ID   12AH_CLOS4              Reviewed;          29 AA.
AC   P21215;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=12-alpha-hydroxysteroid dehydrogenase;
DE            EC=1.1.1.176;
DE   Flags: Fragment;
OS   Clostridium sp. (strain ATCC 29733 / VPI C48-50).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1507;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2007406; DOI=10.1111/j.1432-1033.1991.tb15835.x;
RA   Braun M., Luensdorf H., Bueckmann A.F.;
RT   "12 alpha-hydroxysteroid dehydrogenase from Clostridium group P, strain C
RT   48-50. Production, purification and characterization.";
RL   Eur. J. Biochem. 196:439-450(1991).
CC   -!- FUNCTION: Catalyzes the oxidation of the 12-alpha-hydroxyl group of
CC       bile acids, both in their free and conjugated form. Also acts on bile
CC       alcohols.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholate + NADP(+) = 3alpha,7alpha-dihydroxy-12-oxo-5beta-
CC         cholanate + H(+) + NADPH; Xref=Rhea:RHEA:14129, ChEBI:CHEBI:11901,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.176;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: The thermostability of the enzyme is greatly increased
CC       due to NADP binding.
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   PIR; S14099; S14099.
DR   AlphaFoldDB; P21215; -.
DR   SMR; P21215; -.
DR   eggNOG; COG1028; Bacteria.
DR   BioCyc; MetaCyc:MON-15705; -.
DR   GO; GO:0047013; F:cholate 12-alpha dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Bile acid catabolism; Direct protein sequencing; Lipid degradation;
KW   Lipid metabolism; NADP; Oxidoreductase; Steroid metabolism.
FT   CHAIN           1..>29
FT                   /note="12-alpha-hydroxysteroid dehydrogenase"
FT                   /id="PRO_0000064347"
FT   NON_TER         29
SQ   SEQUENCE   29 AA;  2900 MW;  A827DB34DB6C8812 CRC64;
     MIFDGKVAII TGGGKAKSIG YGIAVAYAK