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PredicateValue (sorted: default)
rdfs:label
"(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID"
rdf:type
ns1:drugs
ns1:description
" experimental This compound belongs to the dihydroxy bile acids, alcohols and derivatives. These are compounds containing or derived from a bile acid or alcohol, and which bears exactly two carboxylic acid groups. Dihydroxy Bile Acids, Alcohols and Derivatives Organic Compounds Lipids Steroids and Steroid Derivatives Bile Acids, Alcohols and Derivatives Hydroxysteroids Cyclohexanols Cyclic Alcohols and Derivatives Enolates Polyamines Carboxylic Acids 3-hydroxy-steroid 12-hydroxy-steroid cyclohexanol cyclic alcohol secondary alcohol polyamine enolate carboxylic acid carboxylic acid derivative alcohol logP 3.3 ALOGPS logS -4.3 ALOGPS Water Solubility 1.73e-02 g/l ALOGPS logP 3.79 ChemAxon IUPAC Name (4R)-4-[(1S,2S,5R,7R,10R,11S,14R,15R,16S)-5,16-dihydroxy-2,15-dimethyltetracyclo[8.7.0.0^{2,7}.0^{11,15}]heptadecan-14-yl]pentanoic acid ChemAxon Traditional IUPAC Name deoxycholic acid ChemAxon Molecular Weight 392.572 ChemAxon Monoisotopic Weight 392.292659768 ChemAxon SMILES [H][C@@](C)(CCC(O)=O)[C@@]1([H])CC[C@@]2([H])[C@]3([H])CC[C@]4([H])C[C@]([H])(O)CC[C@]4(C)[C@@]3([H])C[C@]([H])(O)[C@]12C ChemAxon Molecular Formula C24H40O4 ChemAxon InChI InChI=1S/C24H40O4/c1-14(4-9-22(27)28)18-7-8-19-17-6-5-15-12-16(25)10-11-23(15,2)20(17)13-21(26)24(18,19)3/h14-21,25-26H,4-13H2,1-3H3,(H,27,28)/t14-,15-,16-,17+,18-,19+,20+,21+,23+,24-/m1/s1 ChemAxon InChIKey InChIKey=KXGVEGMKQFWNSR-LLQZFEROSA-N ChemAxon Polar Surface Area (PSA) 77.76 ChemAxon Refractivity 109.2 ChemAxon Polarizability 46.28 ChemAxon Rotatable Bond Count 4 ChemAxon H Bond Acceptor Count 4 ChemAxon H Bond Donor Count 3 ChemAxon pKa (strongest acidic) 4.65 ChemAxon pKa (strongest basic) -0.35 ChemAxon Physiological Charge -1 ChemAxon Number of Rings 4 ChemAxon Bioavailability 1 ChemAxon Rule of Five true ChemAxon Ghose Filter true ChemAxon PubChem Compound 222528 PubChem Substance 99444161 ChemSpider 193196 PDB DXC BE0001236 Steroid Delta-isomerase Pseudomonas putida # 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 Steroid Delta-isomerase Involved in steroid delta-isomerase activity A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- steroid ksi None 4.53 14536.0 Pseudomonas putida GenBank Gene Database L13127 GenBank Protein Database 309871 UniProtKB P07445 UniProt Accession SDIS_PSEPU Delta(5)-3-ketosteroid isomerase EC 5.3.3.1 >Steroid Delta-isomerase MNLPTAQEVQGLMARYIELVDVGDIEAIVQMYADDATVEDPFGQPPIHGREQIAAFYRQG LGGGKVRACLTGPVRASHNGCGAMPFRVEMVWNGQPCALDVIDVMRFDEHGRIQTMQAYW SEVNLSVREPQ >396 bp ATGAACCTACCGACTGCGCAGGAAGTCCAGGGCCTGATGGCCCGTTACATCGAGCTGGTC GATGTCGGGGATATCGAGGCGATCGTGCAGATGTACGCCGATGACGCCACGGTCGAAGAC CCGTTTGGCCAGCCGCCGATCCACGGCCGCGAGCAGATTGCCGCGTTCTATCGCCAGGGT TTGGGCGGGGGCAAGGTCCGCGCCTGCCTGACCGGGCCGGTACGGGCCAGCCATAACGGC TGCGGGGCGATGCCGTTTCGCGTCGAGATGGTCTGGAACGGCCAGCCCTGTGCACTGGAT GTCATCGATGTGATGCGCTTTGATGAGCACGGCCGGATCCAGACGATGCAAGCCTACTGG AGCGAGGTCAACCTCAGCGTGCGCGAGCCGCAGTAG PF02136 NTF2 component cell component intracellular function isomerase activity function intramolecular oxidoreductase activity function intramolecular oxidoreductase activity, transposing C=C bonds function steroid delta-isomerase activity function catalytic activity function transporter activity process physiological process process cellular physiological process process transport BE0002929 PpcA Geobacter sulfurreducens # 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 PpcA Involved in iron ion binding ppcA None 9.72 9748.0 Geobacter sulfurreducens GenBank Gene Database AF505790 UniProtKB Q8GGK7 UniProt Accession Q8GGK7_GEOSN Cytochrome c3 >PpcA MKKVIASLALSVFCAGLAFAADDIVLKAKNGDVKFPHKAHQKAVPDCKKCHEKGPGKIEG FGKEMAHGKGCKGCHEEMKKGPTKCGECHKK >273 bp ATGAAAAAGGTTATTGCTTCTCTCGCGCTGTCCGTATTCTGCGCCGGCCTCGCCTTTGCC GCCGACGACATCGTCCTCAAGGCCAAGAACGGTGATGTGAAGTTCCCGCACAAGGCCCAC CAGAAGGCTGTTCCCGACTGTAAGAAGTGCCACGAGAAAGGCCCGGGCAAGATCGAGGGC TTCGGCAAAGAGATGGCTCATGGCAAGGGCTGCAAGGGGTGCCACGAAGAAATGAAGAAG GGGCCGACGAAGTGCGGCGAGTGCCACAAGAAG function tetrapyrrole binding function heme binding function ion binding function cation binding function transition metal ion binding function iron ion binding function transporter activity function electron transporter activity function binding process physiological process process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport BE0004053 Elongation factor Tu GTP-binding domain-containing protein 1 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 Elongation factor Tu GTP-binding domain-containing protein 1 Translation, ribosomal structure and biogenesis EFTUD1 15q25.2 None 5.72 125428.7 Human HUGO Gene Nomenclature Committee (HGNC) GNC:25789 GeneCards EFTUD1 GenBank Gene Database AK023181 GenBank Protein Database 10434992 UniProtKB Q7Z2Z2 UniProt Accession ETUD1_HUMAN >Elongation factor Tu GTP-binding domain-containing protein 1 MVLNSLDKMIQLQKNTANIRNICVLAHVDHGKTTLADCLISSNGIISSRLAGKLRYMDSR EDEQIRGITMKSSAISLHYATGNEEYLINLIDSPGHVDFSSEVSTAVRICDGCIIVVDAV EGVCPQTQAVLRQAWLENIRPVLVINKIDRLIVELKFTPQEAYSHLKNILEQINALTGTL FTSKVLEERAERETESQVNPNSEQGEQVYDWSTGLEDTDDSHLYFSPEQGNVVFTSAIDG WGFGIEHFARIYSQKIGIKKEVLMKTLWGDYYINMKAKKIMKGDQAKGKKPLFVQLILEN IWSLYDAVLKKDKDKIDKIVTSLGLKIGAREARHSDPKVQINAICSQWLPISHAVLAMVC QKLPSPLDITAERVERLMCTGSQTFDSFPPETQALKAAFMKCGSEDTAPVIIFVSKMFAV DAKALPQNKPRPLTQEEIAQRRERARQRHAEKLAAAQGQAPLEPTQDGSAIETCPKGEEP RGDEQQVESMTPKPVLQEENNQESFIAFARVFSGVARRGKKIFVLGPKYSPLEFLRRVPL GFSAPPDGLPQVPHMAYCALENLYLLMGRELEYLEEVPPGNVLGIGGLQDFVLKSATLCS LPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGEHVLV TAGEVHLQRCLDDLKERFAKIHISVSEPIIPFRETITKPPKVDMVNEEIGKQQKVAVIHQ MKEDQSKIPEGIQVDSDGLITITTPNKLATLSVRAMPLPEEVTQILEENSDLIRSMEQLT SSLNEGENTHMIHQKTQEKIWEFKGKLEQHLTGRRWRNIVDQIWSFGPRKCGPNILVNKS EDFQNSVWTGPADKASKEASRYRDLGNSIVSGFQLATLSGPMCEEPLMGVCFVLEKWDLS KFEEQGASDLAKEGQEENETCSGGNENQELQDGCSEAFEKRTSQKGESPLTDCYGPFSGQ LIATMKEACRYALQVKPQRLMAAMYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTD MFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEIIPSDPFWVPTTEEEYLHFGEK ADSENQARKYMNAVRKRKGLYVEEKIVEHAEKQRTLSKNK >2574 bp ATGAAAACCTTGTGGGGAGATTACTATATAAATATGAAGGCTAAAAAGATCATGAAGGGT GATCAGGCCAAAGGAAAGAAACCTTTATTTGTACAGTTGATCCTGGAAAATATATGGAGT TTGTATGATGCTGTTTTGAAAAAGGACAAAGACAAAATTGATAAAATAGTGACTTCTTTA GGATTAAAAATTGGAGCCCGGGAGGCACGACATTCAGACCCTAAAGTTCAGATCAACGCC ATTTGCAGTCAGTGGCTACCCATATCCCATGCTGTTCTTGCTATGGTGTGTCAGAAACTT CCTAGTCCCCTTGATATTACAGCTGAGAGAGTGGAGAGACTGATGTGCACAGGATCACAA ACTTTTGACTCTTTTCCACCAGAAACTCAAGCACTGAAAGCAGCTTTTATGAAATGTGGA AGTGAGGACACTGCTCCAGTTATTATATTTGTTTCCAAAATGTTTGCAGTTGATGCTAAG GCCTTGCCTCAGAATAAGCCAAGGCCTCTCACTCAAGAAGAAATTGCTCAGAGACGTGAG CGTGCAAGACAAAGGCATGCAGAGAAGCTTGCAGCAGCACAGGGACAGGCACCCTTGGAG CCCACCCAAGATGGGAGTGCCATTGAAACATGTCCAAAAGGAGACGAGCCAAGAGGTGAC GAGCAACAGGTGGAAAGTATGACCCCTAAACCTGTGCTCCAGGAAGAAAACAACCAAGAG TCTTTTATTGCATTTGCTCGGGTGTTCAGTGGTGTGGCTCGAAGAGGAAAGAAAATTTTT GTCTTGGGGCCCAAATACAGTCCTCTTGAGTTTTTACGAAGGGTACCATTAGGCTTCTCA GCTCCACCAGATGGCCTCCCCCAAGTCCCCCACATGGCATACTGTGCTCTGGAAAACCTG TATCTTCTGATGGGAAGGGAACTGGAATATCTAGAGGAGGTACCTCCAGGAAATGTGCTA GGAATAGGAGGCCTTCAAGATTTTGTGCTGAAATCTGCAACACTGTGTAGCCTGCCATCC TGCCCACCATTTATACCACTCAACTTCGAAGCCACTCCTATTGTGAGAGTTGCTGTTGAA CCAAAACATCCAAGTGAAATGCCTCGGCTCGTAAAAGGAATGAAACTGTTAAACCAGGCT GATCCCTGTGTCCAGATTTTAATTCAGGAAACGGGAGAGCACGTTTTAGTCACAGCAGGA GAAGTCCACCTTCAGCGATGCCTGGATGACTTAAAAGAAAGGTTTGCAAAGATTCATATC AGTGTATCTGAACCTATTATTCCATTCAGAGAAACAATCACAAAACCCCCAAAAGTTGAC ATGGTCAATGAAGAAATAGGCAAACAGCAAAAAGTTGCAGTCATACACCAAATGAAAGAA GATCAAAGCAAAATCCCTGAAGGAATCCAAGTTGACTCTGACGGGCTAATCACCATAACA ACTCCCAATAAACTTGCCACGCTCAGTGTTCGAGCCATGCCCCTTCCAGAAGAAGTCACC CAGATTCTGGAAGAAAATAGTGATTTGATTCGTTCTATGGAGCAGTTGACATCCTCTTTG AATGAGGGCGAAAATACTCACATGATTCATCAGAAGACCCAAGAGAAAATTTGGGAATTC AAAGGAAAACTGGAGCAACACCTAACAGGGAGAAGATGGAGGAACATTGTTGACCAAATC TGGTCATTTGGCCCAAGAAAATGTGGGCCCAACATACTAGTCAATAAAAGTGAAGATTTT CAGAACTCAGTATGGACAGGTCCAGCTGACAAAGCTTCAAAAGAAGCCAGTAGATACCGA GATTTGGGCAATAGCATTGTGAGTGGCTTCCAACTAGCAACCCTCTCTGGCCCCATGTGT GAGGAGCCTCTCATGGGTGTCTGTTTTGTTCTGGAAAAATGGGACCTAAGTAAATTTGAG GAACAAGGAGCAAGTGATCTGGCAAAAGAGGGACAGGAGGAAAATGAAACCTGTTCTGGT GGAAATGAAAACCAAGAGCTACAAGATGGCTGCTCTGAGGCCTTTGAGAAGAGGACATCA CAGAAAGGAGAATCTCCACTCACTGACTGCTATGGACCTTTCTCAGGACAGCTAATTGCC ACCATGAAAGAAGCATGTCGCTATGCACTGCAAGTGAAACCTCAGCGCCTGATGGCAGCT ATGTACACATGTGACATCATGGCCACTGGTGATGTTCTCGGTCGAGTCTATGCTGTCTTG TCAAAGAGAGAAGGTCGGGTACTTCAAGAAGAAATGAAAGAAGGGACAGACATGTTCATC ATCAAGGCTGTGCTGCCTGTTGCTGAAAGCTTTGGTTTTGCTGATGAAATCAGGAAGAGG ACAAGTGGCCTGGCCAGCCCACAACTAGTATTCAGCCATTGGGAGATCATTCCCAGTGAC CCCTTCTGGGTGCCAACTACTGAGGAGGAATACTTGCACTTTGGGGAGAAGGCTGACTCT GAGAACCAAGCCCGGAAGTACATGAACGCAGTACGAAAGCGGAAGGGGCTTTATGTGGAA GAAAAGATTGTGGAGCATGCAGAAAAGCAGAGGACACTCAGCAAAAATAAGTAG PF00009 GTP_EFTU PF00679 EFG_C PF03764 EFG_IV function guanyl nucleotide binding function GTP binding function binding function nucleotide binding function purine nucleotide binding process physiological process process metabolism process macromolecule metabolism process macromolecule biosynthesis process protein biosynthesis BE0001392 Choloylglycine hydrolase Clostridium perfringens (strain 13 / Type A) # 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 Choloylglycine hydrolase Cell wall/membrane/envelope biogenesis The enzyme catalyzes the degradation of conjugated bile acids in the mammalian gut cbh None 5.07 37186.0 Clostridium perfringens (strain 13 / Type A) GenBank Gene Database U20191 GenBank Protein Database 882252 UniProtKB P54965 UniProt Accession CBH_CLOPE Bile salt hydrolase CBAH Conjugated bile acid hydrolase EC 3.5.1.24 >Choloylglycine hydrolase MCTGLALETKDGLHLFGRNMDIEYSFNQSIIFIPRNFKCVNKSNKKELTTKYAVLGMGTI FDDYPTFADGMNEKGLGCAGLNFPVYVSYSKEDIEGKTNIPVYNFLLWVLANFSSVEEVK EALKNANIVDIPISENIPNTTLHWMISDITGKSIVVEQTKEKLNVFDNNIGVLTNSPTFD WHVANLNQYVGLRYNQVPEFKLGDQSLTALGQGTGLVGLPGDFTPASRFIRVAFLRDAMI KNDKDSIDLIEFFHILNNVAMVRGSTRTVEEKSDLTQYTSCMCLEKGIYYYNTYENNQIN AIDMNKENLDGNEIKTYKYNKTLSINHVN >990 bp ATGTGTACAGGATTAGCCTTAGAAACAAAAGATGGATTACATTTGTTTGGAAGAAATATG GATATTGAATATTCATTTAATCAATCTATTATATTTATTCCTAGGAATTTTAAATGTGTA AACAAATCAAACAAAAAAGAATTAACAACAAAATATGCTGTTCTTGGAATGGGAACTATT TTTGATGATTATCCTACCTTTGCAGATGGTATGAATGAAAAGGGATTAGGGTGTGCTGGC TTAAATTTCCCTGTTTATGTTAGCTATTCTAAAGAAGATATAGAAGGTAAAACTAATATT CCAGTATATAATTTCTTATTATGGGTTTTAGCTAATTTTAGCTCAGTAGAAGAGGTAAAG GAAGCATTAAAAAATGCTAATATAGTGGATATACCTATTAGCGAAAATATTCCTAATACA ACTCTTCATTGGATGATAAGCGATATAACAGGAAAGTCTATTGTGGTTGAACAAACAAAG GAAAAATTAAATGTATTTGATAATAATATTGGAGTATTAACTAATTCACCTACTTTTGAT TGGCATGTAGCAAATTTAAATCAATATGTAGGTTTGAGATATAATCAAGTTCCAGAATTT AAGTTAGGAGATCAATCTTTAACTGCTTTAGGTCAAGGAACTGGTTTAGTAGGATTACCA GGGGACTTTACACCTGCATCTAGATTTATAAGAGTAGCATTTTTAAGAGATGCAATGATA AAAAATGATAAAGATTCAATAGACTTAATTGAATTTTTCCATATATTAAATAATGTTGCT ATGGTAAGAGGATCAACTAGAACTGTAGAAGAAAAAAGTGATCTTACTCAATATACAAGT TGCATGTGTTTAGAAAAAGGAATTTATTATTATAATACCTATGAAAATAATCAAATTAAT GCAATAGACATGAATAAAGAAAACTTAGATGGAAATGAAATTAAAACATATAAATACAAC AAAACTTTAAGTATTAATCATGTAAATTAG PF02275 CBAH BE0004054 Lactaldehyde dehydrogenase Escherichia coli (strain K12) # 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 Lactaldehyde dehydrogenase Energy production and conversion Acts on lactaldehyde as well as other aldehydes aldA None 4.79 52272.4 Escherichia coli (strain K12) GeneCards aldA GenBank Gene Database M64541 GenBank Protein Database 145222 UniProtKB P25553 UniProt Accession ALDA_ECOLI Aldehyde dehydrogenase A Glycolaldehyde dehydrogenase >Lactaldehyde dehydrogenase MSVPVQHPMYIDGQFVTWRGDAWIDVVNPATEAVISRIPDGQAEDARKAIDAAERAQPEW EALPAIERASWLRKISAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR RYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEF TPNNAIAFAKIVDEIGLPRGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAT AAKNITKVCLELGGKAPAIVMDDADLELAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ FVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVAFGGKAVEG KGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEDAISMANDSDYGLTSSIYTQNL NVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQS >1440 bp ATGTCAGTACCCGTTCAACATCCTATGTATATCGATGGACAGTTTGTTACCTGGCGTGGA GACGCATGGATTGATGTGGTAAACCCTGCTACAGAGGCTGTCATTTCCCGCATACCCGAT GGTCAGGCCGAGGATGCCCGTAAGGCAATCGATGCAGCAGAACGTGCACAACCAGAATGG GAAGCGTTGCCTGCTATTGAACGCGCCAGTTGGTTGCGCAAAATCTCCGCCGGGATCCGC GAACGCGCCAGTGAAATCAGTGCGCTGATTGTTGAAGAAGGGGGCAAGATCCAGCAGCTG GCTGAAGTCGAAGTGGCTTTTACTGCCGACTATATCGATTACATGGCGGAGTGGGCACGG CGTTACGAGGGCGAGATTATTCAAAGCGATCGTCCAGGAGAAAATATTCTTTTGTTTAAA CGTGCGCTTGGTGTGACTACCGGCATTCTGCCGTGGAACTTCCCGTTCTTCCTCATTGCC CGCAAAATGGCTCCCGCTCTTTTGACCGGTAATACCATCGTCATTAAACCTAGTGAATTT ACGCCAAACAATGCGATTGCATTCGCCAAAATCGTCGATGAAATAGGCCTTCCGCGCGGC GTGTTTAACCTTGTACTGGGGCGTGGTGAAACCGTTGGGCAAGAACTGGCGGGTAACCCA AAGGTCGCAATGGTCAGTATGACAGGCAGCGTCTCTGCAGGTGAGAAGATCATGGCGACT GCGGCGAAAAACATCACCAAAGTGTGTCTGGAATTGGGGGGTAAAGCACCAGCTATCGTA ATGGACGATGCCGATCTTGAACTGGCAGTCAAAGCCATCGTTGATTCACGCGTCATTAAT AGTGGGCAAGTGTGTAACTGTGCAGAACGTGTTTATGTACAGAAAGGCATTTATGATCAG TTCGTCAATCGGCTGGGTGAAGCGATGCAGGCGGTTCAATTTGGTAACCCCGCTGAACGC AACGACATTGCGATGGGGCCGTTGATTAACGCCGCGGCGCTGGAAAGGGTCGAGCAAAAA GTGGCGCGCGCAGTAGAAGAAGGGGCGAGAGTGGCGTTCGGTGGCAAAGCGGTAGAGGGG AAAGGATATTATTATCCGCCGACATTGCTGCTGGATGTTCGCCAGGAAATGTCGATTATG CATGAGGAAACCTTTGGCCCGGTGCTGCCAGTTGTCGCATTTGACACGCTGGAAGATGCT ATCTCAATGGCTAATGACAGTGATTACGGCCTGACCTCATCAATCTATACCCAAAATCTG AACGTCGCGATGAAAGCCATTAAAGGGCTGAAGTTTGGTGAAACTTACATCAACCGTGAA AACTTCGAAGCTATGCAAGGCTTCCACGCCGGATGGCGTAAATCCGGTATTGGCGGCGCA GATGGTAAACATGGCTTGCATGAATATCTGCAGACCCAGGTGGTTTATTTACAGTCTTAA PF00171 Aldedh BE0001817 Acriflavine resistance protein B Escherichia coli (strain K12) # 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 Acriflavine resistance protein B Defense mechanisms and drug export AcrAB is a drug efflux protein with a broad substrate specificity acrB Cell inner membrane; multi-pass membrane protein 10-28 337-356 366-385 392-413 439-457 466-490 539-555 872-888 899-918 925-943 973-992 999-1018 5.23 113575.0 Escherichia coli (strain K12) GenBank Gene Database M94248 GenBank Protein Database 290406 UniProtKB P31224 UniProt Accession ACRB_ECOLI >Acriflavine resistance protein B MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDT VTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQ EVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGS QYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRL TSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANAL DTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQ NFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVM AEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMAL SVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGR YLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLT KEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKD AMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNG LEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYR MLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEA MELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFS VMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGL IEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIF FVPVFFVVVRRRFSRKNEDIEHSHTVDHH >3150 bp ATGCCTAATTTCTTTATCGATCGCCCGATTTTTGCGTGGGTGATCGCCATTATCATCATG TTGGCAGGGGGGCTGGCGATCCTCAAACTGCCGGTGGCGCAATATCCTACGATTGCACCG CCGGCAGTAACGATCTCCGCCTCCTACCCCGGCGCTGATGCGAAAACAGTGCAGGACACG GTGACACAGGTTATCGAACAGAATATGAACGGTATCGATAACCTGATGTACATGTCCTCT AACAGTGACTCCACGGGTACCGTGCAGATCACCCTGACCTTTGAGTCTGGTACTGATGCG GATATCGCGCAGGTTCAGGTGCAGAACAAACTGCAGCTGGCGATGCCGTTGCTGCCGCAA GAAGTTCAGCAGCAAGGGGTGAGCGTTGAGAAATCATCCAGCAGCTTCCTGATGGTTGTC GGCGTTATCAACACCGATGGCACCATGACGCAGGAGGATATCTCCGACTACGTGGCGGCG AATATGAAAGATGCCATCAGCCGTACGTCGGGCGTGGGTGATGTTCAGTTGTTCGGTTCA CAGTACGCGATGCGTATCTGGATGAACCCGAATGAGCTGAACAAATTCCAGCTAACGCCG GTTGATGTCATTACCGCCATCAAAGCGCAGAACGCCCAGGTTGCGGCGGGTCAGCTCGGT GGTACGCCGCCGGTGAAAGGCCAACAGCTTAACGCCTCTATTATTGCTCAGACGCGTCTG ACCTCTACTGAAGAGTTCGGCAAAATCCTGCTGAAAGTGAATCAGGATGGTTCCCGCGTG CTGCTGCGTGACGTCGCGAAGATTGAGCTGGGTGGTGAGAACTACGACATCATCGCAGAG TTTAACGGCCAACCGGCTTCCGGTCTGGGGATCAAGCTGGCGACCGGTGCAAACGCGCTG GATACCGCTGCGGCAATCCGTGCTGAACTGGCGAAGATGGAACCGTTCTTCCCGTCGGGT CTGAAAATTGTTTACCCATACGACACCACGCCGTTCGTGAAAATCTCTATTCACGAAGTG GTTAAAACGCTGGTCGAAGCGATCATCCTCGTGTTCCTGGTTATGTATCTGTTCCTGCAG AACTTCCGCGCGACGTTGATTCCGACCATTGCCGTACCGGTGGTATTGCTCGGGACCTTT GCCGTCCTTGCCGCCTTTGGCTTCTCGATAAACACGCTAACAATGTTCGGGATGGTGCTC GCCATCGGCCTGTTGGTGGATGACGCCATCGTTGTGGTAGAAAACGTTGAGCGTGTTATG GCGGAAGAAGGTTTGCCGCCAAAAGAAGCTACCCGTAAGTCGATGGGGCAGATTCAGGGC GCTCTGGTCGGTATCGCGATGGTACTGTCGGCGGTATTCGTACCGATGGCCTTCTTTGGC GGTTCTACTGGTGCTATCTATCGTCAGTTCTCTATTACCATTGTTTCAGCAATGGCGCTG TCGGTACTGGTGGCGTTGATCCTGACTCCAGCTCTTTGTGCCACCATGCTGAAACCGATT GCCAAAGGCGATCACGGGGAAGGTAAAAAAGGCTTCTTCGGCTGGTTTAACCGCATGTTC GAGAAGAGCACGCACCACTACACCGACAGCGTAGGCGGTATTCTGCGCAGTACGGGGCGT TACCTGGTGCTGTATCTGATCATCGTGGTCGGCATGGCCTATCTGTTCGTGCGTCTGCCA AGCTCCTTCTTGCCAGATGAGGACCAGGGCGTGTTTATGACCATGGTTCAGCTGCCAGCA GGTGCAACGCAGGAACGTACACAGAAAGTGCTCAATGAGGTAACGCATTACTATCTGACC AAAGAAAAGAACAACGTTGAGTCGGTGTTCGCCGTTAACGGCTTCGGCTTTGCGGGACGT GGTCAGAATACCGGTATTGCGTTCGTTTCCTTGAAGGACTGGGCCGATCGTCCGGGCGAA GAAAACAAAGTTGAAGCGATTACCATGCGTGCAACACGCGCTTTCTCGCAAATCAAAGAT GCGATGGTTTTCGCCTTTAACCTGCCCGCAATCGTGGAACTGGGTACTGCAACCGGCTTT GACTTTGAGCTGATTGACCAGGCTGGCCTTGGTCACGAAAAACTGACTCAGGCGCGTAAC CAGTTGCTTGCAGAAGCAGCGAAGCACCCTGATATGTTGACCAGCGTACGTCCAAACGGT CTGGAAGATACCCCGCAGTTTAAGATTGATATCGACCAGGAAAAAGCGCAGGCGCTGGGT GTTTCTATCAACGACATTAACACCACTCTGGGCGCTGCATGGGGCGGCAGCTATGTGAAC GACTTTATCGACCGCGGTCGTGTGAAGAAAGTTTATGTCATGTCAGAAGCGAAATACCGT ATGCTGCCGGATGATATCGGCGACTGGTATGTTCGTGCTGCTGATGGTCAGATGGTGCCA TTCTCGGCGTTCTCCTCTTCTCGTTGGGAGTACGGTTCGCCGCGTCTGGAACGTTACAAC GGCCTGCCATCCATGGAAATCTTAGGCCAGGCGGCACCGGGTAAAAGTACCGGTGAAGCA ATGGAGCTGATGGAACAACTGGCGAGCAAACTGCCTACCGGTGTTGGCTATGACTGGACG GGGATGTCCTATCAGGAACGTCTCTCCGGCAACCAGGCACCTTCACTGTACGCGATTTCG TTGATTGTCGTGTTCCTGTGTCTGGCGGCGCTGTACGAGAGCTGGTCGATTCCGTTCTCC GTTATGCTGGTCGTTCCGCTGGGGGTTATCGGTGCGTTGCTGGCTGCCACCTTCCGTGGC CTGACCAATGACGTTTACTTCCAGGTAGGCCTGCTCACAACCATTGGGTTGTCGGCGAAG AACGCGATCCTTATCGTCGAATTCGCCAAAGACTTGATGGATAAAGAAGGTAAAGGTCTG ATTGAAGCGACGCTTGATGCGGTGCGGATGCGTTTACGTCCGATCCTGATGACCTCGCTG GCGTTTATCCTCGGCGTTATGCCGCTGGTTATCAGTACTGGTGCTGGTTCCGGCGCGCAG AACGCAGTAGGTACCGGTGTAATGGGCGGGATGGTGACCGCAACGGTACTGGCAATCTTC TTCGTTCCGGTATTCTTTGTGGTGGTTCGCCGCCGCTTTAGCCGCAAGAATGAAGATATC GAGCACAGCCATACTGTCGATCATCATTGA PF00873 ACR_tran component cell component intrinsic to membrane component integral to membrane component membrane function transporter activity process physiological process process cellular physiological process process transport BE0004055 Cytochrome c oxidase subunit 1 Rhodobacter sphaeroides # 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 Cytochrome c oxidase subunit 1 Energy production and conversion Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer ctaD Cell membrane 29-49 97-117 141-161 189-209 227-247 278-298 310-330 348-368 381-401 420-440 455-475 499-519 7.46 63146.4 Rhodobacter sphaeroides GeneCards ctaD GenBank Gene Database X62645 GenBank Protein Database 21955871 UniProtKB P33517 UniProt Accession COX1_RHOSH Cytochrome aa3 subunit 1 Cytochrome c oxidase polypeptide I >Cytochrome c oxidase subunit 1 MADAAIHGHEHDRRGFFTRWFMSTNHKDIGVLYLFTGGLVGLISVAFTVYMRMELMAPGV QFMCAEHLESGLVKGFFQSLWPSAVENCTPNGHLWNVMITGHGILMMFFVVIPALFGGFG NYFMPLHIGAPDMAFPRMNNLSYWLYVAGTSLAVASLFAPGGNGQLGSGIGWVLYPPLST SESGYSTDLAIFAVHLSGASSILGAINMITTFLNMRAPGMTMHKVPLFAWSIFVTAWLIL LALPVLAGAITMLLTDRNFGTTFFQPSGGGDPVLYQHILWFFGHPEVYIIVLPAFGIVSH VIATFAKKPIFGYLPMVYAMVAIGVLGFVVWAHHMYTAGLSLTQQSYFMMATMVIAVPTG IKIFSWIATMWGGSIELKTPMLWALGFLFLFTVGGVTGIVLSQASVDRYYHDTYYVVAHF HYVMSLGAVFGIFAGIYFWIGKMSGRQYPEWAGKLHFWMMFVGANLTFFPQHFLGRQGMP RRYIDYPEAFATWNFVSSLGAFLSFASFLFFLGVIFYTLTRGARVTANNYWNEHADTLEW TLTSPPPEHTFEQLPKREDWERAPAH >1701 bp ATGGCCGACGCAGCCATCCATGGCCACGAGCACGACCGGAGGGGGTTCTTCACCCGCTGG TTCATGTCGACGAACCACAAGGACATCGGCGTTCTCTATCTCTTCACCGGGGGCCTCGTC GGGCTGATCTCGGTGGCCTTCACCGTCTACATGCGGATGGAGCTCATGGCGCCGGGCGTG CAGTTCATGTGCGCCGAACATCTAGAATCGGGCCTCGTGAAGGGCTTCTTCCAGTCGCTC TGGCCCTCGGCGGTGGAAAACTGCACCCCGAACGGCCATCTGTGGAACGTCATGATCACC GGCCACGGGATCCTGATGATGTTCTTCGTGGTCATTCCCGCGCTCTTCGGCGGCTTCGGC AACTATTTCATGCCGCTGCACATCGGCGCGCCGGACATGGCCTTCCCGCGGATGAACAAC CTCTCCTACTGGCTCTATGTCGCGGGCACCTCGCTCGCCGTCGCCTCGCTCTTCGCGCCG GGCGGCAACGGCCAGCTGGGCTCTGGCATCGGCTGGGTGCTCTATCCGCCGCTCTCCACC TCCGAATCGGGCTATTCCACCGACCTCGCGATCTTCGCGGTGCACCTGTCGGGCGCCTCC TCGATCCTCGGCGCGATCAACATGATCACGACCTTCCTGAACATGCGCGCACCCGGCATG ACCATGCACAAGGTGCCGCTCTTCGCCTGGTCGATCTTCGTCACCGCCTGGCTGATCCTG CTGGCGCTGCCCGTGCTCGCCGGCGCCATTACCATGCTGCTGACCGACCGGAACTTCGGC ACCACCTTCTTCCAGCCCTCGGGCGGCGGCGACCCGGTGCTCTACCAGCACATCCTGTGG TTCTTCGGCCACCCGGAGGTCTACATCATCGTGCTGCCGGCCTTCGGCATCGTCAGCCAC GTCATCGCGACCTTCGCCAAAAAGCCGATCTTCGGCTATTTGCCGATGGTCTATGCGATG GTGGCGATCGGCGTGCTGGGCTTCGTGGTCTGGGCCCACCACATGTATACAGCCGGCCTG AGCCTCACCCAGCAGAGCTACTTTATGATGGCGACCATGGTGATCGCAGTGCCCACCGGC ATCAAGATCTTCTCCTGGATCGCGACCATGTGGGGCGGCTCGATCGAGCTCAAGACGCCG ATGCTCTGGGCGCTCGGGTTCCTCTTCCTCTTCACCGTGGGCGGCGTCACCGGCATCGTG CTGAGCCAGGCGAGCGTCGACCGCTATTATCACGACACCTACTATGTCGTGGCGCACTTC CATTATGTGATGAGCCTCGGCGCGGTCTTCGGCATCTTCGCAGGGATCTACTTCTGGATC GGCAAGATGTCGGGCCGGCAATATCCGGAATGGGCCGGGAAGCTGCATTTCTGGATGATG TTCGTGGGCGCGAACCTCACCTTCTTCCCGCAGCACTTCCTCGGCCGCCAGGGCATGCCG CGGCGCTACATCGACTATCCCGAGGCCTTCGCCACCTGGAACTTCGTCTCGTCGCTGGGC GCCTTCCTGTCCTTCGCCTCGTTCCTCTTCTTCCTCGGCGTGATCTTCTACACGCTGACG CGCGGGGCGCGGGTGACGGCGAACAACTACTGGAACGAACATGCCGACACGCTGGAGTGG ACGCTGACCTCTCCGCCGCCGGAGCATACGTTCGAGCAGCTTCCCAAGCGGGAAGACTGG GAACGCGCGCCCGCCCACTGA PF00115 COX1 component cell component membrane function heme-copper terminal oxidase activity function cytochrome-c oxidase activity function catalytic activity function oxidoreductase activity process generation of precursor metabolites and energy process electron transport process physiological process process metabolism process cellular metabolism BE0004056 Cytochrome c oxidase subunit 2 Rhodobacter sphaeroides # 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 Cytochrome c oxidase subunit 2 Energy production and conversion Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B) ctaC Cell membrane 60-80 104-124 4.63 32930.4 Rhodobacter sphaeroides GeneCards ctaC GenBank Gene Database M57680 GenBank Protein Database 15022167 UniProtKB Q03736 UniProt Accession COX2_RHOSH Cytochrome aa3 subunit 2 Cytochrome c oxidase polypeptide II Oxidase aa(3) subunit 2 >Cytochrome c oxidase subunit 2 MRHSTTLTGCATGAAGLLAATAAAAQQQSLEIIGRPQPGGTGFQPSASPVATQIHWLDGF ILVIIAAITIFVTLLILYAVWRFHEKRNKVPARFTHNSPLEIAWTIVPIVILVAIGAFSL PVLFNQQEIPEADVTVKVTGYQWYWGYEYPDEEISFESYMIGSPATGGDNRMSPEVEQQL IEAGYSRDEFLLATDTAMVVPVNKTVVVQVTGADVIHSWTVPAFGVKQDAVPGRLAQLWF RAEREGIFFGQCSELCGISHAYMPITVKVVSEEAYAAWLEQARGGTYELSSVLPATPAGV SVE >912 bp ATGAGACATTCCACGACCTTGACCGGATGCGCCACGGGGGCGGCAGGGCTTCTGGCGGCC ACGGCCGCGGCCGCGCAGCAGCAGAGCCTCGAGATCATCGGGCGGCCGCAGCCGGGGGGC ACGGGCTTCCAGCCTTCGGCGAGCCCGGTGGCCACGCAGATCCATTGGCTCGACGGGTTC ATCCTCGTCATCATCGCCGCCATCACCATCTTCGTCACGCTCCTTATCCTCTATGCGGTC TGGCGCTTCCATGAGAAGCGCAACAAGGTGCCGGCCCGCTTCACCCACAATTCCCCGCTC GAGATCGCCTGGACGATCGTGCCGATCGTCATCCTCGTGGCCATCGGGGCCTTCTCGCTG CCGGTGCTGTTCAACCAGCAGGAAATCCCCGAGGCGGACGTGACGGTGAAGGTCACGGGC TACCAGTGGTACTGGGGCTACGAATATCCCGACGAGGAAATCTCGTTCGAGAGCTACATG ATCGGCTCGCCCGCCACGGGTGGCGACAACCGTATGTCGCCCGAGGTCGAGCAGCAGCTG ATCGAGGCCGGCTACAGCCGCGACGAGTTCCTGCTGGCCACCGACACCGCCATGGTCGTG CCGGTGAACAAGACCGTCGTGGTGCAGGTGACCGGTGCCGACGTGATCCACTCCTGGACC GTGCCCGCCTTCGGCGTGAAGCAGGATGCGGTGCCGGGCCGGCTCGCGCAGCTCTGGTTC CGGGCCGAGCGCGAGGGGATCTTCTTCGGCCAGTGTTCGGAGCTCTGCGGCATCTCGCAC GCCTACATGCCGATCACGGTCAAGGTCGTGTCGGAAGAAGCCTATGCCGCCTGGCTCGAA CAGGCCCGCGGCGGCACCTACGAGCTGTCCTCCGTCCTGCCCGCGACGCCTGCGGGCGTG TCGGTGGAGTGA PF00116 COX2 PF02790 COX2_TM component integral to membrane component membrane component organelle membrane component organelle inner membrane component cell component intrinsic to membrane function catalytic activity function copper ion binding function oxidoreductase activity function ion binding function cation binding function heme-copper terminal oxidase activity function transition metal ion binding function cytochrome-c oxidase activity function binding process metabolism process cellular metabolism process generation of precursor metabolites and energy process electron transport process physiological process "

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

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