EzCatDB: S00325
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DB codeS00325
RLCP classification9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.50,1.1.1.184

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,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

Enzyme Name
UniProtKBKEGG

P80702
Protein name3-alpha-hydroxysteroid dehydrogenase3alpha-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)

Synonyms3-alpha-HSD
EC 1.1.1.50
Hydroxyprostaglandin dehydrogenase
HSD28

KEGG pathways
MAP codePathwaysE.C.
MAP00120Bile acid biosynthesis1.1.1.50
MAP00140C21-Steroid hormone metabolism1.1.1.50
MAP00150Androgen and estrogen metabolism1.1.1.50
MAP00590Arachidonic acid metabolism1.1.1.184

UniProtKB:Accession NumberP80702
Entry nameDIDH_COMTE
ActivityAndrosterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H.
SubunitHomodimer.
Subcellular locationCytoplasm.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00523C00003C01612C00674C01450C00004C00080
E.C.1.1.1.501.1.1.50,1.1.1.1841.1.1.1841.1.1.501.1.1.1841.1.1.50,1.1.1.1841.1.1.50,1.1.1.184
CompoundAndrosteroneNAD+R-CHOH-R'5alpha-Androstane-3,17-dioneR-CO-R'NADHH+
Typecarbohydrate,steroidamide group,amine group,nucleotidecarbohydratecarbohydrate,steroidcarbohydrateamide group,amine group,nucleotideothers
ChEBI16032
15846

15994

16908
15378
PubChem5879
5893

439289
222865

439153
1038
               
1fjhAUnboundUnboundUnboundUnboundUnboundUnbound 
1fjhBUnboundUnboundUnboundUnboundUnboundUnbound 
1fk8AUnboundBound:NADBound:NADUnboundUnboundUnbound 
1fk8BUnboundBound:NADBound:NADUnboundUnboundUnbound 

Active-site residues
resource
literature
pdbCatalytic residues
         
1fjhASER  114;TYR  155;LYS  159
1fjhBSER 1114;TYR 1155;LYS 1159
1fk8ASER  114;TYR  155;LYS  159
1fk8BSER 1114;TYR 1155;LYS 1159

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.41336-41337
[4]p.714-715
[6]Fig.5A

references
[1]
PubMed ID9812981
JournalJ Biol Chem
Year1998
Volume273
Pages30888-96
AuthorsMobus E, Maser E
TitleMolecular 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.
[2]
PubMed ID10833462
JournalBiochem Biophys Res Commun
Year2000
Volume272
Pages622-8
AuthorsMaser E, Mobus E, Xiong G
TitleFunctional expression, purification, and characterization of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni.
[3]
CommentsX-ray crystallography
PubMed ID11007791
JournalJ Biol Chem
Year2000
Volume275
Pages41333-9
AuthorsGrimm C, Maser E, Mobus E, Klebe G, Reuter K, Ficner R
TitleThe crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family.
Related PDB1fjh,1fk8
[4]
PubMed ID11306088
JournalChem Biol Interact
Year2001
Volume130-132
Pages707-22
AuthorsMaser E, Xiong G, Grimm C, Ficner R, Reuter K
Title3alpha-Hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: biological significance, three-dimensional structure and gene regulation.
[5]
PubMed ID11306089
JournalChem Biol Interact
Year2001
Volume130-132
Pages723-36
AuthorsXiong G, Martin H, Blum A, Schafers C, Maser E
TitleA model on the regulation of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase expression in Comamonas testosteroni.
[6]
PubMed ID15572373
JournalJ Biol Chem
Year2004
Volume280
Pages3522-8
AuthorsHwang CC, Chang YH, Hsu CN, Hsu HH, Li CW, Pon HI
TitleMechanistic roles of Ser114, Tyr155 and Lys159 in 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni.

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.

createdupdated
2004-05-132012-06-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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