ID   GPO_LACLA               Reviewed;         157 AA.
AC   Q9CFV1;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Glutathione peroxidase;
DE            EC=1.11.1.9;
GN   Name=gpo; OrderedLocusNames=LL1364; ORFNames=L0198;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK05462.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005176; AAK05462.1; ALT_INIT; Genomic_DNA.
DR   PIR; D86795; D86795.
DR   RefSeq; NP_267520.2; NC_002662.1.
DR   RefSeq; WP_010905907.1; NC_002662.1.
DR   AlphaFoldDB; Q9CFV1; -.
DR   SMR; Q9CFV1; -.
DR   STRING; 272623.L0198; -.
DR   PeroxiBase; 3753; LllGPx01_IL1403.
DR   PaxDb; Q9CFV1; -.
DR   EnsemblBacteria; AAK05462; AAK05462; L0198.
DR   KEGG; lla:L0198; -.
DR   PATRIC; fig|272623.7.peg.1470; -.
DR   eggNOG; COG0386; Bacteria.
DR   HOGENOM; CLU_029507_4_0_9; -.
DR   OMA; FPMMSKI; -.
DR   Proteomes; UP000002196; Chromosome.
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   InterPro; IPR013766; Thioredoxin_domain.
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.
FT   CHAIN           1..157
FT                   /note="Glutathione peroxidase"
FT                   /id="PRO_0000066661"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  18024 MW;  2D049998339E9CE2 CRC64;
     MNFYDFSAFK MNGETVSMSD FKGKVVIVVN TASKCGFTPQ FEGLEKLYEN YKDQGLEILG
     FPCNQFVNQD AGENSEINEF CQLNYGVTFP MFQKIKVNGK EAHPLYQFLK KEAKGALSGT
     IKWNFTKFLI DREGNVIERF APKTEPKEME EEIQKLL