ID   GSTE_PSEUF              Reviewed;          24 AA.
AC   P82997;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   Flags: Fragment;
OS   Pseudomonas sp. (strain CF600).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=79676 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11900268; DOI=10.1016/s0923-2508(01)01293-1;
RA   Santos P.M., Mignogna G., Heipieper H.J., Zennaro E.;
RT   "Occurrence and properties of glutathione S-transferases in phenol-
RT   degrading Pseudomonas strains.";
RL   Res. Microbiol. 153:89-98(2002).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000269|PubMed:11900268}.
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:11900268};
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:11900268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11900268}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P82997; -.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; NAS:UniProtKB.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Transferase.
FT   CHAIN           1..>24
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185978"
FT   NON_TER         24
FT                   /evidence="ECO:0000303|PubMed:11900268"
SQ   SEQUENCE   24 AA;  2756 MW;  7C6BBA2B3C9C32BA CRC64;
     MLKLHGFSVS NYYNMVKLAL LEKG