ID   DIDH_PSESP              Reviewed;          15 AA.
AC   P80701;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   28-JAN-2026, entry version 57.
DE   RecName: Full=3-alpha-hydroxysteroid dehydrogenase/carbonyl reductase;
DE            Short=3-alpha-HSD;
DE            EC=1.1.1.50;
DE   AltName: Full=3-alpha-hydroxysteroid dehydrogenase/3-oxosteroid reductase;
DE   AltName: Full=HSD29;
DE   AltName: Full=Hydroxyprostaglandin dehydrogenase;
DE   Flags: Fragment;
OS   Pseudomonas sp.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   PROTEIN SEQUENCE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8944761; DOI=10.1111/j.1432-1033.1996.00744.x;
RA   Oppermann U.C.T., Maser E.;
RT   "Characterization of a 3 alpha-hydroxysteroid dehydrogenase/carbonyl
RT   reductase from the Gram-negative bacterium Comamonas testosteroni.";
RL   Eur. J. Biochem. 241:744-749(1996).
CC   -!- FUNCTION: Along with the 3 alpha-hydroxysteroid dehydrogenase and 3-
CC       oxo-reductase activities towards a variety of cis or trans fused A/B
CC       ring steroids, it also reduces several xenobiotic carbonyl compounds,
CC       including a metyrapone-based class of insecticides, to the respective
CC       alcohol metabolites. No detectable activity on testosterone,
CC       progesterone or 3-oxo-desogestrel.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + NADPH +
CC         H(+); Xref=Rhea:RHEA:34783, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.50;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + NADH +
CC         H(+); Xref=Rhea:RHEA:34779, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835,
CC         ChEBI:CHEBI:47788, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.50;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=26.7 uM for androsterone {ECO:0000269|PubMed:8944761};
CC         KM=6.8 uM for fusidic acid {ECO:0000269|PubMed:8944761};
CC         KM=630 uM for metyrapone {ECO:0000269|PubMed:8944761};
CC         Vmax=5.5 umol/min/mg enzyme for androsterone
CC         {ECO:0000269|PubMed:8944761};
CC         Vmax=11.3 umol/min/mg enzyme fusidic acid
CC         {ECO:0000269|PubMed:8944761};
CC         Vmax=0.6 umol/min/mg enzyme metyrapone {ECO:0000269|PubMed:8944761};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   BRENDA; 1.1.1.357; 5085.
DR   SABIO-RK; P80701; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0140169; F:3-alpha-hydroxysteroid 3-dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..>15
FT                   /note="3-alpha-hydroxysteroid dehydrogenase/carbonyl
FT                   reductase"
FT                   /id="PRO_0000054657"
FT   REGION          6..>15
FT                   /note="Involved in cofactor binding"
FT                   /evidence="ECO:0000250"
FT   NON_TER         15
SQ   SEQUENCE   15 AA;  1315 MW;  9506860D070A7790 CRC64;
     QVIAITGSAS GIGAA
//