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Predicate	Value (sorted: default)
rdfs:label	"S-Mercaptocysteine"
rdf:type	drugbank:drugs
drugbank:description	" 5652-32-4 experimental This compound belongs to the alpha amino acids and derivatives. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon), or a derivative thereof. Alpha Amino Acids and Derivatives Organic Compounds Organic Acids and Derivatives Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Organic Disulfides Polyamines Enolates Carboxylic Acids Monoalkylamines organic disulfide polyamine enolate carboxylic acid primary amine amine organonitrogen compound primary aliphatic amine logP -2 ALOGPS logS -1 ALOGPS Water Solubility 1.43e+01 g/l ALOGPS logP -2.4 ChemAxon IUPAC Name (2R)-2-amino-3-disulfanylpropanoic acid ChemAxon Traditional IUPAC Name S-mercaptocysteine ChemAxon Molecular Weight 153.223 ChemAxon Monoisotopic Weight 152.991819853 ChemAxon SMILES N[C@@H](CSS)C(O)=O ChemAxon Molecular Formula C3H7NO2S2 ChemAxon InChI InChI=1S/C3H7NO2S2/c4-2(1-8-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1 ChemAxon InChIKey InChIKey=XBKONSCREBSMCS-REOHCLBHSA-N ChemAxon Polar Surface Area (PSA) 63.32 ChemAxon Refractivity 33.99 ChemAxon Polarizability 14.3 ChemAxon Rotatable Bond Count 3 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 2.04 ChemAxon pKa (strongest basic) 8.9 ChemAxon Physiological Charge 0 ChemAxon Number of Rings 0 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon ChEBI 28839 PubChem Compound 165331 PubChem Substance 46505635 KEGG Compound C01962 ChemSpider 3818714 PDB CSS BE0002377 3-mercaptopyruvate sulfurtransferase Leishmania major unknown 3-mercaptopyruvate sulfurtransferase Inorganic ion transport and metabolism MST None 6.29 40155.0 Leishmania major GenBank Gene Database AJ313201 UniProtKB Q7K9G0 UniProt Accession Q7K9G0_LEIMA EC 2.8.1.2 >Mercaptopyruvate sulfurtransferase MSAPAAAPKHPGKVFLDPSEVKDHLAEYRIVDCRYSLKIKDHGSIQYAKEHVKSAIRADV DTNLSKLVPTSTARHPLPPCAEFIDWCMANGMAGELPVLCYDDECGAMGGCRLWWMLNSL GADAYVINGGFQACKAAGLEMESGEPSSLPRPATHWPFKTAFQHHYLVDEIPPNAIITDA RSADRFASTVRPYAADKMPGHIEGARNLPYTSHLVTRGDGKVLRSEEEIRHNIMTVVQGA GDAADLSSFVFSCGSGVTACINIALVHHLGLGHPYLYCGSWSEYSGLFRPPIMRSIIDDY GMCMQMQTPSLGDNPKANLDTMTLKVDGAPCERPDAEVQSAATHLHAGEAATVYFKSGRV VTIEVPAVPN >1113 bp ATGTCTGCTCCTGCTGCTGCGCCGAAACACCCGGGCAAGGTGTTCCTGGACCCGAGCGAG GTAAAGGACCACCTTGCTGAGTACCGCATCGTGGACTGCCGGTACAGCTTGAAGATAAAG GACCACGGCAGCATCCAGTACGCGAAGGAGCACGTGAAGAGCGCCATCCGCGCCGATGTG GATACGAACCTCTCTAAGTTGGTGCCCACCAGCACCGCCCGGCATCCGCTACCGCCCTGT GCTGAGTTTATCGACTGGTGCATGGCGAACGGGATGGCGGGAGAGCTGCCAGTGCTCTGC TACGATGACGAGTGCGGCGCCATGGGTGGATGCCGCCTGTGGTGGATGCTGAACTCTCTT GGCGCCGACGCGTACGTGATCAACGGCGGCTTTCAGGCCTGCAAGGCTGCGGGGCTGGAG ATGGAGTCCGGCGAGCCCTCGTCGCTGCCAAGACCCGCAACGCACTGGCCCTTCAAGACG GCCTTTCAGCATCACTACCTTGTGGATGAAATCCCGCCCAACGCAATCATCACCGACGCG CGCTCCGCCGACCGCTTCGCCTCGACAGTACGACCTTACGCCGCAGACAAGATGCCAGGC CACATCGAAGGTGCGCGTAACCTCCCCTACACGTCGCACCTCGTGACACGCGGTGACGGC AAGGTGCTGCGCAGTGAGGAAGAGATCCGCCACAACATCATGACCGTCGTGCAAGGCGCG GGTGACGCGGCTGATCTATCGAGCTTCGTCTTCTCCTGCGGCAGCGGCGTCACCGCCTGC ATCAATATCGCCCTGGTGCACCACCTCGGCCTGGGCCATCCGTACCTCTACTGTGGCTCC TGGTCTGAGTACAGCGGCCTCTTCCGCCCCCCCATAATGCGCAGCATCATCGACGACTAC GGCATGTGCATGCAAATGCAGACCCCTAGCCTCGGCGACAACCCGAAGGCAAACCTCGAC ACCATGACGCTGAAGGTCGACGGCGCGCCCTGCGAGAGACCCGATGCGGAGGTGCAGAGC GCCGCAACCCACCTCCACGCTGGCGAGGCCGCTACCGTGTACTTCAAGAGCGGCCGCGTC GTCACGATCGAGGTGCCGGCAGTGCCCAACTAA BE0002823 L-cysteine/cystine lyase C-DES Synechocystis sp. (strain PCC 6714) unknown L-cysteine/cystine lyase C-DES Involved in transaminase activity c-des None 6.1 43155.0 Synechocystis sp. (strain PCC 6714) GenBank Gene Database AF061964 UniProtKB Q9ZHG9 UniProt Accession Q9ZHG9_SYNY4 >L-cysteine/cystine lyase C-DES MADPVNLIPDRHQFPGLANKTYFNFGGQGILPTVALEAITAMYGYLQENGPFSIAANQHI QQLIAQLRQALAETFNVDPNTITITDNVTTGCDIVLWGLDWHQGDEILLTDCEHPGIIAI VQAIAARFGITYRFFPVAATLNQGDAAAVLANHLGPKTRLVILSHLLWNTGQVLPLAEIM AVCRRHQGNYPVRVLVDGAQSAGSLPLDFSRLEVDYYAFTGHKWFAGPAGVGGLYIHGDC LGEINPTYVGWRSITYGAKGEPTGWAEGGKRFEVATSAYPQYAGLLAALQLHQRQGTAEE RYQAICQRSEFLWRGLNQLPHVHCLATSAPQAGLVSFTVDSPLGHRAIVQKLEEQRIYLR TIADPDCIRACCHYITDEEEINHLLARLADFGP >1182 bp ATGGCTGACCCTGTGAACCTAATACCCGATCGCCACCAATTTCCTGGCCTAGCCAATAAG ACCTATTTTAATTTTGGCGGCCAGGGTATTTTGCCCACCGTTGCCCTGGAAGCTATTACG GCTATGTATGGCTATCTACAGGAAAATGGCCCTTTTTCCATTGCCGCTAATCAACATATT CAGCAGTTAATTGCCCAACTACGGCAGGCTTTGGCGGAAACTTTTAACGTTGATCCCAAC ACAATTACAATCACCGATAACGTCACCACCGGCTGTGACATTGTGCTTTGGGGTTTGGAT TGGCACCAGGGCGATGAAATTTTGCTCACCGACTGCGAACATCCCGGCATCATTGCCATT GTCCAGGCGATCGCCGCCCGGTTTGGCATTACCTACCGTTTTTTCCCGGTGGCGGCCACG TTAAACCAGGGAGATGCGGCCGCAGTGTTGGCTAATCATCTGGGGCCAAAAACCCGCTTG GTTATTCTCAGTCATTTACTCTGGAACACTGGCCAAGTATTGCCCCTAGCAGAAATTATG GCCGTTTGTCGCCGTCACCAAGGAAATTATCCAGTGCGGGTTTTAGTGGATGGGGCCCAA TCTGCCGGTTCCTTACCCCTAGATTTTTCCCGGTTAGAAGTGGATTATTATGCTTTCACC GGCCATAAATGGTTTGCTGGCCCCGCTGGGGTGGGGGGATTGTATATCCATGGCGATTGC CTGGGGGAAATTAATCCGACCTATGTGGGTTGGCGCAGTATCACCTATGGCGCTAAAGGG GAACCCACCGGCTGGGCTGAAGGGGGCAAACGGTTTGAAGTGGCCACCTCCGCCTATCCC CAATATGCCGGTCTGTTGGCCGCTCTCCAGTTGCACCAACGGCAAGGCACCGCTGAGGAA CGTTACCAAGCCATTTGTCAACGTAGTGAATTCCTGTGGCGGGGCTTGAACCAGTTACCC CATGTCCATTGTTTAGCTACATCGGCTCCCCAAGCAGGTTTGGTCTCCTTCACCGTGGAT TCTCCCTTGGGCCACCGGGCGATCGTGCAGAAACTGGAGGAGCAACGCATCTATCTCCGT ACCATCGCTGACCCTGACTGTATCCGGGCCTGTTGCCATTACATAACCGATGAGGAGGAA ATTAATCATTTATTGGCTAGACTAGCTGACTTTGGCCCCTAA PF00266 Aminotran_5 function transferase activity function transferase activity, transferring nitrogenous groups function transaminase activity function catalytic activity process metabolism process physiological process BE0002824 3-mercaptopyruvate sulfurtransferase Escherichia coli (strain K12) unknown 3-mercaptopyruvate sulfurtransferase Involved in thiosulfate sulfurtransferase activity Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity sseA Cytoplasm (Probable) None 4.3 30812.0 Escherichia coli (strain K12) GenBank Gene Database AP009048 UniProtKB P31142 UniProt Accession THTM_ECOLI EC 2.8.1.2 MST Rhodanese-like protein >3-mercaptopyruvate sulfurtransferase MSTTWFVGADWLAEHIDDPEIQIIDARMASPGQEDRNVAQEYLNGHIPGAVFFDIEALSD HTSPLPHMLPRPETFAVAMRELGVNQDKHLIVYDEGNLFSAPRAWWMLRTFGVEKVSILG GGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVKVTDVLLASHENTAQIIDARPAARF NAEVDEPRPGLRRGHIPGALNVPWTELVREGELKTTDELDAIFFGRGVSYDKPIIVSCGS GVTAAVVLLALATLDVPNVKLYDGAWSEWGARADLPVEPVK >843 bp TCCACGACATGGTTTGTAGGAGCCGACTGGCTCGCCGAACATATTGATGACCCGGAAATT CAGATTATCGATGCCCGCATGGCGTCGCCTGGACAGGAGGATCGTAACGTTGCTCAGGAG TATCTGAATGGACATATTCCCGGCGCAGTGTTTTTTGATATCGAAGCGCTTTCTGATCAC ACTTCCCCGCTTCCGCACATGCTGCCGCGCCCGGAAACGTTCGCCGTGGCGATGCGTGAA TTAGGCGTTAACCAGGATAAGCACCTGATTGTCTATGACGAAGGTAATCTTTTCTCAGCC CCACGAGCATGGTGGATGCTGCGCACCTTTGGTGTAGAGAAAGTGTCGATTCTGGGGGGT GGACTTGCAGGCTGGCAGCGCGATGATCTGCTGTTAGAAGAAGGTGCAGTAGAGCTGCCG GAAGGAGAGTTTAACGCCGCGTTTAATCCTGAAGCCGTGGTGAAAGTAACCGATGTATTA TTGGCAAGCCATGAAAATACGGCGCAAATTATTGATGCCCGCCCGGCTGCACGTTTTAAC GCAGAAGTTGATGAACCTCGCCCAGGTTTACGTCGCGGACATATTCCCGGAGCACTGAAT GTTCCGTGGACGGAACTGGTGCGCGAAGGCGAACTAAAAACGACCGATGAACTGGATGCG ATATTTTTTGGTCGCGGCGTCAGCTACGACAAACCAATTATCGTCAGCTGCGGCTCTGGT GTAACGGCAGCCGTGGTTTTGTTAGCACTCGCGACGCTGGATGTGCCAAACGTGAAACTG TACGACGGCGCATGGAGTGAATGGGGCGCGCGGGCAGATTTACCGGTTGAGCCAGTGAAA TAA PF00581 Rhodanese function catalytic activity function transferase activity function transferase activity, transferring sulfur-containing groups function sulfurtransferase activity function thiosulfate sulfurtransferase activity process transport process ion transport process anion transport process inorganic anion transport process physiological process process sulfate transport process cellular physiological process BE0002825 Hydroxylamine reductase Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) unknown Hydroxylamine reductase Involved in oxidoreductase activity, acting on other nitrogenous compounds as donors Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O (By similarity) hcp Cytoplasm None 5.29 59980.0 Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) GenBank Gene Database Z11707 UniProtKB P31101 UniProt Accession HCP_DESVH EC 1.7.-.- HCP Hybrid-cluster protein Prismane protein >Hydroxylamine reductase MFCFQCQETAKNTGCTVKGMCGKPEETANLQDLLIFVLRGIAIYGEKLKELGQPDRSNDD FVLQGLFATITNANWDDARFEAMISEGLARRDKLRNAFLAVYKAKNGKDFSEPLPEAATW TGDSTAFAEKAKSVGILATENEDVRSLRELLIIGLKGVAAYAEHAAVLGFRKTEIDEFML EALASTTKDLSVDEMVALVMKAGGMAVTTMALLDEANTTTYGNPEITQVNIGVGKNPGIL ISGHDLKDMAELLKQTEGTGVDVYTHGEMLPANYYPAFKKYPHFVGNYGGSWWQQNPEFE SFNGPILLTTNCLVPLKKENTYLDRLYTTGVVGYEGAKHIADRPAGGAKDFSALIAQAKK CPPPVEIETGSIVGGFAHHQVLALADKVVEAVKSGAIKRFVVMAGCDGRQKSRSYYTEVA ENLPKDTVILTAGCAKYRYNKLNLGDIGGIPRVLDAGQCNDSYSLAVIALKLKEVFGLDD INDLPVSYDIAWYEQKAVAVLLALLFLGVKGIRLGPTLPAFLSPNVAKVLVENFNIKPIG TVQDDIAAMMAGK >1662 bp ATGTTTTGCTTCCAGTGTCAGGAAACAGCGAAGAATACGGGATGCACGGTCAAAGGTATG TGCGGCAAGCCGGAAGAAACCGCCAATTTGCAGGATCTGCTCATTTTTGTGCTGCGTGGC ATCGCCATTTATGGCGAAAAATTAAAGGAGTTGGGACAGCCGGACCGCTCTAATGACGAC TTCGTGCTCCAGGGATTATTTGCGACCATCACCAATGCTAACTGGGATGATGCCCGATTT GAGGCTATGATATCGGAAGGCTTGGCTCGGCGTGACAAGTTGAGAAATGCTTTTCTGGCT GTTTACAAGGCAAAAAATGGCAAAGATTTCAGCGAGCCGTTGCCCGAAGCCGCGACTTGG ACTGGGGACTCTACCGCTTTTGCTGAAAAGGCCAAGAGCGTAGGCATTCTGGCAACTGAG AACGAAGATGTGCGTTCTTTGCGCGAACTGCTCATAATCGGTCTGAAAGGTGTCGCGGCC TATGCCGAGCACGCTGCTGTACTGGGCTTTCGCAAGACCGAAATCGACGAATTCATGCTT GAGGCCCTGGCTTCAACGACCAAGGATTTGTCCGTGGATGAAATGGTCGCGCTGGTCATG AAGGCCGGCGGCATGGCCGTAACCACCATGGCCCTGCTGGACGAGGCCAACACCACTACC TACGGCAACCCGGAAATCACCCAGGTCAACATCGGCGTGGGCAAGAACCCCGGCATCCTC ATCAGCGGCCATGACCTGAAGGATATGGCCGAGTTGCTGAAGCAGACCGAGGGCACAGGC GTGGACGTTTACACCCACGGCGAAATGCTTCCCGCCAACTATTATCCGGCGTTCAAGAAG TACCCGCATTTCGTGGGGAACTACGGCGGTTCCTGGTGGCAGCAGAATCCCGAATTCGAG TCCTTCAACGGCCCCATCCTGCTGACCACAAACTGTCTGGTGCCGCTCAAAAAAGAGAAC ACCTATCTGGACCGTCTCTACACCACTGGCGTGGTTGGGTATGAAGGGGCCAAGCACATC GCTGACCGGCCTGCGGGAGGAGCCAAGGATTTCTCGGCGCTGATCGCACAGGCCAAGAAA TGTCCTCCGCCCGTTGAGATCGAGACTGGTAGCATCGTCGGCGGTTTCGCCCATCATCAG GTACTAGCCTTGGCCGACAAGGTGGTTGAGGCTGTCAAGTCCGGCGCGATCAAGCGCTTT GTGGTCATGGCCGGGTGTGACGGTCGGCAGAAGTCTCGTTCCTATTACACTGAAGTGGCC GAAAATTTGCCCAAGGACACCGTGATCTTGACGGCCGGTTGCGCCAAGTACCGCTATAAC AAACTGAATCTCGGTGACATCGGTGGCATTCCACGTGTGCTGGACGCAGGGCAGTGCAAC GATTCCTATTCCCTGGCCGTCATTGCTCTGAAACTCAAAGAAGTCTTCGGCCTGGATGAC ATCAACGATCTGCCCGTATCTTACGATATCGCCTGGTACGAGCAGAAGGCCGTGGCCGTG CTTCTGGCCCTCCTATTCTTAGGTGTGAAGGGAATCCGCCTCGGACCCACGCTTCCGGCA TTCCTGTCCCCGAACGTGGCCAAGGTACTGGTTGAAAATTTCAACATCAAACCAATCGGA ACAGTGCAGGATGACATCGCGGCCATGATGGCGGGTAAATAG PF03063 Prismane component cell component intracellular component cytoplasm function oxidoreductase activity function ion binding function cation binding function transition metal ion binding function iron ion binding function binding function catalytic activity function oxidoreductase activity, acting on other nitrogenous compounds as donors process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism BE0004455 Thiosulfate sulfurtransferase Human # Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10592235 unknown Thiosulfate sulfurtransferase TST Human UniProtKB Q16762 UniProt Accession THTR_HUMAN BE0002826 Sulfurtransferase Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) unknown Sulfurtransferase Involved in thiosulfate sulfurtransferase activity TTHA1028 None 5.14 32925.0 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) GenBank Gene Database AP008226 UniProtKB Q5SJI0 UniProt Accession Q5SJI0_THET8 >Thiosulfate sulfurtransferase MGYAHPEVLVSTDWVQEHLEDPKVRVLEVDEDILLYDTGHIPGAQKIDWQRDFWDPVVRD FISEEEFAKLMERLGISNDTTVVLYGDKNNWWAAYAFWFFKYNGHKDVRLMNGGRQKWVE EGRPLTTEVPSYPPGRYEVPYRDESIRAYRDDVLEHIIKVKEGKGALVDVRSPQEYRGEL THMPDYPQEGALRAGHIPGAKNIPWAKAVNPDGTFKSAEELRALYEPLGITKDKDIVVYC RIAERSSHSWFVLKYLLGYPHVKNYDGSWTEWGNLVGVPIAKGEE >858 bp ATGGGGTACGCCCATCCCGAGGTTTTGGTGAGCACCGACTGGGTCCAGGAGCACCTGGAG GACCCCAAGGTACGGGTCCTCGAGGTGGACGAGGACATCCTCCTCTACGACACCGGGCAC ATCCCGGGGGCCCAGAAGATTGACTGGCAGCGGGACTTCTGGGACCCGGTGGTCCGGGAC TTCATCAGCGAGGAGGAGTTCGCCAAGCTCATGGAAAGGCTCGGCATCTCCAACGACACC ACCGTGGTCCTCTACGGGGACAAGAACAACTGGTGGGCCGCCTACGCCTTCTGGTTCTTC AAGTACAACGGCCACAAGGACGTGCGGCTCATGAACGGCGGGCGGCAAAAGTGGGTGGAG GAAGGCCGCCCCCTCACCACCGAGGTCCCCTCCTACCCCCCGGGGCGCTACGAGGTCCCC TACCGGGACGAGTCCATCCGGGCCTACCGGGACGACGTCCTGGAGCACATCATCAAGGTG AAGGAAGGCAAGGGCGCCCTGGTGGACGTGCGTAGCCCCCAGGAGTACCGCGGGGAGCTC ACCCACATGCCCGACTACCCCCAGGAGGGGGCCCTCCGCGCCGGCCACATCCCCGGGGCG AAGAACATCCCCTGGGCCAAAGCGGTGAACCCCGACGGCACCTTCAAAAGCGCCGAGGAG CTCCGGGCCCTCTACGAGCCTCTCGGGATCACCAAAGACAAGGACATCGTCGTCTACTGC CGCATCGCCGAGCGGTCCAGCCACTCCTGGTTCGTCCTCAAGTACCTCCTGGGCTACCCC CACGTGAAGAACTACGACGGCTCCTGGACCGAGTGGGGCAACCTGGTGGGGGTGCCCATC GCCAAAGGCGAGGAGTAG PF00581 Rhodanese function catalytic activity function transferase activity function transferase activity, transferring sulfur-containing groups function sulfurtransferase activity function thiosulfate sulfurtransferase activity process transport process ion transport process anion transport process inorganic anion transport process physiological process process sulfate transport process cellular physiological process BE0001760 Thiosulfate sulfurtransferase GlpE Shigella flexneri # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Thiosulfate sulfurtransferase GlpE Inorganic ion transport and metabolism Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide glpE Cytoplasm None 4.29 12083.0 Shigella flexneri GenBank Gene Database AE005674 GenBank Protein Database 24053900 UniProtKB P0A6V7 UniProt Accession GLPE_SHIFL EC 2.8.1.1 >Thiosulfate sulfurtransferase glpE MDQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRDNDFDTP VMVMCYHGNSSKGAAQYLLQQGYDVVYSIDGGFEAWQRQFPAEVAYGA >264 bp TTACGCGCCGTACGCCACCTCTGCGGGAAACTGTCGCTGCCAGGCTTCAAAGCCGCCGTC AATGCTATAGACCACATCGTAGCCCTGTTGCAGCAGATACTGCGCCGCCCCTTTGCTGCT ATTGCCGTGATAACACATCACCATCACCGGAGTGTCAAAGTCGTTATCACGCATAAACGC GCCCAGCGTGTCGTTGGTTAAATGGAAAGCCTGCACCGCATGCCCCATAGCGAAACTCTG TGGATCGCGAATATCGACCAGCAC PF00581 Rhodanese BE0001799 Hydroxylamine reductase Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Hydroxylamine reductase Energy production and conversion Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O hcp Cytoplasm None 6.45 58660.0 Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949) GenBank Gene Database Z11975 GenBank Protein Database 49286 UniProtKB Q01770 UniProt Accession HCP_DESDA EC 1.7.-.- HCP Hybrid-cluster protein Prismane protein >Hydroxylamine reductase MSNAMFCYQCQETVGNKGCTQVGVCGKKPETAALQDALIYVTKGLGQIATRLRAEGKAVD HRIDRLVTGNLFATITNANFDDDILAERVRMTCAAKKELAASLTDKSGLSDAALWEASEK SAMLAKAGTVGVMATTDDDVRSLRWLITFGLKGMAAYAKHADVLGKHENSLDAFMQEALA KTLDDSLSVADLVALTLETGKFGVSAMALLDAANTGTYGHPEITKVNIGVGSNPGILISG HDLRDLEMLLKQTEGTGVDVYTHSEMLPAHYYPAFKKYAHFKGNYGNAWWKQKEEFESFN GPVLLTTNCLVPPKDSYKDRVYTTGIVGFTGCKHIPGEIGEHKDFSAIIAHAKTCPAPTE IESGEIIGGFAHNQVLALADKVIDAVKSGAIKKFVVMAGCDGRAKSRSYYTDFAEGLPKD TVILTAGCAKYRYNKLNLGDIGGIPRVLDAGQCNDSYSLAVIALKLKEVFGLEDVNDLPI VYNIAWYEQKAVIVLLALLSLGVKNIHLGPTLPAFLSPNVAKVLVEQFNIGGITSPQDDL KAFFG >1638 bp ATGAGTAATGCCATGTTCTGCTACCAGTGCCAGGAAACCGTGGGTAACAAAGGCTGCACC CAGGTAGGCGTGTGCGGCAAAAAGCCTGAAACAGCCGCCCTTCAGGACGCGCTGATCTAT GTGACCAAGGGCCTCGGCCAGATCGCCACGCGCCTGCGCGCCGAAGGCAAGGCCGTTGAC CACAGGATAGACCGCCTGGTTACCGGCAACCTGTTTGCCACCATCACCAATGCCAACTTT GACGACGACATCCTTGCCGAGCGTGTGCGCATGACCTGTGCCGCCAAAAAGGAACTGGCC GCGTCCCTTACCGACAAGAGCGGCCTCAGCGATGCAGCCTTGTGGGAAGCATCCGAAAAG TCCGCCATGCTGGCCAAGGCCGGAACCGTAGGCGTTATGGCCACCACCGATGATGATGTG CGCTCCCTGCGCTGGCTCATCACCTTTGGGCTCAAGGGCATGGCGGCCTACGCCAAACAT GCGGATGTGCTTGGCAAGCATGAAAACAGCCTTGACGCCTTCATGCAGGAAGCCCTTGCC AAAACCCTGGATGACAGCCTGAGCGTGGCCGACCTTGTGGCCCTGACCCTTGAAACGGGC AAGTTCGGCGTATCGGCCATGGCCCTGCTGGATGCTGCCAATACCGGTACCTACGGCCAC CCAGAAATTACCAAGGTCAACATCGGCGTGGGCAGCAATCCCGGCATCCTCATTTCCGGG CATGACCTGCGCGACCTTGAAATGCTGCTCAAGCAGACCGAAGGCACAGGCGTTGACGTG TACACCCACTCTGAAATGCTGCCCGCCCATTACTACCCTGCCTTCAAGAAGTACGCGCAC TTCAAGGGCAACTACGGCAATGCATGGTGGAAACAGAAAGAAGAATTTGAAAGCTTTAAC GGCCCCGTGCTGCTGACCACCAACTGCCTTGTGCCGCCCAAGGACAGCTACAAGGACCGC GTGTACACCACCGGCATCGTGGGTTTTACGGGCTGCAAGCATATCCCCGGTGAAATCGGC GAACACAAGGACTTCAGCGCCATCATCGCCCATGCCAAGACCTGTCCCGCGCCTACGGAA ATCGAATCCGGCGAAATCATCGGCGGCTTCGCGCACAATCAGGTACTGGCCCTGGCCGAC AAGGTGATTGACGCGGTCAAATCCGGCGCCATCAAAAAGTTCGTGGTCATGGCCGGCTGC GACGGCCGCGCCAAGTCCCGCAGCTACTACACCGACTTTGCCGAAGGCCTGCCCAAAGAC ACGGTCATCCTTACCGCCGGTTGCGCCAAATATCGCTACAACAAGCTCAACCTGGGTGAC ATCGGCGGCATCCCGCGCGTACTGGACGCCGGGCAGTGCAACGACTCCTACTCCCTGGCC GTCATCGCCCTCAAGCTCAAGGAAGTATTCGGCCTCGAGGACGTCAACGACCTGCCCATC GTCTACAATATCGCCTGGTACGAGCAGAAGGCCGTTATCGTGCTGCTGGCCCTGCTGAGC CTCGGCGTGAAGAATATCCACCTCGGACCGACGCTGCCCGCCTTCCTTTCGCCCAACGTG GCCAAGGTGCTGGTGGAACAGTTCAACATCGGCGGCATCACCAGTCCGCAGGACGACCTC AAGGCGTTCTTCGGCTAA PF03063 Prismane component intracellular component cytoplasm component cell function catalytic activity function oxidoreductase activity, acting on other nitrogenous compounds as donors function oxidoreductase activity function ion binding function cation binding function transition metal ion binding function iron ion binding function binding process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process BE0001511 Cysteine desulfurase Escherichia coli (strain K12) # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 # Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17016423 unknown Cysteine desulfurase Amino acid transport and metabolism Cysteine desulfurases mobilize the sulfur from L- cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo sufS Cytoplasm None 6.32 44434.0 Escherichia coli (strain K12) GenBank Gene Database AB055108 GenBank Protein Database 12619308 UniProtKB P77444 UniProt Accession SUFS_ECOLI EC 2.8.1.7 EC 4.4.1.16 SCL Selenocysteine beta-lyase Selenocysteine lyase Selenocysteine reductase >Cysteine desulfurase MIFSVDKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHT LSAQATEKMENVRKRASLFINARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQ MEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTE NPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE ALLQEMPPWEGGGSMIATVSLSEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLN NIAEYEQNLMHYALSQLESVPDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRT GHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRIHRLLG >1221 bp ATGATTTTTTCCGTCGACAAAGTGCGGGCCGACTTTCCGGTGCTTTCGCGTGAGGTAAAC GGTTTGCCGCTGGCTTATCTCGACAGCGCCGCCAGTGCGCAGAAACCGAGCCAGGTGATT GACGCCGAGGCCGAGTTTTATCGTCATGGCTACGCGGCGGTGCATCGTGGTATTCATACC TTAAGCGCCCAGGCGACCGAGAAAATGGAGAACGTGCGCAAGCGGGCATCGCTGTTTATT AATGCCCGTTCGGCGGAAGAGCTGGTGTTCGTCCGCGGCACGACGGAAGGGATCAATCTG GTCGCCAATAGCTGGGGCAACAGCAACGTGCGGGCGGGCGATAACATCATCATCAGTCAG ATGGAGCACCACGCTAACATTGTTCCCTGGCAGATGCTTTGCGCACGCGTTGGCGCAGAG CTGCGTGTGATCCCGCTCAATCCCGATGGTACGTTGCAACTGGAGACGCTGCCTACGCTG TTTGATGAGAAAACTCGCCTGCTGGCAATTACTCATGTCTCCAACGTGCTTGGCACAGAA AATCCACTGGCGGAAATGATCACGCTTGCGCACCAGCATGGCGCAAAAGTGCTGGTGGAT GGCGCTCAGGCGGTGATGCATCATCCGGTGGATGTTCAGGCGCTGGATTGCGACTTTTAC GTGTTCTCCGGGCATAAACTGTATGGCCCCACCGGAATTGGCATTCTTTATGTGAAAGAA GCCTTGTTGCAGGAGATGCCGCCGTGGGAAGGGGGCGGTTCTATGATCGCCACCGTCAGC CTGAGTGAAGGCACTACCTGGACCAAAGCACCATGGCGGTTTGAAGCCGGTACACCCAAT ACCGGGGGCATCATTGGTCTTGGCGCGGCGCTGGAGTATGTTTCGGCGCTGGGGCTTAAT AACATAGCCGAGTATGAACAGAATCTGATGCATTATGCGCTATCACAGCTGGAATCTGTA CCGGATCTCACTCTCTATGGCCCACAAAACAGGCTTGGCGTTATTGCTTTTAATCTCGGT AAACACCACGCCTATGATGTTGGCAGTTTTCTCGATAATTACGGCATTGCTGTGCGTACC GGACATCACTGCGCAATGCCATTGATGGCCTATTACAACGTCCCTGCGATGTGTCGGGCG TCGCTGGCCATGTATAACACCCATGAAGAAGTGGATCGTCTGGTGACCGGCCTGCAACGT ATTCACCGTTTGCTGGGATAA PF00266 Aminotran_5 function catalytic activity function transferase activity, transferring sulfur-containing groups function sulfurtransferase activity function cysteine desulfurase activity function vitamin binding function pyridoxal phosphate binding function transferase activity function transferase activity, transferring nitrogenous groups function binding function transaminase activity process sulfur amino acid metabolism process cysteine metabolism process metabolism process cellular metabolism process amino acid metabolism process amino acid and derivative metabolism process physiological process "
owl:sameAs	drug:EXPT01038

All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines3/drugbank_small.nt

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