ID   GPX_MCV1                Reviewed;         220 AA.
AC   Q98234;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   29-SEP-2021, entry version 102.
DE   RecName: Full=Glutathione peroxidase;
DE            Short=GPx;
DE            Short=GSHPx;
DE            EC=1.11.1.9;
GN   Name=GPX1; OrderedLocusNames=MC066L;
OS   Molluscum contagiosum virus subtype 1 (MOCV) (MCVI).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Molluscipoxvirus.
OX   NCBI_TaxID=10280;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RX   PubMed=8670425; DOI=10.1126/science.273.5276.813;
RA   Senkevich T.G., Bugert J.J., Sisler J.R., Koonin E.V., Darai G., Moss B.;
RT   "Genome sequence of a human tumorigenic poxvirus: prediction of specific
RT   host response-evasion genes.";
RL   Science 273:813-816(1996).
CC   -!- FUNCTION: May protect the virus and component of infected cells from
CC       oxidative damage by peroxides whose formation may be stimulated by
CC       infection. {ECO:0000269|PubMed:8670425}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC   -!- PTM: During periods of oxidative stress, Sec-64 may react with a
CC       superoxide radical, irreversibly lose hydroselenide and be converted to
CC       dehydroalanine. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This enzyme has been acquitted by lateral transfer from
CC       its human host and has retained 74% identity with cellular GPX1.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; U60315; AAC55194.2; -; Genomic_DNA.
DR   PIR; T30668; T30668.
DR   RefSeq; NP_044017.2; NC_001731.1.
DR   GeneID; 1487085; -.
DR   KEGG; vg:1487085; -.
DR   Proteomes; UP000000869; Genome.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Peroxidase; Reference proteome; Selenocysteine.
FT   CHAIN           1..220
FT                   /note="Glutathione peroxidase"
FT                   /id="PRO_0000318766"
FT   ACT_SITE        64
FT                   /evidence="ECO:0000250"
FT   SITE            64
FT                   /note="Subject to oxidation and hydroselenide loss to
FT                   dehydroalanine"
FT                   /evidence="ECO:0000250"
FT   NON_STD         64
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  24218 MW;  C51FC8C2BF704247 CRC64;
     MADGSGARFP RFSELCAKYA AQLAAAETRS VYAFSARPIT GGEPVSLGFL RGRVLLIENV
     ASLUGSTVRE YTQMNELQRR LGARGLVVLG FPCNQFGHQE NAQNAEILPS LKHVRPGNGF
     EPNFMLFEKC EVNGARAHPL FAFLREALPA PSDDMSTLVS DPQLIAWSPV CRNDVAWNFE
     KFLVGADGTP VRRYSHRCQT LAVEPDIEAL LPPPARGYYA