ID   GSTA_PLEPL              Reviewed;         225 AA.
AC   P30568;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Glutathione S-transferase A;
DE            Short=GST-A;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta;
OS   Pleuronectes platessa (European plaice).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC   Pleuronectes.
OX   NCBI_TaxID=8262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8503846; DOI=10.1042/bj2920189;
RA   Leaver M.J., Scott K., George S.G.;
RT   "Cloning and characterization of the major hepatic glutathione S-
RT   transferase from a marine teleost flatfish, the plaice (Pleuronectes
RT   platessa), with structural similarities to plant, insect and mammalian
RT   Theta class isoenzymes.";
RL   Biochem. J. 292:189-195(1993).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Found in all the tissues examined. Highest values
CC       found in liver and in intestinal mucosa.
CC   -!- INDUCTION: By epoxides and by antioxidants.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; X63761; CAA45293.1; -; mRNA.
DR   PIR; S33308; S33308.
DR   AlphaFoldDB; P30568; -.
DR   SMR; P30568; -.
DR   PRIDE; P30568; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Transferase.
FT   CHAIN           1..225
FT                   /note="Glutathione S-transferase A"
FT                   /id="PRO_0000185946"
FT   DOMAIN          3..85
FT                   /note="GST N-terminal"
FT   DOMAIN          92..217
FT                   /note="GST C-terminal"
FT   BINDING         18
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        140
FT                   /note="L -> V (in Ref. 1; figure 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143..144
FT                   /note="EL -> DV (in Ref. 1; figure 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147..148
FT                   /note="WE -> SQ (in Ref. 1; figure 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   225 AA;  25724 MW;  37899602D07C077F CRC64;
     MAKDMTLLWG SGSPPCWRVM IVLEEKNLQA YNSKLLSFEK GEHKSAEVMS MNPRGQLPSF
     KHGSKVLNES YAACMYLESQ FKSQGNKLIP DCPAEQAMMY QRMFEGLTLA QKMADVIYYS
     WKVPEAERHD SAVKRNKENL STELKLWEEY LQKTSGSFVA GKSFSLADVS VFPGVAYLFR
     FGLTEERYPQ LTAYYNSLKE RPSIKASWPP TWLESPQGQD MLKDV