ID   GPO_LACLM               Reviewed;         157 AA.
AC   O32770; A2RK72;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Glutathione peroxidase;
DE            EC=1.11.1.9;
GN   Name=gpo; OrderedLocusNames=llmg_1088;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9721272; DOI=10.1128/jb.180.17.4380-4386.1998;
RA   Martinussen J., Hammer K.;
RT   "The carB gene encoding the large subunit of carbamoylphosphate synthetase
RT   from Lactococcus lactis is transcribed monocistronically.";
RL   J. Bacteriol. 180:4380-4386(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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}.
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DR   EMBL; AJ000109; CAA03927.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97682.1; -; Genomic_DNA.
DR   RefSeq; WP_011834996.1; NZ_WJVF01000012.1.
DR   AlphaFoldDB; O32770; -.
DR   SMR; O32770; -.
DR   STRING; 416870.llmg_1088; -.
DR   PeroxiBase; 3754; LlcGPx01_MG1363.
DR   EnsemblBacteria; CAL97682; CAL97682; llmg_1088.
DR   GeneID; 61109649; -.
DR   KEGG; llm:llmg_1088; -.
DR   eggNOG; COG0386; Bacteria.
DR   HOGENOM; CLU_029507_4_0_9; -.
DR   OMA; FPMMSKI; -.
DR   PhylomeDB; O32770; -.
DR   BioCyc; LLAC416870:LLMG_RS05525-MON; -.
DR   Proteomes; UP000000364; 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.
FT   CHAIN           1..157
FT                   /note="Glutathione peroxidase"
FT                   /id="PRO_0000066662"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  17970 MW;  AD6C53806E03C7E9 CRC64;
     MNFYDFSAVK MNGETVSMSD YKGKVVIVVN TASKCGFTPQ FEGLEKLYET YKDQGLEILG
     FPCNQFANQD AGENTEINEF CQLNYGVTFT MFQKIKVNGK EAHPLYQFLK KEAKGALSGT
     IKWNFTKFLI DRDGQVIERF APKTEPEEME EEIKKLL