ID   3BHS_VACCC              Reviewed;         346 AA.
AC   P21097;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   02-SEP-2026, entry version 118.
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   Name=OPG174; ORFNames=A44L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
CC   -!- FUNCTION: Catalyzes the oxidative conversion of Delta(5)-ene-3-beta-
CC       hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-
CC       beta-HSD enzymatic system plays a crucial role in the biosynthesis of
CC       all classes of hormonal steroids. During viral infection, steroid
CC       production contributes to virulence by inhibiting the host inflammatory
CC       response. {ECO:0000250|UniProtKB:P26670}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3beta-hydroxy-Delta(5)-steroid + NAD(+) = a 3-oxo-Delta(5)-
CC         steroid + NADH + H(+); 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         Evidence={ECO:0000250|UniProtKB:P26670};
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; Evidence={ECO:0000250|UniProtKB:P26670};
CC   -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC       {ECO:0000250|UniProtKB:P26670}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD 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   EMBL; M35027; AAA48175.1; -; Genomic_DNA.
DR   PIR; A42522; WMVZ1W.
DR   SMR; P21097; -.
DR   UniPathway; UPA00062; -.
DR   GO; GO:0003854; F:3-beta-hydroxy-Delta5-steroid dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0004769; F:steroid Delta-isomerase activity; ISS:UniProtKB.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0052031; P:symbiont-mediated perturbation of host defense response; IEA:UniProtKB-KW.
DR   FunFam; 3.40.50.720:FF:000495; 3 hydroxysteroid dehydrogenase, putative; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR050177; Lipid_A_modif_metabolic_enz.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43245; BIFUNCTIONAL POLYMYXIN RESISTANCE PROTEIN ARNA; 1.
DR   PANTHER; PTHR43245:SF51; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY 42E, MEMBER 2; 1.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Early protein; Host-virus interaction; Isomerase; Multifunctional enzyme;
KW   NAD; Oxidoreductase; Steroidogenesis; Viral immunoevasion.
FT   CHAIN           1..346
FT                   /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT                   isomerase"
FT                   /id="PRO_0000087794"
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;  39366 MW;  F308D8BC9C811469 CRC64;
     MAVYAVTGGA GFLGRYIVKL LISADDVQEI RVIDIVEDPQ PITSKVKVIN YIQCDINDFD
     KVREALDGVN LIIHTAALVD VFGKYTDNEI MKVNYYGTQT ILAACVDLGI KYLIYTSSME
     AIGPNKHGDP FIGHEHTLYD ISPGHVYAKS KRMAEQLVMK ANNSVIMNGA KLYTCCLRPT
     GIYGEGDKLT KVFYEQCKQH GNIMYRTVDD NAVHSRVYVG NAAWMHVLAA KYIQYPGSKI
     KGNAYFCYDY SPSCSYDMFN LLLMKPLGIE QGSRIPRWML KMYACKNDMK RILFRKPSLL
     NNYTLKISNT TFEVRTNNAE LDFNYSPIFD VDVAFKRTRK WLEESE
//