ID   GST_LACPN               Reviewed;          50 AA.
AC   C0HLL7;
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 S-transferase {ECO:0000303|PubMed:32181246};
DE            EC=2.5.1.18 {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 S-transferase, which conjugates reduced
CC       glutathione to a wide number of exogenous and endogenous hydrophobic
CC       electrophiles. {ECO:0000269|PubMed:32181246}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000269|PubMed:32181246};
CC   -!- ACTIVITY REGULATION: Inhibited by Fe(2+) and DTT. Slightly inhibited by
CC       SDS and Zn(2+). Activity is slightly increased by Mn(2+).
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 GST superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLL7; -.
DR   SMR; C0HLL7; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   SUPFAM; SSF47616; SSF47616; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Transferase.
FT   CHAIN           1..50
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000448246"
FT   NON_TER         50
FT                   /evidence="ECO:0000303|PubMed:32181246"
SQ   SEQUENCE   50 AA;  5887 MW;  4594CD306E95B88E CRC64;
     YLFVMTNRMK LLNYSFEGLP NLKKLDEIMR QHPAVKRVLE QEGAPHTLTD