Resource D-Dethiobiotin

Predicate	Value (sorted: default)
rdfs:label	"D-Dethiobiotin"
rdf:type	ns1:drugs
ns1:description	" experimental This compound belongs to the heterocyclic fatty acids. These are fatty acids containing an heterocyclic attached to the acyl chain. Heterocyclic Fatty Acids Organic Compounds Lipids Fatty Acids and Conjugates Heterocyclic Fatty Acids Amino Fatty Acids Imidazolidinones Enolates Carboxylic Acids Polyamines imidazolidinone imidazolidine carboxylic acid derivative polyamine enolate carboxylic acid organonitrogen compound Mitogens logP 0.72 ALOGPS logS -2.2 ALOGPS Water Solubility 1.27e+00 g/l ALOGPS logP 0.73 ChemAxon IUPAC Name 6-[(4R,5S)-5-methyl-2-oxoimidazolidin-4-yl]hexanoic acid ChemAxon Traditional IUPAC Name (4R,5S)-dethiobiotin ChemAxon Molecular Weight 214.2615 ChemAxon Monoisotopic Weight 214.131742452 ChemAxon SMILES [H][C@@]1(C)NC(=O)N[C@]1([H])CCCCCC(O)=O ChemAxon Molecular Formula C10H18N2O3 ChemAxon InChI InChI=1S/C10H18N2O3/c1-7-8(12-10(15)11-7)5-3-2-4-6-9(13)14/h7-8H,2-6H2,1H3,(H,13,14)(H2,11,12,15)/t7-,8+/m0/s1 ChemAxon InChIKey InChIKey=AUTOLBMXDDTRRT-JGVFFNPUSA-N ChemAxon Polar Surface Area (PSA) 78.43 ChemAxon Refractivity 54.4 ChemAxon Polarizability 23.15 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 4.63 ChemAxon pKa (strongest basic) -1.8 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 445027 PubChem Substance 46504720 ChemSpider 392787 PDB DTB BE0001731 Biotin synthase 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 # 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 Biotin synthase Coenzyme transport and metabolism Dethiobiotin + sulfur + 2 S-adenosyl-L- methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine bioB None 5.13 38649.0 Escherichia coli (strain K12) GenBank Gene Database J04423 GenBank Protein Database 145425 UniProtKB P12996 UniProt Accession BIOB_ECOLI Biotin synthetase EC 2.8.1.6 >Biotin synthase MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYC PQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGV KAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKV RDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDA FDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDK DLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL >1041 bp ATGGCTCACCGCCCACGCTGGACATTGTCGCAAGTCACAGAATTATTTGAAAAACCGTTG CTGGATCTGCTGTTTGAAGCGCAGCAGGTGCATCGCCAGCATTTCGATCCTCGTCAGGTG CAGGTCAGCACGTTGCTGTCGATTAAGACCGGAGCTTGTCCGGAAGATTGCAAATACTGC CCGCAAACGTCGCGCTACAAAACCGGGCTGGAAGCCGAGCGGTTGATGGAAGTTGAACAG GTGCTGGAGTCGGCGCGCAAAGCGAAAGCGGCAGGATCGACGCGCTTCTGTATGGGCGCG GCGTGGAAGAATCCCCACGAACGCGATATGCCGTACCTGGAACAAATGGTGCAGGGGGTA AAAGCGATGGGGCTGGAGGCGTGTATGACGCTGGGCACGTTGAGTGAATCTCAGGCGCAG CGCCTCGCGAACGCCGGGCTGGATTACTACAACCACAACCTGGACACCTCGCCGGAGTTT TACGGCAATATCATCACCACACGCACTTATCAGGAACGCCTCGATACGCTGGAAAAAGTG CGCGATGCCGGGATCAAAGTCTGTTCTGGCGGCATTGTGGGCTTAGGCGAAACGGTAAAA GATCGCGCCGGATTATTGCTGCAACTGGCAAACCTGCCGACGCCGCCGGAAAGCGTGCCA ATCAACATGCTGGTGAAGGTGAAAGGCACGCCGCTTGCCGATAACGATGATGTCGATGCC TTTGATTTTATTCGCACCATTGCGGTCGCGCGGATCATGATGCCAACCTCTTACGTGCGC CTTTCTGCCGGACGCGAGCAGATGAACGAACAGACTCAGGCGATGTGCTTTATGGCAGGC GCAAACTCGATTTTCTACGGTTGCAAACTGCTGACCACGCCGAATCCGGAAGAAGATAAA GACCTGCAACTGTTCCGCAAACTGGGGCTAAATCCGCAGCAAACTGCCGTGCTGGCAGGG GATAACGAACAACAGCAACGTCTTGAACAGGCGCTGATGACCCCGGACACCGACGAATAT TACAACGCGGCAGCATTATGA PF06968 BATS PF04055 Radical_SAM function cation binding function transition metal ion binding function iron ion binding function transferase activity function binding function transferase activity, transferring sulfur-containing groups function catalytic activity function sulfurtransferase activity function ion binding function biotin synthase activity process vitamin metabolism process water-soluble vitamin metabolism process physiological process process biotin metabolism process metabolism process biotin biosynthesis process cellular metabolism BE0001271 ATP-dependent dethiobiotin synthetase BioD 1 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 # 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 ATP-dependent dethiobiotin synthetase BioD 1 Coenzyme transport and metabolism ATP + 7,8-diaminononanoate + CO(2) = ADP + phosphate + dethiobiotin bioD Cytoplasm None 5.64 24140.0 Escherichia coli (strain K12) GenBank Gene Database J04423 GenBank Protein Database 145427 UniProtKB P13000 UniProt Accession BIOD1_ECOLI Dethiobiotin synthase DTB synthetase DTBS EC 6.3.3.3 >Dethiobiotin synthetase MSKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGLRNSDALALQ RNSSLQLDYATVNPYTFAEPTSPHIISAQEGRPIESLVMSAGLRALEQQADWVLVEGAGG WFTPLSDTFTFADWVTQEQLPVILVVGVKLGCINHAMLTAQVIQHAGLTLAGWVANDVTP PGKRHAEYMTTLTRMIPAPLLGEIPWLAENPENAATGKYINLALL >660 bp GTGAGTAAACGTTATTTTGTCACCGGAACGGATACCGAAGTGGGGAAAACTGTCGCCAGT TGTGCACTTTTACAAGCCGCAAAGCGAGCAGGCTACCGGACGGCAGGTTATAAACCGGTC GCCTCTGGCAGCGAAAAGACCCCGGAAGGTTTACGCAATAGCGACGCGCTGGCGTTACAG CGCAACAGCAGCCTGCAGCTGGATTACGCAACAGTAAATCCTTACACCTTCGCAGAACCC ACTTCGCCGCACATCATCAGCGCGCAAGAGGGCAGACCGATAGAATCATTGGTAATGAGC GCCGGATTACGCGCGCTTGAACAACAGGCTGACTGGGTGTTAGTGGAAGGTGCTGGCGGC TGGTTTACGCCGCTTTCTGACACTTTCACTTTTGCAGATTGGGTAACACAGGAACAACTG CCGGTGATACTGGTAGTTGGTGTGAAACTCGGCTGTATTAATCACGCGATGTTGACTGCA CAGGTAATACAACACGCCGGACTGACTCTGGCGGGTTGGGTGGCGAACGATGTTACGCCT CCGGGAAAACGTCACGCTGAATATATGACCACGCTCACCCGCATGATTCCGCGCCGCTGC TGGGAGAGATCCCCTGGCTTGCAGAAAATCCAGAAAATGCGGCAACCGGAAAGTACATAA PF01656 CbiA function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function ligase activity, forming carbon-nitrogen bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function glutaminase activity function nucleotide binding function cyclo-ligase activity function purine nucleotide binding function binding function adenyl nucleotide binding function cobyrinic acid a,c-diamide synthase activity function ATP binding function dethiobiotin synthase activity function catalytic activity function ligase activity process porphyrin biosynthesis process vitamin metabolism process water-soluble vitamin metabolism process cobalamin biosynthesis process physiological process process biotin metabolism process metabolism process heterocycle metabolism process biotin biosynthesis process cellular metabolism process porphyrin metabolism BE0004052 ATP-dependent dethiobiotin synthetase BioD Mycobacterium tuberculosis # 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 ATP-dependent dethiobiotin synthetase BioD Coenzyme transport and metabolism ATP + 7,8-diaminononanoate + CO(2) = ADP + phosphate + dethiobiotin bioD None 4.92 22455.7 Mycobacterium tuberculosis GeneCards bioD GenBank Gene Database BX842577 GenBank Protein Database 2916953 UniProtKB O06620 UniProt Accession BIOD_MYCTU Dethiobiotin synthase DTB synthetase DTBS >Dethiobiotin synthetase MTILVVTGTGTGVGKTVVCAALASAARQAGIDVAVCKPVQTGTARGDDDLAEVGRLAGVT QLAGLARYPQPMAPAAAAEHAGMALPARDQIVRLIADLDRPGRLTLVEGAGGLLVELAEP GVTLRDVAVDVAAAALVVVTADLGTLNHTKLTLEALAAQQVSCAGLVIGSWPDPPGLVAA SNRSALARIAMVRAALPAGAASLDAGDFAAMSAAAFDRNWVAGLVG >1104 bp ATGTCGGACGGCGCGGTGGTACGGGCATTGGTATTGGAGGCGCCGCGCAGGCTGGTCGTG CGCCAGTACCGGCTGCCGCGCATCGGCGATGATGACGCACTAGTGCGAGTAGAGGCCTGC GGGCTGTGCGGCACCGATCACGAGCAATACACGGGCGAGCTGGCCGGTGGGTTTGCCTTC GTACCTGGCCACGAGACGGTCGGGACGATTGCGGCCATCGGTCCGCGGGCGGAGCAGCGG TGGGGCGTGTCGGCCGGCGACCGAGTAGCCGTCGAGGTATTCCAGTCGTGTCGGCAGTGC GCTAACTGTCGTGGCGGCGAGTACCGGCGTTGTGTACGGCATGGCCTCGCTGACATGTAC GGGTTCATCCCGGTTGACCGAGAGCCTGGCCTGTGGGGCGGTTACGCCGAATATCAGTAC CTGGCGCCGGATTCGATGGTGTTGCGGGTGGCCGGTGACCTCAGCCCGGAAGTGGCCACC TTGTTCAACCCGCTGGGGGCGGGAATACGTTGGGGAGTAACGATTCCCGAAACCAAACCG GGCGACGTCGTGGCGGTGCTGGGTCCAGGAATCCGGGGGCTGTGCGCCGCCGCGGCGGCA AAAGGGGCCGGTGCCGGGTTCGTGATGGTGACCGGGTTGGGACCCCGTGACGCCGACCGG TTGGCGCTGGCGGCACAGTTCGGAGCCGACCTCGCCGTCGATGTTGCGATCGATGACCCG GTCGCCGCCCTGACCGAACAGACCGGTGGGCTGGCAGACGTCGTTGTCGACGTGACCGCC AAGGCGCCAGCGGCATTCGCACAGGCGATAGCGCTAGCCCGGCCCGCCGGGACCGTTGTT GTCGCCGGCACCCGGGGCGTGGGCAGCGGGGCACCGGGATTTTCGCCCGACGTCGTTGTG TTCAAGGAGCTGCGTGTGCTTGGCGCCCTCGGCGTAGACGCCACCGCCTACCGGGCCGCG CTTGATCTGTTGGTGTCCGGTCGATACCCCTTCGCAAGCCTGCCTCGCCGCTGCGTGCGG CTCGAAGGCGCCGAGGATCTGCTGGCTACCATGGCCGGTGAACGCGACGGTGTCCCGCCT ATCCACGGAGTGCTCACACCATGA function purine nucleotide binding function adenyl nucleotide binding function ATP binding function ligase activity function ligase activity, forming carbon-nitrogen bonds function binding function catalytic activity function cyclo-ligase activity function dethiobiotin synthase activity function nucleotide binding process vitamin metabolism process physiological process process water-soluble vitamin metabolism process metabolism process cellular metabolism process biotin metabolism process biotin biosynthesis "
ns1:drugCategory	?:Mitogens
owl:sameAs	?:EXPT01280

"D-Dethiobiotin"

" experimental This compound belongs to the heterocyclic fatty acids. These are fatty acids containing an heterocyclic attached to the acyl chain. Heterocyclic Fatty Acids Organic Compounds Lipids Fatty Acids and Conjugates Heterocyclic Fatty Acids Amino Fatty Acids Imidazolidinones Enolates Carboxylic Acids Polyamines imidazolidinone imidazolidine carboxylic acid derivative polyamine enolate carboxylic acid organonitrogen compound Mitogens logP 0.72 ALOGPS logS -2.2 ALOGPS Water Solubility 1.27e+00 g/l ALOGPS logP 0.73 ChemAxon IUPAC Name 6-[(4R,5S)-5-methyl-2-oxoimidazolidin-4-yl]hexanoic acid ChemAxon Traditional IUPAC Name (4R,5S)-dethiobiotin ChemAxon Molecular Weight 214.2615 ChemAxon Monoisotopic Weight 214.131742452 ChemAxon SMILES [H][C@@]1(C)NC(=O)N[C@]1([H])CCCCCC(O)=O ChemAxon Molecular Formula C10H18N2O3 ChemAxon InChI InChI=1S/C10H18N2O3/c1-7-8(12-10(15)11-7)5-3-2-4-6-9(13)14/h7-8H,2-6H2,1H3,(H,13,14)(H2,11,12,15)/t7-,8+/m0/s1 ChemAxon InChIKey InChIKey=AUTOLBMXDDTRRT-JGVFFNPUSA-N ChemAxon Polar Surface Area (PSA) 78.43 ChemAxon Refractivity 54.4 ChemAxon Polarizability 23.15 ChemAxon Rotatable Bond Count 6 ChemAxon H Bond Acceptor Count 3 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 4.63 ChemAxon pKa (strongest basic) -1.8 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 1 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 445027 PubChem Substance 46504720 ChemSpider 392787 PDB DTB BE0001731 Biotin synthase 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 # 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 Biotin synthase Coenzyme transport and metabolism Dethiobiotin + sulfur + 2 S-adenosyl-L- methionine = biotin + 2 L-methionine + 2 5'-deoxyadenosine bioB None 5.13 38649.0 Escherichia coli (strain K12) GenBank Gene Database J04423 GenBank Protein Database 145425 UniProtKB P12996 UniProt Accession BIOB_ECOLI Biotin synthetase EC 2.8.1.6 >Biotin synthase MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYC PQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGV KAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKV RDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDA FDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDK DLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL >1041 bp ATGGCTCACCGCCCACGCTGGACATTGTCGCAAGTCACAGAATTATTTGAAAAACCGTTG CTGGATCTGCTGTTTGAAGCGCAGCAGGTGCATCGCCAGCATTTCGATCCTCGTCAGGTG CAGGTCAGCACGTTGCTGTCGATTAAGACCGGAGCTTGTCCGGAAGATTGCAAATACTGC CCGCAAACGTCGCGCTACAAAACCGGGCTGGAAGCCGAGCGGTTGATGGAAGTTGAACAG GTGCTGGAGTCGGCGCGCAAAGCGAAAGCGGCAGGATCGACGCGCTTCTGTATGGGCGCG GCGTGGAAGAATCCCCACGAACGCGATATGCCGTACCTGGAACAAATGGTGCAGGGGGTA AAAGCGATGGGGCTGGAGGCGTGTATGACGCTGGGCACGTTGAGTGAATCTCAGGCGCAG CGCCTCGCGAACGCCGGGCTGGATTACTACAACCACAACCTGGACACCTCGCCGGAGTTT TACGGCAATATCATCACCACACGCACTTATCAGGAACGCCTCGATACGCTGGAAAAAGTG CGCGATGCCGGGATCAAAGTCTGTTCTGGCGGCATTGTGGGCTTAGGCGAAACGGTAAAA GATCGCGCCGGATTATTGCTGCAACTGGCAAACCTGCCGACGCCGCCGGAAAGCGTGCCA ATCAACATGCTGGTGAAGGTGAAAGGCACGCCGCTTGCCGATAACGATGATGTCGATGCC TTTGATTTTATTCGCACCATTGCGGTCGCGCGGATCATGATGCCAACCTCTTACGTGCGC CTTTCTGCCGGACGCGAGCAGATGAACGAACAGACTCAGGCGATGTGCTTTATGGCAGGC GCAAACTCGATTTTCTACGGTTGCAAACTGCTGACCACGCCGAATCCGGAAGAAGATAAA GACCTGCAACTGTTCCGCAAACTGGGGCTAAATCCGCAGCAAACTGCCGTGCTGGCAGGG GATAACGAACAACAGCAACGTCTTGAACAGGCGCTGATGACCCCGGACACCGACGAATAT TACAACGCGGCAGCATTATGA PF06968 BATS PF04055 Radical_SAM function cation binding function transition metal ion binding function iron ion binding function transferase activity function binding function transferase activity, transferring sulfur-containing groups function catalytic activity function sulfurtransferase activity function ion binding function biotin synthase activity process vitamin metabolism process water-soluble vitamin metabolism process physiological process process biotin metabolism process metabolism process biotin biosynthesis process cellular metabolism BE0001271 ATP-dependent dethiobiotin synthetase BioD 1 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 # 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 ATP-dependent dethiobiotin synthetase BioD 1 Coenzyme transport and metabolism ATP + 7,8-diaminononanoate + CO(2) = ADP + phosphate + dethiobiotin bioD Cytoplasm None 5.64 24140.0 Escherichia coli (strain K12) GenBank Gene Database J04423 GenBank Protein Database 145427 UniProtKB P13000 UniProt Accession BIOD1_ECOLI Dethiobiotin synthase DTB synthetase DTBS EC 6.3.3.3 >Dethiobiotin synthetase MSKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGLRNSDALALQ RNSSLQLDYATVNPYTFAEPTSPHIISAQEGRPIESLVMSAGLRALEQQADWVLVEGAGG WFTPLSDTFTFADWVTQEQLPVILVVGVKLGCINHAMLTAQVIQHAGLTLAGWVANDVTP PGKRHAEYMTTLTRMIPAPLLGEIPWLAENPENAATGKYINLALL >660 bp GTGAGTAAACGTTATTTTGTCACCGGAACGGATACCGAAGTGGGGAAAACTGTCGCCAGT TGTGCACTTTTACAAGCCGCAAAGCGAGCAGGCTACCGGACGGCAGGTTATAAACCGGTC GCCTCTGGCAGCGAAAAGACCCCGGAAGGTTTACGCAATAGCGACGCGCTGGCGTTACAG CGCAACAGCAGCCTGCAGCTGGATTACGCAACAGTAAATCCTTACACCTTCGCAGAACCC ACTTCGCCGCACATCATCAGCGCGCAAGAGGGCAGACCGATAGAATCATTGGTAATGAGC GCCGGATTACGCGCGCTTGAACAACAGGCTGACTGGGTGTTAGTGGAAGGTGCTGGCGGC TGGTTTACGCCGCTTTCTGACACTTTCACTTTTGCAGATTGGGTAACACAGGAACAACTG CCGGTGATACTGGTAGTTGGTGTGAAACTCGGCTGTATTAATCACGCGATGTTGACTGCA CAGGTAATACAACACGCCGGACTGACTCTGGCGGGTTGGGTGGCGAACGATGTTACGCCT CCGGGAAAACGTCACGCTGAATATATGACCACGCTCACCCGCATGATTCCGCGCCGCTGC TGGGAGAGATCCCCTGGCTTGCAGAAAATCCAGAAAATGCGGCAACCGGAAAGTACATAA PF01656 CbiA function hydrolase activity function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds function ligase activity, forming carbon-nitrogen bonds function hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides function glutaminase activity function nucleotide binding function cyclo-ligase activity function purine nucleotide binding function binding function adenyl nucleotide binding function cobyrinic acid a,c-diamide synthase activity function ATP binding function dethiobiotin synthase activity function catalytic activity function ligase activity process porphyrin biosynthesis process vitamin metabolism process water-soluble vitamin metabolism process cobalamin biosynthesis process physiological process process biotin metabolism process metabolism process heterocycle metabolism process biotin biosynthesis process cellular metabolism process porphyrin metabolism BE0004052 ATP-dependent dethiobiotin synthetase BioD Mycobacterium tuberculosis # 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 ATP-dependent dethiobiotin synthetase BioD Coenzyme transport and metabolism ATP + 7,8-diaminononanoate + CO(2) = ADP + phosphate + dethiobiotin bioD None 4.92 22455.7 Mycobacterium tuberculosis GeneCards bioD GenBank Gene Database BX842577 GenBank Protein Database 2916953 UniProtKB O06620 UniProt Accession BIOD_MYCTU Dethiobiotin synthase DTB synthetase DTBS >Dethiobiotin synthetase MTILVVTGTGTGVGKTVVCAALASAARQAGIDVAVCKPVQTGTARGDDDLAEVGRLAGVT QLAGLARYPQPMAPAAAAEHAGMALPARDQIVRLIADLDRPGRLTLVEGAGGLLVELAEP GVTLRDVAVDVAAAALVVVTADLGTLNHTKLTLEALAAQQVSCAGLVIGSWPDPPGLVAA SNRSALARIAMVRAALPAGAASLDAGDFAAMSAAAFDRNWVAGLVG >1104 bp ATGTCGGACGGCGCGGTGGTACGGGCATTGGTATTGGAGGCGCCGCGCAGGCTGGTCGTG CGCCAGTACCGGCTGCCGCGCATCGGCGATGATGACGCACTAGTGCGAGTAGAGGCCTGC GGGCTGTGCGGCACCGATCACGAGCAATACACGGGCGAGCTGGCCGGTGGGTTTGCCTTC GTACCTGGCCACGAGACGGTCGGGACGATTGCGGCCATCGGTCCGCGGGCGGAGCAGCGG TGGGGCGTGTCGGCCGGCGACCGAGTAGCCGTCGAGGTATTCCAGTCGTGTCGGCAGTGC GCTAACTGTCGTGGCGGCGAGTACCGGCGTTGTGTACGGCATGGCCTCGCTGACATGTAC GGGTTCATCCCGGTTGACCGAGAGCCTGGCCTGTGGGGCGGTTACGCCGAATATCAGTAC CTGGCGCCGGATTCGATGGTGTTGCGGGTGGCCGGTGACCTCAGCCCGGAAGTGGCCACC TTGTTCAACCCGCTGGGGGCGGGAATACGTTGGGGAGTAACGATTCCCGAAACCAAACCG GGCGACGTCGTGGCGGTGCTGGGTCCAGGAATCCGGGGGCTGTGCGCCGCCGCGGCGGCA AAAGGGGCCGGTGCCGGGTTCGTGATGGTGACCGGGTTGGGACCCCGTGACGCCGACCGG TTGGCGCTGGCGGCACAGTTCGGAGCCGACCTCGCCGTCGATGTTGCGATCGATGACCCG GTCGCCGCCCTGACCGAACAGACCGGTGGGCTGGCAGACGTCGTTGTCGACGTGACCGCC AAGGCGCCAGCGGCATTCGCACAGGCGATAGCGCTAGCCCGGCCCGCCGGGACCGTTGTT GTCGCCGGCACCCGGGGCGTGGGCAGCGGGGCACCGGGATTTTCGCCCGACGTCGTTGTG TTCAAGGAGCTGCGTGTGCTTGGCGCCCTCGGCGTAGACGCCACCGCCTACCGGGCCGCG CTTGATCTGTTGGTGTCCGGTCGATACCCCTTCGCAAGCCTGCCTCGCCGCTGCGTGCGG CTCGAAGGCGCCGAGGATCTGCTGGCTACCATGGCCGGTGAACGCGACGGTGTCCCGCCT ATCCACGGAGTGCTCACACCATGA function purine nucleotide binding function adenyl nucleotide binding function ATP binding function ligase activity function ligase activity, forming carbon-nitrogen bonds function binding function catalytic activity function cyclo-ligase activity function dethiobiotin synthase activity function nucleotide binding process vitamin metabolism process physiological process process water-soluble vitamin metabolism process metabolism process cellular metabolism process biotin metabolism process biotin biosynthesis "

owl:sameAs

?:EXPT01280

Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB03775"

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