic acids. DESR17C KD 2: Bacteria DESR17C PL 1239: Firmicutes DESR17C CL 91061: Bacilli DESR17C OD 186826: Lactobacillales DESR17C FM 33958: Lactobacillaceae DESR17C GE 1578: Lactobacillus DESR17C SP 1582: Lactobacillus casei DESR17C SU Lactobacillus casei ATCC 393 DE5DTYB ID DE5DTYB DE5DTYB DN L-Lactate dehydrogenase (ldh) DE5DTYB GN ldh DE5DTYB SN L-lactate ferricytochrome C oxidoreductase; Cytochrome b2 mitochondrial; L-LCR; L-LDH; LBUL_0100 DE5DTYB UC LDH_LACDB DE5DTYB RD DB-053072 DE5DTYB E1 1: Oxidoreductase DE5DTYB E2 1.1: CH-OH donor oxidoreductase DE5DTYB E3 1.1.1: NAD/NADP oxidoreductase DE5DTYB EC 1.1.1.27 DE5DTYB KG Biosynthesis of secondary metabolites:lbu01110; Cysteine and methionine metabolism:lbu00270; Glycolysis / Gluconeogenesis:lbu00010; Metabolic pathways:lbu01100; Microbial metabolism in diverse environments:lbu01120; Propanoate metabolism:lbu00640; Pyruvate metabolism:lbu00620 DE5DTYB SQ MSRKVLLVGDGAVGSNFANDLLQTTQVDELVICDLNKDRAAGDCLDLEDMTYFTGQTKLRAGDYSDAADADVVVITAGVPRKPGESRLDLIKKNEAILRSIVDPVVASGFSGIFVVSANPVDILTTLTQKLSGFPKKRVIGTGTSLDSARLRVELAKRLQVPIESVNAWVLGEHGDSSFENFSSAVVNGKPLLDYPGMTEAALDEIEAHVREKGSEIIVKKGATYYGVAMMLAKIVTAILENNDLALPLSAPLHGEYGIKDEIYLGTLAIINGQGISHVLELPLNDSELAKMRASAATIKATLDSLG DE5DTYB TD Primarily distributed in human gut. DE5DTYB FC This enzyme catalyzes the conversion of lactate to pyruvate, and it also oxidizes other (S)-2-hydroxymonocarboxylic acids. DE5DTYB KD 2: Bacteria DE5DTYB PL 1239: Firmicutes DE5DTYB CL 91061: Bacilli DE5DTYB OD 186826: Lactobacillales DE5DTYB FM 33958: Lactobacillaceae DE5DTYB GE 1578: Lactobacillus DE5DTYB SP 1584: Lactobacillus delbrueckii DE5DTYB SU Lactobacillus delbrueckii subsp. bulgaricus DEWD860 ID DEWD860 DEWD860 DN Linoleate 10-hydratase (10-LAH) DEWD860 GN 10-LAH DEWD860 SN Linoleate hydratase; Oleate hydratase; Hydratase oleate; OA hydratase; Ohase; ohyA DEWD860 UC A0A1I9RYU9_LACPN DEWD860 RD Unifac-6550 DEWD860 E1 4: Lyases DEWD860 E2 4.2: Carbon-oxygen lyase DEWD860 E3 4.2.1: Hydro-lyase DEWD860 EC 4.2.1.84 DEWD860 SQ MVKSKAIMIGAGLSNMAAAVYLIQDGHWDGKDITFYGVDMHGANDGGATTDFTNEYWNKNHPMANTTGYVARGGRMLNYRTYVDLMDLLDRIPSVTEPGMTAAEDTRDFDVKHRTYDIARLMQGGKGIINAGKLGFNNKDRTLLTKLIMMPDSEETKLDNVSIAEYFKDDPHMFQTNFWYMWETTFAFRTQSSAQELRRYMHQMIYEFTQIEHLVGVNRTRYNQFESMILPLIKYLQGQGVTFIDNKIVKDWQFKDTPMQDEITVTGLVIEDAQTGETEEVEVDEETAVIFTNGSITDSATMGDYNTPAPENMDYGVSASLWKKATERFYNLGTPDKFFNDRNASEWVSFTLTTKNHLFLNEIVRITTQEPGNALNSFLSTTPITPLNQKDVNMSIVVHHQPHFTTQQPNETVLWGYFLYPRRQGEFVNKPYIKMTGKEMAQELIGQLSKVDPGPGNIKDKEKEILDSIVNNIPVYMPYASALFNNRAKSDRPEVLPKHSTNLAFTGEFAEQPYQMIFTEQSAVRSGEIAAYHFAGVPMDNLVKTPRYDKDPKTLLKATKKMFD DEWD860 TD Primarily distributed in human gut. DEWD860 FC This enzyme catalyzes the conversion of linoleic acid to 10-hydroxy-12-octadecenoic acid. DEWD860 KD 2: Bacteria DEWD860 PL 1239: Firmicutes DEWD860 CL 91061: Bacilli DEWD860 OD 186826: Lactobacillales DEWD860 FM 33958: Lactobacillaceae DEWD860 GE 1578: Lactobacillus DEWD860 SP 1590: Lactobacillus plantarum DEBI60T ID DEBI60T DEBI60T DN L-arabinose isomerase (araA) DEBI60T GN araA DEBI60T SN Isomerase L-arabinose; D-arabinose aldose-ketose-isomerase; araA DEBI60T UC D9ILD9_LACFE DEBI60T RD Alpha-l-arabinose DEBI60T E1 5: Isomerase DEBI60T E2 5.3: Intramolecular oxidoreductase DEBI60T E3 5.3.1: Aldose/ketose isomerase DEBI60T EC 5.3.1.4 DEBI60T PD 4LQL DEBI60T SQ MRKMQDYKFWFVVGSQPLYGPEALAEVEKDARKLVDGLNKGGKLDYPVEFKLVATTADSITKFMKEANYNDDVAGVITWMHTFSPAKNWIRGTELLQKPLLHLATQFLNNIPFDSIDMDYMNLHQSAHGDREYAYINSRLNVPAASVYGWWGDADVQEQIADWQHVAVAYNESFHIKIARFGDTMRDVAVTEGDKVAAQIKLGWTVDYYPTNELVAVVNGIAEDEIDAAYKDLEANYDLVEGDNDHEKYVHNVRYQLREYLGIKKFLDDNGYDAFTDNFQDLEGLEQLPGLAVQLLMIDGYGFGPEGDFKMAGLTRLLKIAADNKQTALMEDYTLDLRHGHEAIMGSHMLEVDPTLASDKPRVEVHPLGIGGKDDPARLVFTGAEGKGYDITLSYFDDGYKFIGYPVDCKTPEAEMPKLPVAKQMWTPEIGLAEGAKQWMKYGGGHHTVLTLALSEEQLEQLARLFKVDFINIK DEBI60T TD Primarily distributed in human gut. DEBI60T FC This enzyme catalyzes the conversion of L-arabinose to L-ribulose. It requires a divalent metal ion and binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism. It can also convert D-galactose to D-tagatose with lower efficiency. DEBI60T KD 2: Bacteria DEBI60T PL 1239: Firmicutes DEBI60T CL 91061: Bacilli DEBI60T OD 186826: Lactobacillales DEBI60T FM 33958: Lactobacillaceae DEBI60T GE 1578: Lactobacillus DEBI60T SP 1613: Lactobacillus fermentum DEBI60T SU Lactobacillus fermentum CGMCC 2921 DEINPMH ID DEINPMH DEINPMH DN Lactate racemase (Lsa784) DEINPMH GN Lsa784 DEINPMH SN Lactate racemization operon protein LarA; LAS9624_00840; LSAJ112_140075; Lar; Lsa784; lsa784 DEINPMH UC Q3BCH3_LACSK DEINPMH RD D-lactic acid DEINPMH GI 33974450 DEINPMH E1 5: Isomerase DEINPMH E2 5.1: Racemase/epimerase DEINPMH E3 5.1.2: Hydroxy acid racemase/epimerase DEINPMH EC 5.1.2.1 DEINPMH SQ MVAIKLPYDQKIITANIADANFAGKLVSQAATYQNPLSEAETVEQSLDNPIDSPKLEELAKGKKNIVIISSDHTRPVPSHIMTPILLRRIRSVAPDARIRILVATGFHRPSTHEELVNKYGEEIVANEEIVMHISTDDSSVVKIGQLPSGGDCIINKIAVEADLLISEGFIESHFFAGFSGGRKSILPGVASYKTIMANHSGEFINSHYSRTGNLMHNPVHKDMVYAAKTAGLKFILNVVLDEDKHIIGSFAGNLETAHKKGCDFVESLSEVDKIDCDIAISTNGGYPLDQNIYQAVKGMTAAEATNKQGGVIIMVAGARDGHGGDGFYHNIADVKDPKEFLDQAINTPRLETVPDQWTSQILARILVQHHVIFVSDLVDPQLITDMHMELATSLDAALERAYAIEGADAKVTVIPDGLGVIVK DEINPMH TD Primarily distributed in human gut. DEINPMH FC This enzyme contains a unique nickel-containing cofactor, pyridinium-3-thioamide-5-thiocarboxylate mononucleotide Ni pincer complex. DEINPMH KD 2: Bacteria DEINPMH PL 1239: Firmicutes DEINPMH CL 91061: Bacilli DEINPMH OD 186826: Lactobacillales DEINPMH FM 33958: Lactobacillaceae DEINPMH GE 1578: Lactobacillus DEINPMH SP 1599: Lactobacillus sakei DEINPMH SU Lactobacillus sakei NRIC 1071(T) DE0KTEM ID DE0KTEM DE0KTEM DN L,D-carboxypeptidase A (ldcA) DE0KTEM GN ldcA DE0KTEM SN Carboxypeptidase; LD-carboxypeptidase; Murein tetrapeptide carboxypeptidase; VT05_01038; ldcA DE0KTEM UC A0A5K1KMI8_NEIGO DE0KTEM RD Dithiazoline DE0KTEM E1 3: Hydrolases DE0KTEM E2 3.4: Peptidase DE0KTEM E3 3.4.17: Metallocarboxypeptidase DE0KTEM EC 3.4.17.13 DE0KTEM SQ MTEPTSRRRFLKTCTAAGAGLLQACGTSATSVPPLPSSHSVVKARTVPLQTPRRQSSDGNLLRVVASSGFAEDTNRVNTALTRLYNAGFTVTNQQAGSRRFQRFAGTDAQRAADFQEVASGRVATPKVLMGLRGGYGAARILPHIDFASLGARMREHGTLFFGFSDVCAVQLALLAKGNMMSFAGPMAYSDFGKPAPGAFTMDAFIKGATQNRLTVDVPYIQRTDVETEGTLWGGNLSVLASLAGTPYMPDIDGGILFLEDVGEQPYRIERMLNTLYLSGILGKQRAIVFGDFRMEKIRDLYDSSYDFSAVAKHISRTAKIPVLTGFPFGHIADKITFPLGAHTRIRMNGNGGYSVAFEGYPTLDASALTLDTLLPPPDLPIFPESGVADISE DE0KTEM TD Primarily distributed in human gut. DE0KTEM FC This enzyme hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains. DE0KTEM KD 2: Bacteria DE0KTEM PL 1224: Proteobacteria DE0KTEM CL 28216: Betaproteobacteria DE0KTEM OD 206351: Neisseriales DE0KTEM FM 481: Neisseriaceae DE0KTEM GE 482: Neisseria DE0KTEM SP 485: Neisseria gonorrhoeae DE0J45Y ID DE0J45Y DE0J45Y DN Inositol dehydrogenase (idh) DE0J45Y GN idh DE0J45Y SN Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase; Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase; MI 2-dehydrogenase/DCI 3-dehydrogenase; LCABL_02210; idh DE0J45Y UC A0A0J9X1Y2_LACCB DE0J45Y RD Inositol DE0J45Y E1 1: Oxidoreductase DE0J45Y E2 1.1: CH-OH donor oxidoreductase DE0J45Y E3 1.1.1: NAD/NADP oxidoreductase DE0J45Y EC 1.1.1.18 DE0J45Y PD 4MIE; 4MIN; 4MIO; 4MIY; 4MJL DE0J45Y SQ MVVKVGVIGTGAMGRAHIDRLTNVLTGAEVVAVTDIDHEAAEAAVRDFHLNAKVYPDDTSLLQDPDIDAVFVVSFGGAHEATVLKALDTDKFIFTEKPLATTLEGAKRIVDKELTKSKKVIQVGFMRRYDQGIRALKEKLDTGIIGAPLVVRASHINPNVASNYSNEMAITDTLIHEIDEMHWLLDDEYTSIQITYPRQSAEVRNEGLHDPQLATLTTKKGTVIQVLVHVTAQYGYEVKLEVIGETGELQLPNYGLGPILRSNANQQTAVEMSWINRFIQAYNTEVQEFIDEVAKSEPPVGPSAWDGYIAAITAAAANRSQKDQETVLINVAGTPTFYQ DE0J45Y TD Primarily distributed in human gut. DE0J45Y FC This enzyme involves in the oxidation of myo-inositol and D-chiro-inositol to 2-keto-myo-inositol and 1-keto-D-chiro-inositol, respectively. DE0J45Y KD 2: Bacteria DE0J45Y PL 1239: Firmicutes DE0J45Y CL 91061: Bacilli DE0J45Y OD 186826: Lactobacillales DE0J45Y FM 33958: Lactobacillaceae DE0J45Y GE 1578: Lactobacillus DE0J45Y SP 1582: Lactobacillus casei DE0J45Y SU Lactobacillus casei BL23 DEDUGWF ID DEDUGWF DEDUGWF DN Inositol dehydrogenase (idh) DEDUGWF GN iolG DEDUGWF SN Inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase; Myo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase; MI 2-dehydrogenase/DCI 3-dehydrogenase; iolG DEDUGWF UC IOLG_LACCA DEDUGWF RD Inositol DEDUGWF E1 1: Oxidoreductase DEDUGWF E2 1.1: CH-OH donor oxidoreductase DEDUGWF E3 1.1.1: NAD/NADP oxidoreductase DEDUGWF EC 1.1.1.18 DEDUGWF SQ MVVKVGVIGTGAMGRAHIDRLTNVLTGAEVVAVTDIDHEAAEAAVRDFHLNAKVYPDDTSLLQDPDIDAVFVVSFGGAHEATVLKALDTDKFIFTEKPLATTLEGAKRIVDKELTKSKKVIQVGFMRRYDQGIRALKEKLDTGIIGAPLVVRASHINPNVASNYSNEMAITDTLIHEIDEMHWLLDDEYTSIQITYPRQSAEVRNEGLHDPQLATLTTKKGTVIQVLVHVTAQYGYEVKLEVIGETGELQLPNYGLGPILRSNANQQTAVEMSWINRFIQAYNTEVQEFIDQVAKSEPPVGPSAWDGYIAAITAAAANRSQKDQETVLINVAGTPTFYQNKNAIHA DEDUGWF TD Primarily distributed in human gut. DEDUGWF FC This enzyme involves in the oxidation of myo-inositol and D-chiro-inositol to 2-keto-myo-inositol and 1-keto-D-chiro-inositol, respectively. DEDUGWF KD 2: Bacteria DEDUGWF PL 1239: Firmicutes DEDUGWF CL 91061: Bacilli DEDUGWF OD 186826: Lactobacillales DEDUGWF FM 33958: Lactobacillaceae DEDUGWF GE 1578: Lactobacillus DEDUGWF SP 1582: Lactobacillus casei DEDUGWF SU Lactobacillus casei BL23 DEWP153 ID DEWP153 DEWP153 DN Hyaluronidase (hyl) DEWP153 GN hyl DEWP153 SN Chondroitin sulfate hydrolase; Hyaluronate lyase; Chondroitinase; Chondroitinase I; Cumulase; HYase; hyl; hysA DEWP153 UC W5RSC1_9BACI DEWP153 RD Hyaluronan DEWP153 E1 4: Lyases DEWP153 E2 4.2: Carbon-oxygen lyase DEWP153 E3 4.2.2: Polysaccharide-lyase DEWP153 EC 4.2.2.1 DEWP153 SQ NESTLLLNTSFEETEAPKSGWDQLGAPKWGVWRPTGSPIVTITKEASRTGEYGLKIAAAQSARAAVSQDVPVQGGQTYQLGTWLKTDNIVSGQGARLRVVLYEGTQQLGLLYSSRLTGTHDWSQIKMEVKTPANADSIRVQLFFETGTGTALFDDVSLQLIQPATSIAIEESEITIKEQETGLLHAQMVPADASSKVSWVSADPSIATVDNGKVTGVNPGGTTIMAFTDNGLAATSTVKVIKNDGIERPEVTQLDLQPKELELGSGQVRLLQAIIAPATADAEKLVWSSSNEAVASIQKGLIEAKASGTAVITVETEDGSLKSESQITVTDAVVDEYDQLRKKWKSLMTGLDSYDPTNVRMNEMIQNQTKSAETLWKTMFKNNDRSFLWINFASTDNSADIRDSYRNLTTMAKAFANEHSSLYRNPQLLKDITEALEWLYQNRYNESIAQYSNWWHWEIGVPNELNSLMVLLYDYLDQDSIHRYLKVVDHFQPDPTKSGATTPEKYREALGANRIDVSKVVGVRGVIVKDATKIAAARDALSQTFENVTEGDGFYEDGSFVQHENIAYNGSYGIVLIEGLTDMLELLSNSTWQVTDPKVTNVYDWIETAYEPFMYKGALMDMVRGRAISRNFLQDHQAGHTIIKSVIRMAQFAPEPYAEKYNSMAKYWLQEDTYLDYFKNAGNFRDITLAKQLLEKQEVTPRGDLDFHKTFASMDRVVHRKSGYAFGISMYSNRIQNYEDMNDENRKGWYTGEGMTYLYNGDLAQYSDDFWPTVDPYRMPGTTVDTMRRADGSGEHRSSESWTGGSTLKNFGSAGMSYDAWNSSLIAKKSWFMFDNEIVALGAGITSSEDRNVESIVENRKIRNDGSNQLVINGETLNLSNGGQNQTMAAKWAFLEGNVPGADIGYYFPEGKMLTIKKEERTGAWKDINYGGPAEAIKRSYTTMWFDHGVRPEQDTYSYVLLPGLNKEQTHQYSQNPDITILRNDSAVQAVQDVKENIIGANFWKDEKQSAGPLTVYQKASVTMQEKDGVLEIAVCDPTMENKGSIEIEIDGKAFKVLEADESITVENTKPSIKLKVNVNEAKGKTFTAKLKMIPSQKGNSPNSIR DEWP153 TD Primarily distributed in human gut. DEWP153 FC This enzyme catalyzes the degradation of hyaluronan by a beta-elimination reaction and it also acts on chondroitin. DEWP153 KD 2: Bacteria DEWP153 PL 1239: Firmicutes DEWP153 CL 91061: Bacilli DEWP153 OD 1385: Bacillales DEWP153 FM 186817: Bacillaceae DEWP153 GE 1386: Bacillus DEWP153 SP 1404: Bacillus megaterium DE12PUC ID DE12PUC DE12PUC DN Histidine decarboxylase (hdcA) DE12PUC GN hdcA DE12PUC SN Histidine decarboxylase proenzyme; hdcA; HDC; DKZ26_01060 DE12PUC UC A0A0K6GJ74_LACRE DE12PUC RD L-histidine DE12PUC E1 4: Lyases DE12PUC E2 4.1: Carbon-carbon lyase DE12PUC E3 4.1.1: Carboxy-lyase DE12PUC EC 4.1.1.22 DE12PUC SQ MSELDTKLHKLGVDRIAISPYKQWSRGYMEPGNIGNGYVTGLKVDAGVRDKTDDEVLDGIVSYDRAETKNAYIGQINMTTASSFTGPQGHCIGYDLLRNPEVDTAEPLFTVKQWDGSELPIYDAKPLQDSLVEYFGTNNNRRHYPAPGSFIVCANKGVTAERPMNDSDMKPGQGYGVWSAIALSFAKDPAKDSSMFIEDAGVWETPNEDELIEYLKGRRKAIAKSIAECGQDANTSFKGSWIGFAHAMMEPGQIGNAITVAPYISMPVDSIPGGSILTPDTDMDIMENLTMPEWLDKMEYKSLTANGAIKY DE12PUC TD Primarily distributed in human gut. DE12PUC FC This enzyme catalyzes the decarboxylation of histidine to form histamine. DE12PUC KD 2: Bacteria DE12PUC PL 1239: Firmicutes DE12PUC CL 91061: Bacilli DE12PUC OD 186826: Lactobacillales DE12PUC FM 33958: Lactobacillaceae DE12PUC GE 1578: Lactobacillus DE12PUC SP 1598: Lactobacillus reuteri DEIN8FB ID DEIN8FB DEIN8FB DN Glycerol/diol dehydratase (dhaB) DEIN8FB GN gldC DEIN8FB SN Glycerol dehydratase; Propanediol dehydratase pduC; dhaB; gldC; pduC DEIN8FB UC H6V877_LACRE DEIN8FB RD PhIP DEIN8FB E1 4: Lyases DEIN8FB E2 4.2: Carbon-oxygen lyase DEIN8FB E3 4.2.1: Hydro-lyase DEIN8FB EC 4.2.1.30 DEIN8FB SQ RYAPFNAISILIGAQTGRPGVLTQCSVEEATELQLGMRGFTAYAETISVYGTDRVFTDGDDTPWSKGFLASCYASRGLKMRFTSGAGSEVLMGYPEGKSMLYLEARCILLTKASGVQGLQNGAVSCIEIPGAVPNGIREVLGENLLCMMCDIEC DEIN8FB TD Primarily distributed in human gut. DEIN8FB FC This enzyme has two forms. One form requires a cobamide coenzyme, while the other is a glycyl radical enzyme. DEIN8FB KD 2: Bacteria DEIN8FB PL 1239: Firmicutes DEIN8FB CL 91061: Bacilli DEIN8FB OD 186826: Lactobacillales DEIN8FB FM 33958: Lactobacillaceae DEIN8FB GE 1578: Lactobacillus DEIN8FB SP 1598: Lactobacillus reuteri DEWRN24 ID DEWRN24 DEWRN24 DN Glucansucrase (gtf106B) DEWRN24 GN gtf106B DEWRN24 SN Dextransucrase; Sucrose 6-glucosyltransferase; B-512F dextransucrase; B-512FMC dextransucrase; Dextran-sucrase DEWRN24 UC Q5SBN3_LACRE DEWRN24 RD Pyrogallol DEWRN24 E1 2: Transferase DEWRN24 E2 2.4: Glycosyltransferases DEWRN24 E3 2.4.1: Hexosyltransferase DEWRN24 EC 2.4.1.5 DEWRN24 PD 3HZ3; 3KLK; 3KLL; 4AYG DEWRN24 SQ MEIKKHFKLYKSGKQWVTAAVATVAVSTALLYGGVAHADQQVQSSTTQEQTSTVNADTTKTVNLDTNTDQPAQTTDKNQVANDTTTNQSKTDSTSTTVKNPTFIPVSTLSSSDNEKQSQNYNKPDNGNYGNVDAAYFNNNQLHISGWHATNASQGTDSRQVIVRDITTKTELGRTNVTNNVLRPDVKNVHNVYNADNSGFDVNINIDFSKMKDYRDSIEIVSRYSGNGKSVDWWSQPITFDKNNYAYLDTFEVKNGELHATGWNATNKAINYNHHFVILFDRTNGKEVTRQEVRDGQSRPDVAKVYPQVVGANNSGFDVTFNIGDLDYTHQYQILSRYSNADNGEGDYVTYWFAPQSIAPANQSNQGYLDSFDISKNGEVTVTGWNATDLSELQTNHYVILFDQTAGQQVASAKVDLISRPDVAKAYPTVKTAETSGFKVTFKVSNLQPGHQYSVVSRFSADENGNGNDKRHTDYWYSPVTLNQTASNIDTITMTSNGLHITGWMASDNSINEATPYAIILNNGREVTRQKLTLIARPDVAAVYPSLYNSAVSGFDTTIKLTNAQYQALNGQLQVLLRFSKAVDGNPNGTNTVTDQFSKNYATTGGNFDYVKVNGNQIEFSGWHATNQSNDKNSQWIIVLVNGKEVKRQLVNDTKDGAAGFNRNDVYKVNPAIENSIMSGFQGIITLPVTVKDENVQLVHRFSNDAKTGEGNYVDFWSEVMSVKDSFQKGNGPLNQFGLQTINGQQYYIDPTTGQPRKNFLLQNGNDWIYFDKDTGAGTNALKLQFDKGTISADEQYRRGNEAYSYDDKSIENVNGYLTADTWYRPKQILKDGTTWTDSKETDMRPILMVWWPNTVTQAYYLNYMKQYGNLLPASLPSFSTDADSAELNHYSELVQQNIEKRISETGSTDWLRTLMHEFVTKNSMWNKDSENVDYGGLQLQGGFLKYVNSDLTKYANSDWRLMNRTATNIDGKNYGGAEFLLANDIDNSNPVVQAEELNWLYYLMNFGTITGNNPEANFDGIRVDAVDNVDVDLLSIARDYFNAAYNMEQSDASANKHINILEDWGWDDPAYVNKIGNPQLTMDDRLRNAIMDTLSGAPDKNQALNKLITQSLVNRANDNTENAVIPSYNFVRAHDSNAQDQIRQAIQAATGKPYGEFNLDDEKKGMEAYINDQNSTNKKWNLYNMPSAYTILLTNKDSVPRVYYGDLYQDGGQYMEHKTRYFDTITNLLKTRVKYVAGGQTMSVDKNGILTNVRFGKGAMNATDTGTDETRTEGIGVVISNNTNLKLNDGESVVLHMGAAHKNQKYRAVILTTEDGVKNYTNDTDAPVAYTDANGDLHFTNTNLDGQQYTAVRGYANPDVTGYLAVWVPAGAADDQDARTAPSDEAHTTKTAYRSNAALDSNVIYEGFSNFIYWPTTESERTNVRIAQNADLFKSWGITTFELAPQYNSSKDGTFLDSIIDNGYAFTDRYDLGMSTPNKYGSDEDLRNALQALHKAGLQAIADWVPDQIYNLPGKEAVTVTRSDDHGTTWEVSPIKNVVYITNTIGGGEYQKKYGGEFLDTLQKEYPQLFSQVYPVTQTTIDPSVKIKEWSAKYFNGTNILHRGAGYVLRSNDGKYYNLGTSTQQFLPSQLSVQDNEGYGFVKEGNNYHYYDENKQMVKDAFIQDSVGNWYYFDKNGNMVANQSPVEISSNGASGTYLFLNNGTSFRSGLVKTDAGTYYYDGDGRMVRNQTVSDGAMTYVLDENGKLVSESFDSSATEAHPLKPGDLNGQK DEWRN24 TD Primarily distributed in human gut. DEWRN24 FC This enzyme glucosylates the phenolic compounds catechol, pyrogallol, resorcinol, and ethyl gallate. DEWRN24 KD 2: Bacteria DEWRN24 PL 1239: Firmicutes DEWRN24 CL 91061: Bacilli DEWRN24 OD 186826: Lactobacillales DEWRN24 FM 33958: Lactobacillaceae DEWRN24 GE 1578: Lactobacillus DEWRN24 SP 1598: Lactobacillus reuteri DEWRN24 SU Lactobacillus reuteri 121 DE21ZKX ID DE21ZKX DE21ZKX DN GH3 beta-glucosidase (BAD1610) DE21ZKX GN BAD1610 DE21ZKX SN Periplasmic beta-glucosidase GH3; Glucan endo-1 3-beta-D-glucosidase GH3; Beta-D-glucosidase GH3; Beta-D-glucoside glucohydrolase GH3; Beta-glucosidase GH3; GH3; BAD_1610 DE21ZKX UC A1A3V8_BIFAA DE21ZKX RD PNB-D-xyloside DE21ZKX E1 3: Hydrolases DE21ZKX E2 3.2: Glycosylase DE21ZKX E3 3.2.1: O/S-glycosyl compound glycosidase DE21ZKX EC 3.2.1.21 DE21ZKX KG Biosynthesis of secondary metabolites:bad01110; Cyanoamino acid metabolism:bad00460; Metabolic pathways:bad01100; Starch and sucrose metabolism:bad00500 DE21ZKX SQ MTMPRSMYNHADKQEDKEKSYIELDSTETEIIKYLNDNYKDVILLVKSSAAMELDWLKQYPNIKAVVYSQNVTNALAKVFSGEVNPSGRTVDTFAADALASPAAQNFGSYQYYDENGKATKYNYVDYAEGIYVGYKYYETRYEDKVLGQGNAGDYDYAKEVVYPFGYGLSYTDFKWSDFSVARHGNDFVATVTVTNTGDTAGKDVVELYAQSPYTDYDKRNAVEKASVNLVGYGKTSELKPGTSETVRITFGKDQLKAYDYKGAKTYILDAGQYRFTAATDANQAVNNILADKGKTVADGMTSEGDKTMVASWTPENTDADTTTFASDSTTGKAISNLFDAASDPEVAYLSRSDWTGTFPKHYGESSGEINTWGNEINCKDSDGNNASCTWKKTASTKLIKHLEGNDSGTTVDKDSIMDTPTFGKKNGLKVSDMRGLAYDDAQWDKILDELTEDDYNQLIYFSGYGVDYIKSVDKPFQTDADSATGWMYGGTGKTFPSIMMLTQTWNAQLAEDLGEMMGNEALLGGANGWYAPAMNIHRTPFSGRNGEYYSEDGYMSGSMASLEVKGAATKGVYSYIKHFALNDQENHRGDRPGNFSVATWSNEQAIREIYLKPFDMCMHLGDMDMKTVVKKSDGTYENKVVKTPIAKGVMTSFNRIGATWTGGSHALIQQLLRDEWGFNGLIITDNANTGKFMSPYQMLEAGADIKLLNVSDDPTGEKLDFNDAATYHYARQAMHHLLYTVANTNCMNGALPGAGFKFSNGMKTIQIVFNTVCSVILAMLAFFSVWRWMPGTIKRVAARKEARVARKAARKAAKG DE21ZKX TD Primarily distributed in human gut. DE21ZKX FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DE21ZKX KD 2: Bacteria DE21ZKX PL 201174: Actinobacteria DE21ZKX CL 1760: Actinobacteria DE21ZKX OD 85004: Bifidobacteriales DE21ZKX FM 31953: Bifidobacteriaceae DE21ZKX GE 1678: Bifidobacterium DE21ZKX SP 1680: Bifidobacterium adolescentis DEHUP0C ID DEHUP0C DEHUP0C DN D-Lactate dehydrogenase (ldhA) DEHUP0C GN ldhA DEHUP0C SN Glycolate dehydrogenase; D-lactate ferricytochrome C oxidoreductase; Fermentative lactate dehydrogenase; D-LDH; Ldb0101; ldhA DEHUP0C UC LDHD_LACDA DEHUP0C RD DB-053072 DEHUP0C GI 4085369 DEHUP0C E1 1: Oxidoreductase DEHUP0C E2 1.1: CH-OH donor oxidoreductase DEHUP0C E3 1.1.1: NAD/NADP oxidoreductase DEHUP0C EC 1.1.1.28 DEHUP0C KG Metabolic pathways:ldb01100; Microbial metabolism in diverse environments:ldb01120; Pyruvate metabolism:ldb00620 DEHUP0C PD 1DLD; 1J49; 1J4A DEHUP0C SQ MTKIFAYAIREDEKPFLKEWEDAHKDVEVEYTDKLLTPETVALAKGADGVVVYQQLDYTAETLQALADNGITKMSLRNVGVDNIDMAKAKELGFQITNVPVYSPNAIAEHAAIQAARILRQDKAMDEKVARHDLRWAPTIGREVRDQVVGVIGTGHIGQVFMQIMEGFGAKVIAYDIFRNPELEKKGYYVDSLDDLYKQADVISLHVPDVPANVHMINDESIAKMKQDVVIVNVSRGPLVDTDAVIRGLDSGKIFGYAMDVYEGEVGIFNEDWEGKEFPDARLADLIARPNVLVTPHTAFYTTHAVRNMVVKAFDNNLELVEGKEAETPVKVG DEHUP0C TD Primarily distributed in human gut. DEHUP0C FC This enzyme has D-lactate dehydrogenase activity. DEHUP0C KD 2: Bacteria DEHUP0C PL 1239: Firmicutes DEHUP0C CL 91061: Bacilli DEHUP0C OD 186826: Lactobacillales DEHUP0C FM 33958: Lactobacillaceae DEHUP0C GE 1578: Lactobacillus DEHUP0C SP 1584: Lactobacillus delbrueckii DEHUP0C SU Lactobacillus delbrueckii subsp. bulgaricus DE1KTC4 ID DE1KTC4 DE1KTC4 DN Dextransucrase 4 (dsrF4) DE1KTC4 GN dsrF4 DE1KTC4 SN Glucansucrase 4; Sucrose 6-glucosyltransferase 4; Dextransucrase IV DE1KTC4 UC GTF4_LEUME DE1KTC4 RD RTR-001007 DE1KTC4 E1 2: Transferase DE1KTC4 E2 2.4: Glycosyltransferases DE1KTC4 E3 2.4.1: Hexosyltransferase DE1KTC4 EC 2.4.1.5 DE1KTC4 SQ MIRTSKKAIAVAVGLIASATASAGDATAPIFVSNAMLDKHVIYQDFAFYQPYDGTVYKTLARQAPELRNLGITDVWFAPPYRALNDGRFSEGYAVIDRYDLGEFPQGRGNAIATKYGTGAQLREAIESMHRQRINAIADIVPNQMFFSQREVASVTAVDIFGNPTNPSASNVLYPGYSKGGGLGQKQYGVIKQWQAKYENGTSPQALGIDRIMVDGAGAPYRYYGPGDARNHLPAWLEATDAARVGALNTIDTYLSVDGSYAAQSAATAIPVYRPYLLYYVDPRRDATVQPYLTYMRAHGFPGNSDDAVRQSIINGNTDAVTKATNDYLALQPGYSASSEAGAAAFRFNKPSNADVNKNVLQYEFLLGSDIDNSNATVQNETLNWQRFLLDKYGFDGFRFDAAGHYNTDILRQSAQLMSGRYGHDMNNHLSVIESYVDPQIAFENSNGNGQLAYDGTLYSTMYNTLEQANPGGPLSDIFAKSIVGQARFGAGRAIPNWSFVTNHDQEHNVIAKIPVPPTQKAGYTPDAAIQLAQMSIYDNDRKQAVKQYAPYNVPSAYAVLLTNKDTVPTVFYGDLYESDKAYVSTKTPYYDAITRLLKIRQKFVAGAQVLTYYKTNTSPSVAGQDLLASVRVGTDRGTGVATVIGNNPATDATIRVDMGLQHANQTFTNMFGQWPERLQTDGRGVLTVHVTGSSTPQVHGYLGVWVPTSEGEGSMMGYAS DE1KTC4 TD Primarily distributed in human gut. DE1KTC4 FC This enzyme involves in the production of dextran, an extracellular glucan polymer. DE1KTC4 KD 2: Bacteria DE1KTC4 PL 1239: Firmicutes DE1KTC4 CL 91061: Bacilli DE1KTC4 OD 186826: Lactobacillales DE1KTC4 FM 81850: Leuconostocaceae DE1KTC4 GE 1243: Leuconostoc DE1KTC4 SP 1245: Leuconostoc mesenteroides DE1KTC4 SU Leuconostoc mesenteroides 0326 DED68N5 ID DED68N5 DED68N5 DN Dextransucrase 3 (dsrF3) DED68N5 GN dsrF3 DED68N5 SN Glucansucrase 3; Sucrose 6-glucosyltransferase 3; Dextransucrase III DED68N5 UC GTF3_LEUME DED68N5 RD RTR-001007 DED68N5 E1 2: Transferase DED68N5 E2 2.4: Glycosyltransferases DED68N5 E3 2.4.1: Hexosyltransferase DED68N5 EC 2.4.1.5 DED68N5 SQ MRASPSQFFAISLLSITISGLLSGAAVAAQTPTALEQVPDGKGGVKWQEVQHDASAEEEQKGQGRKKFLGIQAITTEPDGSVKVEMGKPEVRQPASGDVFVSNEKLDEHVIFQAFALYQPNDNATYKALAENAPQLAQWGITDVWSPPPYRAASDSKYGEGYAIADRYDLGTYGKGPTKYGTADELKAAIGALHNNDIRIQVDVVPNQIIGLNERHVLPVTGVDMYGQPMNPFLDHYLYSTYSKGSAPGQTEHGVIKEWDYFHFHGTTTQYQGLFRVLSDANSKLYRYLGPNHPENYLPAFLAESDAAKYGKINTIDGYLLADTWFAVENAESENAVYAPLFLYYEEPRSGVVEQTFMDFARSKGYTGSDEEIRETMLAELRMTPNPIGPLMDEYLAAQPGYSKKSEDDAKVTALRYDGPENDASHIGTNVLDFEFLVGNDLDTIREDVQQEQLNWQKYLLDFGFDGFRIDAASHINTDMLRDEVTQRLNYFAGEDVNEHLSYIESYVAQQVDFEQSNNYGQMAMDAGPFSGLMFSFGRDWAPLRYAFEASLIDRVNGGPALPNWSFVNNHDQEHNILVNVPLTEEEAGGYEPNSQPYELRQLEKYDADRNSVEKQWAPHNVPAMYAILLTTKDTVPTVFYGDMFVSSKPYMSTPTPYRDDIVNILKLRKQFAKGEQVIRYENSNTGSNGEDLVSNIRLGNDRKTGVAVVAGNNPALDTTITVDMGAQHRNQWFVDAMGYQPERLKTDKDGRLTVQVKGTQNVDVKGYLAAWVPDLQAQE DED68N5 TD Primarily distributed in human gut. DED68N5 FC This enzyme involves in the production of dextran, an extracellular glucan polymer. DED68N5 KD 2: Bacteria DED68N5 PL 1239: Firmicutes DED68N5 CL 91061: Bacilli DED68N5 OD 186826: Lactobacillales DED68N5 FM 81850: Leuconostocaceae DED68N5 GE 1243: Leuconostoc DED68N5 SP 1245: Leuconostoc mesenteroides DED68N5 SU Leuconostoc mesenteroides 0326 DE174E0 ID DE174E0 DE174E0 DN Dextransucrase 2 (dsrF2) DE174E0 GN dsrF DE174E0 SN Glucansucrase 2; Sucrose 6-glucosyltransferase 2; Dextransucrase II; Dextransucrase DsrF; dsrF2 DE174E0 UC GTF2_LEUME DE174E0 RD RTR-001007 DE174E0 E1 2: Transferase DE174E0 E2 2.4: Glycosyltransferases DE174E0 E3 2.4.1: Hexosyltransferase DE174E0 EC 2.4.1.5 DE174E0 SQ MRASPSQFFAISLLSIAISGLLSGAAVAAPAPAALEQVPDGKGGVKWQEVQADKPAEEEQEGKGRKKFLGIQAITTEPDGSVKVEMGKPEVRQPASGDVFVSNEKLDEHVIFQAFALYQPNDNATYKALAENAPQLAQWGITDVWSPPPYRAASDSKYGEGYAIADRYDLGAYDKGPTKYGTADELKAAIGALHNNDIRIQVDVVPNQIIGLNERHVLPVTGVDMYGKPMNPFLDHYLYSTYSKGSAPGQAEHGVIKEWDYFHFHGTTTQYQGLFRVLSDANSKLYRYLGPNHPENYLPAFLAESDAAKYGKINTIDGYLLADTWFAVENAESENAVYAPLFLYYEEPRSGVVEQTFMDFARENGYTGSDEDIRATMLAELRMTPNPLGPLMDEYLAAQPGYSKKSEDDAKVTALRYDGPENDASHIGTNVLDFEFLVGNDLDTIREDVQQEQLNWQKYLLDFGFDGFRIDAASHINTDMLRDEVTQRLNYFAGEDVNEHLSYIESYVAQQVDFEQSNNYGQMAMDAGPFSGLMFSFGRDWAPLRYAFEASLIDRVNGGPALPNWSFVNNHDQEHNILVTVPLTEEEAGGYEPNSQPYELRQLEKYDADRNSVEKQWAPHNVPAMYAILLTTRDTVPTVFYGDMFMSSKPYMSTPTPYRDDIVNILKLRKQFAKGEQVIRYENSNTGSNGEDLVSNIRLGNDRKTGVAVVAGNNPALDTTITVDMGAQHRNQWFVDAMGYQPERLKTDKDGRLTVQVKGTQNVDVKGYLAAWVPDLQAQE DE174E0 TD Primarily distributed in human gut. DE174E0 FC This enzyme involves in the production of dextran, an extracellular glucan polymer. DE174E0 KD 2: Bacteria DE174E0 PL 1239: Firmicutes DE174E0 CL 91061: Bacilli DE174E0 OD 186826: Lactobacillales DE174E0 FM 81850: Leuconostocaceae DE174E0 GE 1243: Leuconostoc DE174E0 SP 1245: Leuconostoc mesenteroides DE174E0 SU Leuconostoc mesenteroides 0326 DEEPQJ8 ID DEEPQJ8 DEEPQJ8 DN Dextransucrase 1 (dsrF1) DEEPQJ8 GN dsrF DEEPQJ8 SN Glucansucrase 1; Sucrose 6-glucosyltransferase 1; Dextransucrase I; dsrF1 DEEPQJ8 UC GTF1_LEUME DEEPQJ8 RD RTR-001007 DEEPQJ8 E1 2: Transferase DEEPQJ8 E2 2.4: Glycosyltransferases DEEPQJ8 E3 2.4.1: Hexosyltransferase DEEPQJ8 EC 2.4.1.5 DEEPQJ8 SQ MFSVLLVAGSVSYFPKSAKAYTSGTSLDNRVIFQSFSLYMPYESNMYKILSAKGNELKDWGITDIWLPPAYRSFNAARYMEGYAIADRYDLGEFNQGPNNTRPTKYGTSDELKSMVSVLHANGLKVQEDLVPNQVLGLSKREAVYVTRVDQDGNLFKNPYTTGLTTQIRANLYLAYTKGGGEGQAKYGYIKEWNKKYFNGTSLQGQGMDRVMKDSEGIPYRYFGPNKPNYLPSWLDEAAAANKINTVDTYLPVDGWYAAKDAKTSDNYWKPMLMHDPGYLKYMKSHGYSSVDDILNGDNGQIASLTDAYIASQPGYGFGSEERSFKNDDSGSDDQDQFLFVKKNGTTVPNLYNTISGHNQFLVGMDIDNGNPTVQKEQIHWMNWLLDTYQFDGFRIDAAGHYDKQVLLDEGDVMKQHFGSHLNDHLSYIESYQSAGTDFENENGNPQLMMDYALFYSLQNALGKNSPSNSLSTIATNAVVNRASAGTANATPNWSFVNNHDQEKNRVNKIMLDQYGIKPGIHYDTSAPKAFQDLYDKKTEAKALDIYEKDMESTVKTYAPSNVPSQYAYILTNKDTVPTVFYGDLYKTNASYMSEHTPYYDTIVKLLKVRKNYAYGDQQVTYYKSNTSGTAGKDLISSVRYGKDQNTGVATIIGNNPKTDTTIKVDMGTRHANQLFEDATGFHNEKLYTDSKGVLTVHVKGTQNAQVKGYLGVWIPSKKAATPKQGPALQYGKYVTVTNKHYAVYQDFNWKKKNVTAVNKTYLAKVQYHHSNGSTYLSLYDGKGKWAGYINAKAVKTGSGKQGAAIQYGKHVKVTSKNYAVYQNFNWQKKNIRAVNKTYLAKYIYYHINGLSYLSLYDNKGKWIGYINAKAVKSK DEEPQJ8 TD Primarily distributed in human gut. DEEPQJ8 FC This enzyme involves in the production of dextran, an extracellular glucan polymer. DEEPQJ8 KD 2: Bacteria DEEPQJ8 PL 1239: Firmicutes DEEPQJ8 CL 91061: Bacilli DEEPQJ8 OD 186826: Lactobacillales DEEPQJ8 FM 81850: Leuconostocaceae DEEPQJ8 GE 1243: Leuconostoc DEEPQJ8 SP 1245: Leuconostoc mesenteroides DEEPQJ8 SU Leuconostoc mesenteroides 0326 DEMQRS9 ID DEMQRS9 DEMQRS9 DN Cytochrome P450 BM3 (cypBM3) DEMQRS9 GN cypBM3 DEMQRS9 SN Cytochrome P450 family 102 subfamily A member 3; Cytochrome cypBM3; P450 BM3; cypBM3 DEMQRS9 UC M9TKI6_BACME DEMQRS9 RD HY-12638 DEMQRS9 E1 1: Oxidoreductase DEMQRS9 E2 1.14: Oxygen paired donor oxidoreductase DEMQRS9 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEMQRS9 EC 1.14.14.1 DEMQRS9 SQ DKPVQLGCKFADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLIQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQDDIKVMNDLVDKIIADRKASGEQSDDLLTHYAKRKDPETGEPLDDENIRYQIITFLIAGHETT DEMQRS9 TD Primarily distributed in human gut. DEMQRS9 FC This enzyme is P-450 heme-thiolate protein, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. DEMQRS9 KD 2: Bacteria DEMQRS9 PL 1239: Firmicutes DEMQRS9 CL 91061: Bacilli DEMQRS9 OD 1385: Bacillales DEMQRS9 FM 186817: Bacillaceae DEMQRS9 GE 1386: Bacillus DEMQRS9 SP 1404: Bacillus megaterium DEZNP5G ID DEZNP5G DEZNP5G DN Cytochrome P450 51B1 (cyp51) DEZNP5G GN cyp51B1 DEZNP5G SN Cytochrome P450 family 51 subfamily B member 1; Cytochrome cyp51B1; MMAR_4932; P450 51B1; cyp51B1 DEZNP5G UC B2HH81_MYCMM DEZNP5G RD Dihydrolanosterol DEZNP5G E1 1: Oxidoreductase DEZNP5G E2 1.14: Oxygen paired donor oxidoreductase DEZNP5G E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DEZNP5G EC 1.14.14.154 DEZNP5G KG Biosynthesis of secondary metabolites:mmi01110; Metabolic pathways:mmi01100; Steroid biosynthesis:mmi00100 DEZNP5G SQ MTTAIVPRVSGGEEEHGHLEEFRTDPIGLMQRVRDECGDVGWFQLANKHVVLLSGAKANEFFFRSSDEELDQAEAYPFMTPIFGKGVVFDASPERRKEMLHNSALRGEHMKGHATTIEREVHRMIENWGQEGEIDLLEFFAELTIYTSTSCLIGTKFRNQLDSRFAHFYHELERGTDPLCYVDPYLPIESFRRRDEARKGLVALVQDIMHQRVANPPTDKRDRDMLDVLVSITDEQGNPRFCADEVTGMFISLMFAGHHTSSGTSAWTLIELLRHPDAYAAVIDELDELYADGQPVSFHALRQIPRLENVLKETLRLHPPLIILMRVAKGEFQVEGYPIHEGELVAASPAISNRIAEDFPDPDEFVPERYQEPRQEDLINRWTWIPFGAGRHRCVGAAFATMQIKAIFSVLLREYEFEMAQPADSYRNDHSKMVVQLARPARVRYRRRKMSDNRGH DEZNP5G TD Primarily distributed in human gut. DEZNP5G FC This enzyme is cytochrome P-450 (heme-thiolate) protein acting on a range of steroids with a 14alpha-methyl group, such as obtusifoliol and lanosterol. And it catalyses a hydroxylation and a reduction of the 14alpha-methyl group, followed by a second hydroxylation, resulting in the elimination of formate and formation of a 14(15) double bond. DEZNP5G KD 2: Bacteria DEZNP5G PL 201174: Actinobacteria DEZNP5G CL 1760: Actinobacteria DEZNP5G OD 85007: Corynebacteriales DEZNP5G FM 1762: Mycobacteriaceae DEZNP5G GE 1763: Mycobacterium DEZNP5G SP 1773: Mycobacterium tuberculosis DE87ZNW ID DE87ZNW DE87ZNW DN Cytochrome P450 121A1 (cyp121) DE87ZNW GN cyp121 DE87ZNW SN Cytochrome P450 family 121 subfamily A member 1; Cytochrome P450 121; Cytochrome P450 MT2; MTCY339.34c; Mycocyclosin synthase; Rv2276; cyp121 DE87ZNW UC CP121_MYCTU DE87ZNW RD Phytanic acid DE87ZNW GI 888373 DE87ZNW E1 1: Oxidoreductase DE87ZNW E2 1.14: Oxygen paired donor oxidoreductase DE87ZNW E3 1.14.19: Oxygen paired donor oxidoreductase DE87ZNW EC 1.14.19.70 DE87ZNW PD 1N40; 1N4G; 2IJ5; 2IJ7; 3CXV; 3CXX; 3CXY; 3CXZ; 3CY0; 3CY1; 3G5F; 3G5H; 4G1X; 4G2G; 4G44; 4G48; 4ICT; 4IPS; 4IPW; 4IQ7; 4IQ9; 5IBD; 5IBE; 5IBF; 5IBG; 5IBH; 5IBI; 5IBJ; 5OP9 DE87ZNW SQ MTATVLLEVPFSARGDRIPDAVAELRTREPIRKVRTITGAEAWLVSSYALCTQVLEDRRFSMKETAAAGAPRLNALTVPPEVVNNMGNIADAGLRKAVMKAITPKAPGLEQFLRDTANSLLDNLITEGAPADLRNDFADPLATALHCKVLGIPQEDGPKLFRSLSIAFMSSADPIPAAKINWDRDIEYMAGILENPNITTGLMGELSRLRKDPAYSHVSDELFATIGVTFFGAGVISTGSFLTTALISLIQRPQLRNLLHEKPELIPAGVEELLRINLSFADGLPRLATADIQVGDVLVRKGELVLVLLEGANFDPEHFPNPGSIELDRPNPTSHLAFGRGQHFCPGSALGRRHAQIGIEALLKKMPGVDLAVPIDQLVWRTRFQRRIPERLPVLW DE87ZNW TD Primarily distributed in human gut. DE87ZNW FC This enzyme is a P-450 heme-thiolate protein, and it catalyzes C-C bond formation between the carbons ortho to the phenolic hydroxyl of cyclo(L-tyr-L-tyr) (cYY) producing mycocyclosin. The enzme also can use cyclo(L-Tyr-L-Phe) (cYF), cyclo(L-Tyr-L-Trp) (cYW) and cyclo(L-Tyr-L-3,4-dihydroxyphenylalanine) (cY-DOPA) as substrate. DE87ZNW KD 2: Bacteria DE87ZNW PL 201174: Actinobacteria DE87ZNW CL 1760: Actinobacteria DE87ZNW OD 85007: Corynebacteriales DE87ZNW FM 1762: Mycobacteriaceae DE87ZNW GE 1763: Mycobacterium DE87ZNW SP 1773: Mycobacterium tuberculosis DE06B47 ID DE06B47 DE06B47 DN Cytochrome P450 109B1 (cyp109) DE06B47 GN CYP109B1 DE06B47 SN Cytochrome P450 family 109 subfamily B member 1; Flavocytochrome P450 109B1; P450 109B1; cyp109B1; BSUW23_09845 DE06B47 UC U5U1Z3_BACIU DE06B47 RD Beta-ionone DE06B47 E1 1: Oxidoreductase DE06B47 E2 1.14: Oxygen paired donor oxidoreductase DE06B47 E3 1.14.14: Flavin/flavoprotein donor oxidoreductase DE06B47 EC 1.14.14.1 DE06B47 SQ MNVLNRRQALQRALLNGKNKQDAYHPFPWYESMRKDAPVSFDEENQVWSVFLYDDVKKVIGDKELFSSYMPQQSSAIGNSIINMDPPRHTQIRSVVNKAFTPRVMKQWEPRIQEITDELIQKFQGRSEFDLVHDFSYPLPVIVISELLGVPSEHMDQFKTWSDLLVSTPKDKSEEAEEAFLEERNKCEEELAAFFANIIEEKRNKPAQDVISILVEAEETGEKLSGEELVPFCTLLLVAGNETTTNLISNAMYSILETPDVYNVLRSHPELTPQAVEEALRFRAPAPVLRRIAKRDTEIGGHLIKEGDMVLAFVASANRDETKFDRAHLFDIHRHPNPHIAFGHGIHFCLGAPLARLEAKIALTSLISAFPHMECVSITPIENSVIYGLKSFRVKM DE06B47 TD Primarily distributed in human gut. DE06B47 FC This enzyme is P-450 heme-thiolate protein, acting on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalysed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups. DE06B47 KD 2: Bacteria DE06B47 PL 1239: Firmicutes DE06B47 CL 91061: Bacilli DE06B47 OD 1385: Bacillales DE06B47 FM 186817: Bacillaceae DE06B47 GE 1386: Bacillus DE06B47 SP 1392: Bacillus anthracis DE3FVRW ID DE3FVRW DE3FVRW DN Beta-lactamase (blaB) DE3FVRW GN blaB DE3FVRW SN Penicillinase; Cephalosporinase; Beta-lactam; Metallo-beta-lactamase type 2a; Metallo-beta-lactamase type IIa; Metallothioprotein beta-lactamase IIa; Zinc-requiring beta-lactamase Iia DE3FVRW UC BLA2_BAC17 DE3FVRW RD Ampicillin DE3FVRW E1 3: Hydrolases DE3FVRW E2 3.5: Carbon-nitrogen hydrolase DE3FVRW E3 3.5.2: Cyclic amide hydrolase DE3FVRW EC 3.5.2.6 DE3FVRW SQ MKKNTLLKVGLCVSLLGTTQFVSTISSVQASQKVEQIVIKNETGTISISQLNKNVWVHTELGYFNGEAVPSNGLVLNTSKGLVLVDSSWDNKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGITALKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYQILAGGCLVKSAEAKNLGNVADAYVNEWSTSIENMLKRYRNINLVVPGHGKVGDKGLLLHTLDLLK DE3FVRW TD Primarily distributed in human gut. DE3FVRW FC This enzyme confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. DE3FVRW KD 2: Bacteria DE3FVRW PL 1239: Firmicutes DE3FVRW CL 91061: Bacilli DE3FVRW OD 1385: Bacillales DE3FVRW FM 186817: Bacillaceae DE3FVRW GE 1386: Bacillus DE3FVRW SP 1404: Bacillus megaterium DEEZ5CV ID DEEZ5CV DEEZ5CV DN Beta-lactamase (blaB) DEEZ5CV GN bla DEEZ5CV SN Penicillinase; Cephalosporinase; Beta-lactam; Beta-lactamase OXY-1; bla DEEZ5CV UC BLO1_KLEOX DEEZ5CV RD Tazobactam DEEZ5CV E1 3: Hydrolases DEEZ5CV E2 3.5: Carbon-nitrogen hydrolase DEEZ5CV E3 3.5.2: Cyclic amide hydrolase DEEZ5CV EC 3.5.2.6 DEEZ5CV PD 3BYD DEEZ5CV SQ MLKSSWRKTALMAAAAVPLLLASGSLWASADAIQQKLADLEKRSGGRLGVALINTADDSQTLYRGDERFAMCSTGKVMAAAAVLKQSESNPEVVNKRLEIKKSDLVVWSPITEKHLQSGMTLAELSAAALQYSDNTAMNKMISYLGGPEKVTAFAQSIGDVTFRLDRTEPALNSAIPGDKRDTTTPLAMAESLRKLTLGNALGEQQRAQLVTWLKGNTTGGQSIRAGLPASWAVGDKTGAGDYGTTNDIAVIWPENHAPLVLVTYFTQPQQDAKSRKEVLAAAAKIVTEGL DEEZ5CV TD Primarily distributed in human skin. DEEZ5CV FC This enzyme hydrolyzes broad-spectrum beta-lactam antibiotics and is active against cephalosporins. DEEZ5CV KD 2: Bacteria DEEZ5CV PL 1224: Proteobacteria DEEZ5CV CL 1236: Gammaproteobacteria DEEZ5CV OD 91347: Enterobacterales DEEZ5CV FM 543: Enterobacteriaceae DEEZ5CV GE 570: Klebsiella DEEZ5CV SP 571: Klebsiella oxytoca DEVHXAU ID DEVHXAU DEVHXAU DN Beta-lactamase (blaB) DEVHXAU GN bla DEVHXAU SN Penicillinase; Cephalosporinase; Beta-lactam; Beta-lactamase CTX-M-2; Cefotaximase 2; bla DEVHXAU UC BLC2_SALTM DEVHXAU RD Cefotaxime DEVHXAU E1 3: Hydrolases DEVHXAU E2 3.5: Carbon-nitrogen hydrolase DEVHXAU E3 3.5.2: Cyclic amide hydrolase DEVHXAU EC 3.5.2.6 DEVHXAU SQ MMTQSIRRSMLTVMATLPLLFSSATLHAQANSVQQQLEALEKSSGGRLGVALINTADNSQILYRADERFAMCSTSKVMAAAAVLKQSESDKHLLNQRVEIKKSDLVNYNPIAEKHVNGTMTLAELGAAALQYSDNTAMNKLIAHLGGPDKVTAFARSLGDETFRLDRTEPTLNTAIPGDPRDTTTPLAMAQTLKNLTLGKALAETQRAQLVTWLKGNTTGSASIRAGLPKSWVVGDKTGSGDYGTTNDIAVIWPENHAPLVLVTYFTQPEQKAESRRDILAAAAKIVTHGF DEVHXAU TD Primarily distributed in human gut. DEVHXAU FC This enzyme has cefotaxime-hydrolyzing activity. DEVHXAU KD 2: Bacteria DEVHXAU PL 1224: Proteobacteria DEVHXAU CL 1236: Gammaproteobacteria DEVHXAU OD 91347: Enterobacterales DEVHXAU FM 543: Enterobacteriaceae DEVHXAU GE 590: Salmonella DEVHXAU SP 28901: Salmonella enterica DEVHXAU SU Salmonella enterica subsp. enterica serovar Typhimurium DEUHIQS ID DEUHIQS DEUHIQS DN Beta-lactamase (blaB) DEUHIQS GN blaFRI-4 DEUHIQS SN Penicillinase; Cephalosporinase; Beta-lactam; blaFRI-4 DEUHIQS UC A0A1S7IV31_ENTAS DEUHIQS RD Imipenem DEUHIQS E1 3: Hydrolases DEUHIQS E2 3.5: Carbon-nitrogen hydrolase DEUHIQS E3 3.5.2: Cyclic amide hydrolase DEUHIQS EC 3.5.2.6 DEUHIQS SQ MFFFKKSASTFIFLLCLPLNSFASQESNGVEQMRELETSFGGRIGVYILNTKNGKEFSYRQDERFPLCSSFKAFLAASVLKRTQDKSVSLDDMMEYSGRVMEKHSPVSEKYRETGASVQTLAKAAIQYSDNGASNLLMERYIGGPEGLTAFMRSTGDTDFRLDRWELELNSAIPGDERDTSTPKAVAISLNNIAFGSVLDAKNKSLLQDWLKGNTTGNARIRAAVPDKWVVGDKTGTCGLYGTANDIAILWPDANSPAVMAVYTTRPNQNDKHDETVIKNAAKIAINAVYGSTK DEUHIQS TD Primarily distributed in human gut. DEUHIQS FC This enzyme hydrolyzes beta-lactam. DEUHIQS KD 2: Bacteria DEUHIQS PL 1224: Proteobacteria DEUHIQS CL 1236: Gammaproteobacteria DEUHIQS OD 91347: Enterobacterales DEUHIQS FM 543: Enterobacteriaceae DEUHIQS GE 547: Enterobacter DEUHIQS SP 69218: Enterobacter cancerogenus DEG5Y4W ID DEG5Y4W DEG5Y4W DN Beta-lactamase (blaB) DEG5Y4W GN blaOXA-1 DEG5Y4W SN Penicillinase; Cephalosporinase; Beta-lactam; blaOXA-1 DEG5Y4W UC A0A344X3A2_STASP DEG5Y4W RD Ampicillin DEG5Y4W E1 3: Hydrolases DEG5Y4W E2 3.5: Carbon-nitrogen hydrolase DEG5Y4W E3 3.5.2: Cyclic amide hydrolase DEG5Y4W EC 3.5.2.6 DEG5Y4W SQ EGTEGCFLLYDASTNAEIAQFNKAKCATQMAPDSTFKIALSLMAFDAEIIDQKTIFKWDKTPKGMEIWNSNHTPKTWMQFSVVWVSQEITQKIGLNKIKNYLKDFDYGNQDFSGDKERNNGLTEAWLESSLKISPEEQIQFLRKIINHNLPVKNSAIENTIENMYLQDLDNSTKLYGKTGAGFTANRTLQNGWFEGFIISKSGHKYVFVSALTGNLGSNLTSSIKAKKNAITILNTLNL DEG5Y4W TD Primarily distributed in human oral cavity. DEG5Y4W FC This enzyme hydrolyzes beta-lactam. DEG5Y4W KD 2: Bacteria DEG5Y4W PL 1239: Firmicutes DEG5Y4W CL 91061: Bacilli DEG5Y4W OD 1385: Bacillales DEG5Y4W FM 90964: Staphylococcaceae DEG5Y4W GE 1279: Staphylococcus DEG5Y4W SP 1280: Staphylococcus aureus DEF01WC ID DEF01WC DEF01WC DN Beta-lactamase (blaB) DEF01WC GN ampC DEF01WC SN Penicillinase; Cephalosporinase; Beta-lactam; NCTC9695_01822 DEF01WC UC A0A3S4HKA9_CHRVL DEF01WC RD Cefoxitin DEF01WC E1 3: Hydrolases DEF01WC E2 3.5: Carbon-nitrogen hydrolase DEF01WC E3 3.5.2: Cyclic amide hydrolase DEF01WC EC 3.5.2.6 DEF01WC SQ MMQSLKFRTLAGMLGCLTFLPLAAQAANDAGKSDLDAAVEATIPPLMKAKDIPGMAVAVLADGKAHYFNYGVASRETGQPVTQDTLFELGSISKTFTGILGGYALAQGKLSLADKASRYQPELKGSVFDRVSLLQLATYSAGGLPLQFPDAVAGQASMLAYYRGWKPDYAPGERRLYSNPSIGLFGHLAARSLGQPFDQAMERGLLPKLGLSHTFIHVPEAEQSRYAWGYAKAGKPIRVGAGVLDAEAYGIKSSAADLLKYLAINMSPPADPALQRALDASHAAYYRVGDMRQGLGWEGYRYPISLERLLAGNSNEIAFQPQKVEWLNPPRLAEGDVLLNKTGSTSGFGAYVLFVPARKVGIVMLANRNYPNAERVRAAYRILLAVDPSLARRRGD DEF01WC TD Primarily distributed in human skin. DEF01WC FC This enzyme hydrolyzes beta-lactam. DEF01WC KD 2: Bacteria DEF01WC PL 1224: Proteobacteria DEF01WC CL 28216: Betaproteobacteria DEF01WC OD 206351: Neisseriales DEF01WC FM 1499392: Chromobacteriaceae DEF01WC GE 535: Chromobacterium DEF01WC SP 536: Chromobacterium violaceum DE2IMU4 ID DE2IMU4 DE2IMU4 DN Beta-glucuronidase (uidA) DE2IMU4 GN uidA DE2IMU4 SN Beta-galactosidase/beta-glucuronidase; Beta-galactosidase BgaB; JFP838_00890 DE2IMU4 UC A0A127EEJ8_CLOPF DE2IMU4 RD SN-38G DE2IMU4 E1 3: Hydrolases DE2IMU4 E2 3.2: Glycosylase DE2IMU4 E3 3.2.1: O/S-glycosyl compound glycosidase DE2IMU4 EC 3.2.1.31 DE2IMU4 SQ MLYPIITESRQLIDLSGIWKFKLNEGNGLTEELSKAPLKDTIEMAVPSSYNDLVESQEVRDHVGWVWYERNFTIPKTLLNERIVLRFGSATHEAKVYLNGELLVEHKGGFTPFEAEINNLLVSGDNRLTVAVNNIIDETTLPVGLVKEVEVDGKKVIKNSVNFDFFNYAGIHRPVKIYTTPKSYVEDITIVTDFKENNGYVNYEVQAVGKCNIKVTIIDEENNIVAEGEGESGKLTINNVHLWEPMNAYLYKLKVELLDDEEIIDTYFEEFGVRTVEVKDGKFLINNKPFYFKGFGKHEDSYVNGRGINEAINIKDFNLMKWIGANSFRTSHYPYSEEIMRLADREGIVVIDETPAVGLHLNFMATGFGGDATKRDTWKEIGTKEAHERILRELVSRDKNHPCVVMWSVANEPDSDSEGAKEYFEPLIKLTKELDPQKRPVTVVTYLMSTPDRCKVGDIVDVLCLNRYYGWYVAGGDLEEAKRMLEDELKGWEERCPNTPIMFTEYGADTVAGLHDTVPVMFTEEYQVEYYKANHEVMDKCKNFVGEQVWNFADFATSQGIIRVQGNKKGIFTRERKPKMIAHSLRERWTNIPEFGYKK DE2IMU4 TD Primarily distributed in human gut. DE2IMU4 FC This enzyme takes part in glucuronoside catabolic process. It catalyzes the hydrolysis of beta-glucuronide containing substrates. DE2IMU4 KD 2: Bacteria DE2IMU4 PL 1239: Firmicutes DE2IMU4 CL 186801: Clostridia DE2IMU4 OD 186802: Clostridiales DE2IMU4 FM 31979: Clostridiaceae DE2IMU4 GE 1485: Clostridium DE2IMU4 SP 1502: Clostridium perfringens DE7Y39R ID DE7Y39R DE7Y39R DN Beta-glucuronidase (uidA) DE7Y39R GN uidA DE7Y39R SN Beta-galactosidase/beta-glucuronidase; Beta-galactosidase BgaB; BGK71_00200; CCE29_06935; FEZ43_12625; NCTC13710_00049; PY91_01090; uidA DE7Y39R UC A0A2A5L2J1_LACRH DE7Y39R RD Diclofenac glucuronide DE7Y39R GI 8420464 DE7Y39R E1 3: Hydrolases DE7Y39R E2 3.2: Glycosylase DE7Y39R E3 3.2.1: O/S-glycosyl compound glycosidase DE7Y39R EC 3.2.1.31 DE7Y39R PD 6ECA DE7Y39R SQ METSLLYPVTNDQRTDQKLDGLWQFKFDEAGEGEKSGWETGFHDGVSMPVPASFNDFFTDKASREYTGDFWYSRNFFVPSAAKGKALFLRFDAVTHRATIFVNGKEIRTHEGGFLPFAADISEAVKYGAENTVVVKGNNELSREALPAGDTITLRNGKKMVRPFFDFYNYSGLNRSVHLLSLPQERVLDYTTTFALAGNDATVNYTVETNGDAPVTVSLADADGQVVATAQGKQGALQVQNAHLWQVRNAYLYTLTIQLGDDTQTPLDTYTDRIGIRTIKISGTDILVNDKPIYLKGFGRHEDSPFAGRAFDLNVEKKDFALMKWIGANSFRTSHYPYDEQVYKIADEEGFLLTDEVPAVGFKMAAAAFLGGLNQSFFKGPWLKKLHERHIDQIRDLIKRDKNHPSVLAWSLFNEPDTIDENAVPYFKQIFDESKDLDPQGRPRTFTLSEDDTIETSKVLDFPDFYMLNRYPGWYHFGGYQISDGEAGLRDEMDKWQKAGVKKPVVFTEFGADTEAGLHKLPSVMWTEEYQVEVLKMFSRVFDDYDFIKGEQVWNLADFQTVEGNMRVNGNKKGIFTRDRQPKAAAFFYHDRWNKLPLDYKAK DE7Y39R TD Primarily distributed in human gut. DE7Y39R FC This enzyme takes part in glucuronoside catabolic process. It catalyzes the hydrolysis of beta-glucuronide containing substrates. DE7Y39R KD 2: Bacteria DE7Y39R PL 1239: Firmicutes DE7Y39R CL 91061: Bacilli DE7Y39R OD 186826: Lactobacillales DE7Y39R FM 33958: Lactobacillaceae DE7Y39R GE 1578: Lactobacillus DE7Y39R SP 47715: Lactobacillus rhamnosus DERFVMW ID DERFVMW DERFVMW DN Beta-glucuronidase (uidA) DERFVMW GN uidA DERFVMW SN Beta-galactosidase/beta-glucuronidase; Beta-galactosidase BgaB; AX245_05480; E8E04_02325; F5F86_07650; uidA DERFVMW UC A0A0E1EGE5_STRAG DERFVMW RD SN-38G DERFVMW E1 3: Hydrolases DERFVMW E2 3.2: Glycosylase DERFVMW E3 3.2.1: O/S-glycosyl compound glycosidase DERFVMW EC 3.2.1.31 DERFVMW KG Biosynthesis of secondary metabolites:sage01110; Metabolic pathways:sage01100; Pentose and glucuronate interconversions:sage00040 DERFVMW SQ MLYPLLTKTRNTYDLGGIWNFKLGEHNPNELLPSDEVMVIPTSFNDLMVSKEKRDYIGDFWYEKVIEVPKVSEGEEMVLRFGSVTHQAKIYVDGILVGEHKGGFTPFEVLVPECKYNNEKIKVSICANNVLDYTTLPVGNYSEIIQEDGSIKKKVRENFDFFNYAGVHRPLKLMIRPKNHISDITITSRLSDDLQSADLHFLVETNQKVDEVRISVFDEDNKLVGETKDSRLFLSDVHLWEVLNAYLYTARVEIFVDNQLQDVYEENFGLREIEVTNGQFLLNRKPIYFKGFGKHEDTFINGRGLNEAANLMDLNLLKDIGANSFRTSHYPYSEEMMRLADRMGVLVIDEVPAVGLFQNFNASLDLSPKDNGTWSLMQTKAAHEQAIQELVKRDKNHPSVVMWVVANEPASHEAGAHDYFEPLVKLYKDLDPQKRPVTLVNILMATPDRDQVMDLVDVVCLNRYYGWYVDHGDLTNAEVGLRKELLEWQDKFPDKPIIITEYGADTLPGLHSTWNIPYTEEFQCDFYEMSHRVFDGIPNLVGEQVWNFADFETNLMILRVQGNHKGLFSRNRQPKQVVKEFKKRWMTIPHYHNKKNSVK DERFVMW TD Primarily distributed in human gut. DERFVMW FC This enzyme takes part in glucuronoside catabolic process. It catalyzes the hydrolysis of beta-glucuronide containing substrates. DERFVMW KD 2: Bacteria DERFVMW PL 1239: Firmicutes DERFVMW CL 91061: Bacilli DERFVMW OD 186826: Lactobacillales DERFVMW FM 1300: Streptococcaceae DERFVMW GE 1301: Streptococcus DERFVMW SP 1311: Streptococcus agalactiae DEXLYGD ID DEXLYGD DEXLYGD DN Beta-glucosidase (bglA) DEXLYGD GN beta-glucosidaseA DEXLYGD SN Periplasmic beta-glucosidase; Glucan endo-1 3-beta-D-glucosidase; Beta-D-glucosidase; Beta-glucosidase A DEXLYGD UC Q9ZNN7_BACSP DEXLYGD RD AS-35335 DEXLYGD E1 3: Hydrolases DEXLYGD E2 3.2: Glycosylase DEXLYGD E3 3.2.1: O/S-glycosyl compound glycosidase DEXLYGD EC 3.2.1.21 DEXLYGD SQ MASIQFPKDFVWGTATASYQIEGAYNEDGRGMSIWDTFSRTPGKVVNGDTGDIACDSYHRYEEDIALLKNLGVKAYRFSIAWPRIYPDGDGELNQKGLDYYAKVIDGLLAAGIEPCVTLYHWDLPQALQDKGGWDNRDTIRAFVRYAETAFKAFGGKVKQWITFNETWCVSFLSNYIGAHAPGNTDLQLAVNVAHNCMVAHGEAVKAFRALGISGEIGTTHNLYWFEPYTTKPEDVAAAHRNRAYNNEWFMDPTFKGQYPQFMVDWFKGKGVEVPIQPGDMETIAQPIDFIGVNFYSGGFGRYKEGEGLFDCEEVQVGFDKTFMDWNVYAEGLYKVLSWVHEEYGDVPIYITENGACYEDELTQEGRVHDAKRADYFKKHFIQCHRLIESGVPLKGYFAWSLLDNFEWAEGYVKRFGIVYTDYKTLKRYPKDSYRFIQSVIENDGFEA DEXLYGD TD Primarily distributed in human gut. DEXLYGD FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DEXLYGD KD 2: Bacteria DEXLYGD PL 1239: Firmicutes DEXLYGD CL 91061: Bacilli DEXLYGD OD 1385: Bacillales DEXLYGD FM 186817: Bacillaceae DEXLYGD GE 1386: Bacillus DEXLYGD SP 1423: Bacillus subtilis DEUQTKA ID DEUQTKA DEUQTKA DN Beta-glucosidase (bglA) DEUQTKA GN bglA DEUQTKA SN Periplasmic beta-glucosidase; Glucan endo-1 3-beta-D-glucosidase; Beta-D-glucosidase; BGK71_01895 DEUQTKA UC A0A249DCH3_LACRH DEUQTKA RD CCG-208408 DEUQTKA E1 3: Hydrolases DEUQTKA E2 3.2: Glycosylase DEUQTKA E3 3.2.1: O/S-glycosyl compound glycosidase DEUQTKA EC 3.2.1.21 DEUQTKA SQ MTQQQLYTPKGFPKNFLWGGAIAANQAEGAWQTDGRGPSQADIMLLPEKYSRLGSFGEHVTRADIERALADKSGNYPRRRGIDFFHTYDSDLDLMKEMGFNTFRTSFSWSRIFPNGDEKEPNEKGLKFYDKLIQKMLDLDITPVMTISHYEMPLNLITKYGGWENPEMINFFNRFAQVLLDRYHDKVKYWIVFNQVNDVYGWGEFAGLGILKENQPNEKQAKFQAVHHQFIANAQTVKYGHQIDNDIKIGMMLGLTNVYPASTKPQDVMATYKRWNKDTFFFSDVLARGEYPGYMLRYFEDNNIQLSIDQKELDLIKNNPVDFIAFSYYSSSLISADTPDSLLPNPELEESIWGWSFDPIGFRYGFNVLWDRYHLPLFVAENGLGALDTVEDNKIHDAYRIKYLKAHIKQMKEAIKDGVHIFGYAAWGPIDIVSYSQAEMSKRYGFVYVDLDDKGNGTGKRIRKDSFYWYQKVIESNGDQI DEUQTKA TD Primarily distributed in human gut. DEUQTKA FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DEUQTKA KD 2: Bacteria DEUQTKA PL 1239: Firmicutes DEUQTKA CL 91061: Bacilli DEUQTKA OD 186826: Lactobacillales DEUQTKA FM 33958: Lactobacillaceae DEUQTKA GE 1578: Lactobacillus DEUQTKA SP 47715: Lactobacillus rhamnosus DEUQTKA SU Lactobacillus rhamnosus HN001; Lactobacillus rhamnosus subsp. Rhamnosus NCTC 10302 DEE8WXK ID DEE8WXK DEE8WXK DN Beta-glucosidase (bglA) DEE8WXK GN bglA DEE8WXK SN Periplasmic beta-glucosidase; Glucan endo-1 3-beta-D-glucosidase; Beta-D-glucosidase; BADO_0074; ERS852419_00699; LU08_00495 DEE8WXK UC A0A076JJU4_BIFAD DEE8WXK RD Ginsenoside Rb1 DEE8WXK E1 3: Hydrolases DEE8WXK E2 3.2: Glycosylase DEE8WXK E3 3.2.1: O/S-glycosyl compound glycosidase DEE8WXK EC 3.2.1.21 DEE8WXK KG Biosynthesis of secondary metabolites:badl01110; Cyanoamino acid metabolism:badl00460; Metabolic pathways:badl01100; Starch and sucrose metabolism:badl00500 DEE8WXK SQ MTLTFPQDFTFGTATAAYQIEGAVTEDGRCPSIWDTFSHTPGATIAGDTGDVATDSYHRWREDLALLKDLGVDAYRFSIAVPRIISTPDGVPNEKGLDFYEGVVDALLEAGIKPVVTLYHWDLPQYLGDEGGWLNRRTAYALADYAGIVAKRLGDRVDTWTTLNEPWCSSYLSYGAKEHAPGLGLGPGAFPAVHHLNLAHGLMTQAVRAEVGDKAKCSVTLNLQFNRGDADACHRLDLISNRAFLDPMLRGRYPDELFSITKGICDWDFIQSGDLELIHQPIDVLGINYYSTNRVAMSDRPQFPQSTEASTAPGASDVDWLPTEGPHTDMGWNIDPDGLHDLLVRVHDNYPEVDLVVTENGMACKDQLTVNEDGTKSVHDPDRIDYLKRHFAAAKRAIDEGVPLTGYFVWSLLDNFEWYFGYAKRFGITYVDYATQERIPKDSFMWYRDFLASRKG DEE8WXK TD Primarily distributed in human gut. DEE8WXK FC This enzyme has wide specificity for beta-D-glucosides such as beta-D-galactosides, alpha-L-arabinosides, beta-D-xylosides, beta-D-fucosides. DEE8WXK KD 2: Bacteria DEE8WXK PL 201174: Actinobacteria DEE8WXK CL 1760: Actinobacteria DEE8WXK OD 85004: Bifidobacteriales DEE8WXK FM 31953: Bifidobacteriaceae DEE8WXK GE 1678: Bifidobacterium DEE8WXK SP 1680: Bifidobacterium adolescentis DEBUN2V ID DEBUN2V DEBUN2V DN Beta-galactosidase (bgaB) DEBUN2V GN lacA DEBUN2V SN Beta-galactosidase/glucuronidase; Beta-galactosidase BgaBeta; Beta-Gal II; Beta-gal; lacA DEBUN2V UC BGAL2_LACAI DEBUN2V RD Raffinose DEBUN2V E1 3: Hydrolases DEBUN2V E2 3.2: Glycosylase DEBUN2V E3 3.2.1: O/S-glycosyl compound glycosidase DEBUN2V EC 3.2.1.23 DEBUN2V SQ MTQLSRFLYGGDYNPDQWPEETWSKDIHVFKKADINSATINIFSWALLEPREGKYNFSKLDKVVQQLSDANFDIVMGTATAAMPAWMFKKYPDIARVDYQDRRHVFGQRHNFCPNSSNYQRLAGELEKQLVERYKDNKHIVFWHINNEYGGNCYCENCQNAFKKWLKNKYKTVEGLNKAWNMNVWSHTIYDWDEIVVPNELGDVWGIKGSETIVAGLSIDYLRFQSESMQNLFKMEKKIIKKFDPETPVTTNFHGLPNKMVDYQKWAKGQDIISYDSYPTYDAPAYKAAFLYDLMRSLKHQPFMLMESAPSQVNWQPYSPLK