ID   3BHS_VACCA              Reviewed;         346 AA.
AC   O57245;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase;
DE            Short=3-beta-HSD;
DE   Includes:
DE     RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase;
DE              EC=1.1.1.145;
DE     AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase;
DE     AltName: Full=Progesterone reductase;
DE   Includes:
DE     RecName: Full=Steroid Delta-isomerase;
DE              EC=5.3.3.1;
DE     AltName: Full=Delta-5-3-ketosteroid isomerase;
GN   OrderedLocusNames=MVA157L, ACAM3000_MVA_157;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the
CC       oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the
CC       oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system
CC       plays a crucial role in the biosynthesis of all classes of hormonal
CC       steroids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-
CC         steroid + H(+) + NADH; Xref=Rhea:RHEA:24076, ChEBI:CHEBI:1722,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:47907, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.145;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid;
CC         Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909;
CC         EC=5.3.3.1;
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR   EMBL; U94848; AAB96479.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10555.1; -; Genomic_DNA.
DR   PIR; T37430; T37430.
DR   SMR; O57245; -.
DR   UniPathway; UPA00062; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; Genome.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102294; F:cholesterol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004769; F:steroid delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Isomerase; Multifunctional enzyme; NAD; Oxidoreductase; Steroidogenesis.
FT   CHAIN           1..346
FT                   /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT                   isomerase"
FT                   /id="PRO_0000087793"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  39397 MW;  8A5F09E596B98C7E CRC64;
     MAVYAVTGGA GFLGRYIVKL LISADDVQEI RVIDIVEDPQ PITSKVKVIN YIQCDINDFD
     KVREALDGVN LIIHTAALVD VFGKYTDNEI MKVNYYGTQT ILAACVDLGI KYLIYTSSME
     AIGPNKHGDP FIGHEHTLYD ISPGHVYAKS KRMAEQLVMK ANNSVIMNGA KLYTCCLRPT
     GIYGEGDKLM KVFYEQCKQH GNIMYRTVDD NAVHSRVYVG NAAWMHVLAA KYIQYPGSEI
     KGNAYFCYDY SPSCSYDMFN LLLMKPLGIE QGSRIPRWML KMYACKNDMK RILFRKPSLL
     NNYTLKISNT TFEVRTNNAE LDFNYSPIFN VDVAFERTRK WLEESE