3BHS_FOWPN
ID 3BHS_FOWPN Reviewed; 370 AA.
AC Q67477; Q9J5F8;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=FPV046;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FP-9 / Isolate HP-438;
RX PubMed=8077953; DOI=10.1099/0022-1317-75-9-2495;
RA Skinner M.A., Moore J.B., Binns M.M., Smith G.L., Boursnell M.E.G.;
RT "Deletion of fowlpox virus homologues of vaccinia virus genes between the 3
RT beta-hydroxysteroid dehydrogenase (A44L) and DNA ligase (A50R) genes.";
RL J. Gen. Virol. 75:2495-2498(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(2000).
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 (By similarity). {ECO:0000250}.
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; Z29716; CAA82802.1; -; Genomic_DNA.
DR EMBL; AF198100; AAF44390.1; -; Genomic_DNA.
DR PIR; S41971; S41971.
DR RefSeq; NP_039008.1; NC_002188.1.
DR SMR; Q67477; -.
DR GeneID; 1486594; -.
DR KEGG; vg:1486594; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000008597; 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; Reference proteome;
KW Steroidogenesis.
FT CHAIN 1..370
FT /note="3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-
FT isomerase"
FT /id="PRO_0000087797"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 38..43
FT /note="IRIDQW -> LDRPM (in Ref. 1; CAA82802)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="N -> K (in Ref. 1; CAA82802)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 42349 MW; 730FE72BA84FA681 CRC64;
MRTLVYVVTG GCGFLGRHII NNLILFESSL KEVRVYDIRI DQWLLDLVEK CNIIKIVPVI
GDVRNKSTLD EALRSADVVI HIASINDVAG KFTNDSIMDV NINGTKNVVD SCLYNGVRVL
VYTSSYSAVG PNFLGDAMIR GNENTYYQSN HKEAYPLSKQ LSEKYILEAN GTMSNIGLRL
CTCALRPLGV FGEYCPVLET LYRRSYKSRK MYKYADDKVF HSRVYAGNVA WMHILAARNM
IENGQHSPLC NNVYYCYDTS PTEHYHDFNM HFFNQLGMDL RNTCLPLWCL RFIANINKGL
RVLLSPICSY TPLLNPYTLI KECTTFTIET DKAFKDFGYV PLYTWEESRS KTQLWIRELE
AKSSSQKPKS
