EzCatDB: S00330
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DB codeS00330
RLCP classification9.1050.440000.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.159

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
UniProtKBKEGG

P0AET8Q8YIN7
Protein name7-alpha-hydroxysteroid dehydrogenase
7alpha-hydroxysteroid dehydrogenase
7alpha-hydroxy steroid dehydrogenase
7alpha-HSDH
Synonyms7-alpha-HSDH
EC 1.1.1.159
7-ALPHA-HYDROXYSTEROID DEHYDROGENASE
EC 1.1.1.159
RefSeqNP_416136.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489882.1 (Protein)
NC_007779.1 (DNA/RNA sequence)

PfamPF00106 (adh_short)
[Graphical view]



UniProtKB:Accession NumberP0AET8Q8YIN7
Entry nameHDHA_ECOLIQ8YIN7_BRUME
Activity3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD(+) = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH.
SubunitHomotetramer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00695C00003C00006C04643C00004C00005C00080
Compound3alpha,7alpha,12alpha-Trihydroxy-5beta-cholanateNAD+NADP+3alpha,12alpha-Dihydroxy-7-oxo-5beta-cholanateNADHNADPHH+
Typecarbohydrate,fatty acid,steroidamide group,amine group,nucleotideamide group,amine group,nucleotidecarbohydrate,carboxyl group,steroidamide group,amine group,nucleotideamide group,amine group,nucleotideothers
ChEBI16359
15846
18009
16390
16908
16474
15378
PubChem221493
5893
5886
440419
188292
439153
5884
1038
               
1ahhAUnboundBound:NADUnboundUnboundUnboundUnbound 
1ahhBUnboundBound:NADUnboundUnboundUnboundUnbound 
1ahiAUnboundBound:NADUnboundAnalogue:CHOUnboundUnbound 
1ahiBUnboundBound:NADUnboundAnalogue:CHOUnboundUnbound 
1fmcAUnboundBound:NADUnboundAnalogue:CHOUnboundUnbound 
1fmcBUnboundBound:NADUnboundAnalogue:CHOUnboundUnbound 
3gafAUnboundUnboundUnboundUnboundUnboundUnbound 
3gafBUnboundUnboundUnboundUnboundUnboundUnbound 
3gafCUnboundUnboundUnboundUnboundUnboundUnbound 
3gafDUnboundUnboundUnboundUnboundUnboundUnbound 
3gafEUnboundUnboundUnboundUnboundUnboundUnbound 
3gafFUnboundUnboundUnboundUnboundUnboundUnbound 
3gafGUnboundUnboundUnboundUnboundUnboundUnbound 
3gafHUnboundUnboundUnboundUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot;P0AET8 & literature [8], [11]
pdbCatalytic residues
         
1ahhASER 146;TYR 159;LYS 163
1ahhBSER 146;TYR 159;LYS 163
1ahiASER 146;TYR 159;LYS 163
1ahiBSER 146;TYR 159;LYS 163
1fmcASER 146;TYR 159;LYS 163
1fmcBSER 146;TYR 159;LYS 163
3gafASER 146;TYR 159;LYS 163
3gafBSER 146;TYR 159;LYS 163
3gafCSER 146;TYR 159;LYS 163
3gafDSER 146;TYR 159;LYS 163
3gafESER 146;TYR 159;LYS 163
3gafFSER 146;TYR 159;LYS 163
3gafGSER 146;TYR 159;LYS 163
3gafHSER 146;TYR 159;LYS 163

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]p.7727-7728, Fig.112
[11]p.639-641

references
[1]
PubMed ID4581498
JournalBiochim Biophys Acta
Year1973
Volume309
Pages243-53
AuthorsMacdonald IA, Williams CN, Mahony DE
Title7Alpha-hydroxysteroid dehydrogenase from Escherichia coli B: preliminary studies.
[2]
PubMed ID236764
JournalBiochim Biophys Acta
Year1975
Volume384
Pages12-24
AuthorsMacdonald IA, Williams CN, Mahony DE, Christie WM
TitleNAD- and NADP-dependent 7alpha-hydroxysteroid dehydrogenases from bacteroides fragilis.
[3]
PubMed ID189820
JournalBiochim Biophys Acta
Year1977
Volume486
Pages351-8
AuthorsSherrod JA, Hylemon PB
TitlePartial purification and characterization of NAD-dependent 7alpha-hydroxysteroid dehydrogenase from Bacteroides thetaiotaomicron.
[4]
PubMed ID6574791
JournalBiochim Biophys Acta
Year1983
Volume750
Pages397-403
AuthorsMacdonald IA, Sutherland JD
TitleFurther studies on the bile salt induction of 7 alpha- and 7 beta-hydroxysteroid dehydrogenases in Clostridium absonum.
[5]
PubMed ID6366102
JournalJ Lipid Res
Year1983
Volume24
Pages1550-9
AuthorsMacdonald IA, Sutherland JD, Cohen BI, Mosbach EH
TitleEffect of bile acid oxazoline derivatives on microorganisms participating in 7 alpha-hydroxyl epimerization of primary bile acids.
[6]
PubMed ID2675982
JournalBiochim Biophys Acta
Year1989
Volume998
Pages173-8
AuthorsOttolina G, Riva S, Carrea G, Danieli B, Buckmann AF
TitleEnzymatic synthesis of [4R-2H]NAD (P)H and [4S-2H]NAD(P)H and determination of the stereospecificity of 7 alpha- and 12 alpha hydroxysteroid dehydrogenase.
[7]
PubMed ID2007545
JournalJ Bacteriol
Year1991
Volume173
Pages2173-9
AuthorsYoshimoto T, Higashi H, Kanatani A, Lin XS, Nagai H, Oyama H, Kurazono K, Tsuru D
TitleCloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 AND 1.8 ANGSTROMS)
Medline ID96264882
PubMed ID8672472
JournalBiochemistry
Year1996
Volume35
Pages7715-30
AuthorsTanaka N, Nonaka T, Tanabe T, Yoshimoto T, Tsuru D, Mitsui Y
TitleCrystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli.
Related PDB1ahh,1ahi,1fmc
Related UniProtKBP0AET8
[9]
PubMed ID9562905
JournalBiochem Genet
Year1998
Volume36
Pages37-49
AuthorsSmilda T, Reinders P, Beintema JJ
TitleModeling studies of conformational changes in the substrate-binding loop in Drosophila alcohol dehydrogenase.
[10]
PubMed ID9632680
JournalJ Biol Chem
Year1998
Volume273
Pages16223-8
AuthorsSong W, Chen J, Dean WL, Redinger RN, Prough RA
TitlePurification and characterization of hamster liver microsomal 7alpha-hydroxycholesterol dehydrogenase. Similarity to type I 11beta-hydroxysteroid dehydrogenase.
[11]
PubMed ID9722677
JournalJ Biochem (Tokyo)
Year1998
Volume124
Pages634-41
AuthorsTanabe T, Tanaka N, Uchikawa K, Kabashima T, Ito K, Nonaka T, Mitsui Y, Tsuru M, Yoshimoto T
TitleRoles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli.

comments
This enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, along with Drosophia alcohol dehydrogenase (S00319 in EzCatDB). This enzyme has got a catalytic triad composed of conserved residues, Ser, Tyr, and Lys. The conformation of these residues, compared to that of the NAD molecule, seems to be similar to that of the homologous enzymes.
According to the literature [8] and [11], this enzyme catalyzes hydride transfer reaction, which is similar to that of the homologous enzymes.

createdupdated
2004-02-022011-06-28


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