DB code: S00330

RLCP classification 9.1050.440000.8010 : Hydride transfer
CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.159
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0AET8 7-alpha-hydroxysteroid dehydrogenase
7-alpha-HSDH
EC 1.1.1.159
NP_416136.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489882.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00106 (adh_short)
[Graphical View]
Q8YIN7
7-ALPHA-HYDROXYSTEROID DEHYDROGENASE
EC 1.1.1.159
[Graphical View]

KEGG enzyme name
7alpha-hydroxysteroid dehydrogenase
7alpha-hydroxy steroid dehydrogenase
7alpha-HSDH

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0AET8 HDHA_ECOLI 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD(+) = 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH. Homotetramer.
Q8YIN7 Q8YIN7_BRUME

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00695 C00003 C00006 C04643 C00004 C00005 C00080
E.C.
Compound 3alpha,7alpha,12alpha-Trihydroxy-5beta-cholanate NAD+ NADP+ 3alpha,12alpha-Dihydroxy-7-oxo-5beta-cholanate NADH NADPH H+
Type carbohydrate,fatty acid,steroid amide group,amine group,nucleotide amide group,amine group,nucleotide carbohydrate,carboxyl group,steroid amide group,amine group,nucleotide amide group,amine group,nucleotide others
ChEBI 16359
 16359
 		15846
 15846
 		18009
 18009
 		16390
 16390
 		16908
 16908
 		16474
 16474
 		15378
 15378
PubChem 221493
 221493
 		5893
 5893
 		5886
 5886
 		188292
 440419
 188292
 440419
 		439153
 439153
 		5884
 5884
 		1038
 1038
1ahhA Unbound Bound:NAD Unbound Unbound Unbound Unbound
1ahhB Unbound Bound:NAD Unbound Unbound Unbound Unbound
1ahiA Unbound Bound:NAD Unbound Analogue:CHO Unbound Unbound
1ahiB Unbound Bound:NAD Unbound Analogue:CHO Unbound Unbound
1fmcA Unbound Bound:NAD Unbound Analogue:CHO Unbound Unbound
1fmcB Unbound Bound:NAD Unbound Analogue:CHO Unbound Unbound
3gafA Unbound Unbound Unbound Unbound Unbound Unbound
3gafB Unbound Unbound Unbound Unbound Unbound Unbound
3gafC Unbound Unbound Unbound Unbound Unbound Unbound
3gafD Unbound Unbound Unbound Unbound Unbound Unbound
3gafE Unbound Unbound Unbound Unbound Unbound Unbound
3gafF Unbound Unbound Unbound Unbound Unbound Unbound
3gafG Unbound Unbound Unbound Unbound Unbound Unbound
3gafH Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P0AET8 & literature [8], [11]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ahhA SER 146;TYR 159;LYS 163
1ahhB SER 146;TYR 159;LYS 163
1ahiA SER 146;TYR 159;LYS 163
1ahiB SER 146;TYR 159;LYS 163
1fmcA SER 146;TYR 159;LYS 163
1fmcB SER 146;TYR 159;LYS 163
3gafA SER 146;TYR 159;LYS 163
3gafB SER 146;TYR 159;LYS 163
3gafC SER 146;TYR 159;LYS 163
3gafD SER 146;TYR 159;LYS 163
3gafE SER 146;TYR 159;LYS 163
3gafF SER 146;TYR 159;LYS 163
3gafG SER 146;TYR 159;LYS 163
3gafH SER 146;TYR 159;LYS 163

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[8]
p.7727-7728, Fig.11 2
[11]
p.639-641

References
[1]
Resource
Comments
Medline ID
PubMed ID 4581498
Journal Biochim Biophys Acta
Year 1973
Volume 309
Pages 243-53
Authors Macdonald IA, Williams CN, Mahony DE
Title 7Alpha-hydroxysteroid dehydrogenase from Escherichia coli B: preliminary studies.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 236764
Journal Biochim Biophys Acta
Year 1975
Volume 384
Pages 12-24
Authors Macdonald IA, Williams CN, Mahony DE, Christie WM
Title NAD- and NADP-dependent 7alpha-hydroxysteroid dehydrogenases from bacteroides fragilis.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 189820
Journal Biochim Biophys Acta
Year 1977
Volume 486
Pages 351-8
Authors Sherrod JA, Hylemon PB
Title Partial purification and characterization of NAD-dependent 7alpha-hydroxysteroid dehydrogenase from Bacteroides thetaiotaomicron.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 6574791
Journal Biochim Biophys Acta
Year 1983
Volume 750
Pages 397-403
Authors Macdonald IA, Sutherland JD
Title Further studies on the bile salt induction of 7 alpha- and 7 beta-hydroxysteroid dehydrogenases in Clostridium absonum.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 6366102
Journal J Lipid Res
Year 1983
Volume 24
Pages 1550-9
Authors Macdonald IA, Sutherland JD, Cohen BI, Mosbach EH
Title Effect of bile acid oxazoline derivatives on microorganisms participating in 7 alpha-hydroxyl epimerization of primary bile acids.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 2675982
Journal Biochim Biophys Acta
Year 1989
Volume 998
Pages 173-8
Authors Ottolina G, Riva S, Carrea G, Danieli B, Buckmann AF
Title Enzymatic 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.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 2007545
Journal J Bacteriol
Year 1991
Volume 173
Pages 2173-9
Authors Yoshimoto T, Higashi H, Kanatani A, Lin XS, Nagai H, Oyama H, Kurazono K, Tsuru D
Title Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene from Escherichia coli HB101 and characterization of the expressed enzyme.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 AND 1.8 ANGSTROMS)
Medline ID 96264882
PubMed ID 8672472
Journal Biochemistry
Year 1996
Volume 35
Pages 7715-30
Authors Tanaka N, Nonaka T, Tanabe T, Yoshimoto T, Tsuru D, Mitsui Y
Title Crystal structures of the binary and ternary complexes of 7 alpha-hydroxysteroid dehydrogenase from Escherichia coli.
Related PDB 1ahh 1ahi 1fmc
Related UniProtKB P0AET8
[9]
Resource
Comments
Medline ID
PubMed ID 9562905
Journal Biochem Genet
Year 1998
Volume 36
Pages 37-49
Authors Smilda T, Reinders P, Beintema JJ
Title Modeling studies of conformational changes in the substrate-binding loop in Drosophila alcohol dehydrogenase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9632680
Journal J Biol Chem
Year 1998
Volume 273
Pages 16223-8
Authors Song W, Chen J, Dean WL, Redinger RN, Prough RA
Title Purification and characterization of hamster liver microsomal 7alpha-hydroxycholesterol dehydrogenase. Similarity to type I 11beta-hydroxysteroid dehydrogenase.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 9722677
Journal J Biochem (Tokyo)
Year 1998
Volume 124
Pages 634-41
Authors Tanabe T, Tanaka N, Uchikawa K, Kabashima T, Ito K, Nonaka T, Mitsui Y, Tsuru M, Yoshimoto T
Title Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli.
Related PDB
Related UniProtKB

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.

Created Updated
2004-02-02 2011-06-28