DB code: S00325

RLCP classification 9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domain 3.40.50.720 : Rossmann fold Catalytic domain
E.C. 1.1.1.50 1.1.1.184
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 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 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
P80702 3-alpha-hydroxysteroid dehydrogenase
3-alpha-HSD
EC 1.1.1.50
Hydroxyprostaglandin dehydrogenase
HSD28

KEGG enzyme name
3alpha-hydroxysteroid dehydrogenase (B-specific)
(EC 1.1.1.50 )
hydroxyprostaglandin dehydrogenase
(EC 1.1.1.50 )
3alpha-hydroxysteroid oxidoreductase
(EC 1.1.1.50 )
sterognost 3alpha
(EC 1.1.1.50 )
carbonyl reductase (NADPH)
(EC 1.1.1.184 )
aldehyde reductase 1
(EC 1.1.1.184 )
prostaglandin 9-ketoreductase
(EC 1.1.1.184 )
xenobiotic ketone reductase
(EC 1.1.1.184 )
NADPH-dependent carbonyl reductase
(EC 1.1.1.184 )
ALR3
(EC 1.1.1.184 )
carbonyl reductase
(EC 1.1.1.184 )
nonspecific NADPH-dependent carbonyl reductase
(EC 1.1.1.184 )
aldehyde reductase 1
(EC 1.1.1.184 )
carbonyl reductase (NADPH)
(EC 1.1.1.184 )

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P80702 DIDH_COMTE Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. Homodimer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00120 Bile acid biosynthesis 1.1.1.50
MAP00140 C21-Steroid hormone metabolism 1.1.1.50
MAP00150 Androgen and estrogen metabolism 1.1.1.50
MAP00590 Arachidonic acid metabolism 1.1.1.184

Compound table
Substrates Products Intermediates
KEGG-id C00523 C00003 C01612 C00674 C01450 C00004 C00080
E.C. 1.1.1.50
1.1.1.50
1.1.1.184
1.1.1.184
1.1.1.50
1.1.1.184
1.1.1.50
1.1.1.184
1.1.1.50
1.1.1.184
Compound Androsterone NAD+ R-CHOH-R' 5alpha-Androstane-3,17-dione R-CO-R' NADH H+
Type carbohydrate,steroid amide group,amine group,nucleotide carbohydrate carbohydrate,steroid carbohydrate amide group,amine group,nucleotide others
ChEBI 16032
 16032
 		15846
 15846
 		15994
 15994
 		16908
 16908
 		15378
 15378
PubChem 5879
 5879
 		5893
 5893
 		222865
 439289
 222865
 439289
 		439153
 439153
 		1038
 1038
1fjhA Unbound Unbound Unbound Unbound Unbound Unbound
1fjhB Unbound Unbound Unbound Unbound Unbound Unbound
1fk8A Unbound Bound:NAD Bound:NAD Unbound Unbound Unbound
1fk8B Unbound Bound:NAD Bound:NAD Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1fjhA SER 114;TYR 155;LYS 159
1fjhB SER 1114;TYR 1155;LYS 1159
1fk8A SER 114;TYR 155;LYS 159
1fk8B SER 1114;TYR 1155;LYS 1159

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.41336-41337
[4]
p.714-715
[6]
Fig.5A

References
[1]
Resource
Comments
Medline ID
PubMed ID 9812981
Journal J Biol Chem
Year 1998
Volume 273
Pages 30888-96
Authors Mobus E, Maser E
Title Molecular cloning, overexpression, and characterization of steroid-inducible 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 10833462
Journal Biochem Biophys Res Commun
Year 2000
Volume 272
Pages 622-8
Authors Maser E, Mobus E, Xiong G
Title Functional expression, purification, and characterization of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11007791
Journal J Biol Chem
Year 2000
Volume 275
Pages 41333-9
Authors Grimm C, Maser E, Mobus E, Klebe G, Reuter K, Ficner R
Title The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family.
Related PDB 1fjh 1fk8
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11306088
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 707-22
Authors Maser E, Xiong G, Grimm C, Ficner R, Reuter K
Title 3alpha-Hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: biological significance, three-dimensional structure and gene regulation.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11306089
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 723-36
Authors Xiong G, Martin H, Blum A, Schafers C, Maser E
Title A model on the regulation of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase expression in Comamonas testosteroni.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 15572373
Journal J Biol Chem
Year 2004
Volume 280
Pages 3522-8
Authors Hwang CC, Chang YH, Hsu CN, Hsu HH, Li CW, Pon HI
Title Mechanistic roles of Ser114, Tyr155 and Lys159 in 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni.
Related PDB
Related UniProtKB

Comments
According to the Swiss-prot data (Q9ZFY9), "Acyl-[acyl-carrier protein]" and "trans-2,3-dehydroacyl-[acyl-carrier protein]" are substrate and product, respectively, suggesting that its E.C. number should be 1.3.1.9, instead of 1.1.1.50. However, according to the literature [4] & [6], this enzyme catalyzes dehydrogenation of 3alpha-OH of androsterone.
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. Thus, its catalytic mechanism must be similar to those of the homologous enzymes.

Created Updated
2004-05-13 2012-06-26