ID   A7GP49_BACCN            Unreviewed;       159 AA.
AC   A7GP49;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   02-SEP-2026, entry version 103.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   OrderedLocusNames=Bcer98_1597 {ECO:0000313|EMBL:ABS21907.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21907.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS21907.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.H., Sanchis V.,
RA   Nguen-The C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; CP000764; ABS21907.1; -; Genomic_DNA.
DR   RefSeq; WP_012094082.1; NC_009674.1.
DR   AlphaFoldDB; A7GP49; -.
DR   STRING; 315749.Bcer98_1597; -.
DR   PaxDb; 315749-Bcer98_1597; -.
DR   GeneID; 33896928; -.
DR   KEGG; bcy:Bcer98_1597; -.
DR   eggNOG; COG0386; Bacteria.
DR   HOGENOM; CLU_029507_2_2_9; -.
DR   OrthoDB; 9789406at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   FunFam; 3.40.30.10:FF:000010; Glutathione peroxidase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF78; GLUTATHIONE PEROXIDASE; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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 {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000499};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002300}.
FT   ACT_SITE        35
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   159 AA;  18236 MW;  6D9007C38D576051 CRC64;
     MTVYHFSVKT MTGEERSLRD YEGKVLLIVN VASKCGFTPQ YKGLQSLYEK YKEQGFEILG
     FPCNQFGGQE PGEEEEILNF CEMNYEVTFP LFAKIDVKGK HAHPLYQYIT KQAPGILGIK
     AVKWNFTKFL IGRDGIVMNR FAPQIKPEEL EKAIETLLL
//