Local view for "http://wifo5-04.informatik.uni-mannheim.de/drugbank/resource/drugs/DB07690"
Predicate | Value (sorted: none) |
---|---|
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
"
|
rdf:type | |
rdfs:label |
"(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID"
|
All properties reside in the graph file:///home/swish/src/ClioPatria/guidelines/drugbank_small.nt
The resource does not appear as an object