ID   GPX_LACPN               Reviewed;          49 AA.
AC   C0HLL8;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Glutathione peroxidase {ECO:0000303|PubMed:32181246};
DE            EC=1.11.1.9 {ECO:0000269|PubMed:32181246};
DE   Flags: Fragment;
OS   Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1590 {ECO:0000303|PubMed:32181246};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=KU720558 {ECO:0000303|PubMed:32181246};
RX   PubMed=32181246; DOI=10.3389/fbioe.2020.00078;
RA   Al-Madboly L.A., Ali S.M., Fakharany E.M.E., Ragab A.E., Khedr E.G.,
RA   Elokely K.M.;
RT   "Stress-Based Production, and Characterization of Glutathione Peroxidase
RT   and Glutathione S-Transferase Enzymes From Lactobacillus plantarum.";
RL   Front. Bioeng. Biotechnol. 8:78-78(2020).
CC   -!- FUNCTION: Glutathione peroxidase which may protect the cell from
CC       oxidative damage. {ECO:0000269|PubMed:32181246}.
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         Evidence={ECO:0000269|PubMed:32181246};
CC   -!- ACTIVITY REGULATION: Inhibited by Cu(2+), SDS and DTT. Activity is
CC       slightly increased by Fe(2+), Mn(2+), triton X-100 and EDTA.
CC       {ECO:0000269|PubMed:32181246}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6. {ECO:0000269|PubMed:32181246};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:32181246};
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HLL8; -.
DR   SMR; C0HLL8; -.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase.
FT   CHAIN           1..49
FT                   /note="Glutathione peroxidase"
FT                   /id="PRO_0000448247"
FT   NON_TER         49
FT                   /evidence="ECO:0000303|PubMed:32181246"
SQ   SEQUENCE   49 AA;  5579 MW;  7A699E29D2A4302F CRC64;
     TELSGAPLDL YQYRGQVLLI PQFTGLLYQK SQQEGDVVDG LPSHQFHQY