ID   GSTA2_CHICK             Reviewed;         222 AA.
AC   Q08393;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=Class-alpha;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Tam M.F., Liu L.-F.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 30-222.
RC   TISSUE=Liver;
RX   PubMed=8241281; DOI=10.1016/0167-4781(93)90168-d;
RA   Liu L.-F., Wu S.-H., Tam M.F.;
RT   "Nucleotide sequence of class-alpha glutathione S-transferases from chicken
RT   liver.";
RL   Biochim. Biophys. Acta 1216:332-334(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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
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DR   EMBL; L15387; AAA16573.2; -; mRNA.
DR   PIR; S43432; S43432.
DR   RefSeq; NP_001001776.1; NM_001001776.1.
DR   RefSeq; XP_015140310.1; XM_015284824.1.
DR   RefSeq; XP_015140311.1; XM_015284825.1.
DR   AlphaFoldDB; Q08393; -.
DR   SMR; Q08393; -.
DR   STRING; 9031.ENSGALP00000026289; -.
DR   PaxDb; Q08393; -.
DR   Ensembl; ENSGALT00000026339; ENSGALP00000026289; ENSGALG00000016328.
DR   Ensembl; ENSGALT00000050370; ENSGALP00000058071; ENSGALG00000016328.
DR   Ensembl; ENSGALT00000065509; ENSGALP00000053994; ENSGALG00000016328.
DR   GeneID; 414895; -.
DR   KEGG; gga:414895; -.
DR   CTD; 2939; -.
DR   VEuPathDB; HostDB:geneid_414895; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000167375; -.
DR   HOGENOM; CLU_039475_4_0_1; -.
DR   InParanoid; Q08393; -.
DR   OMA; HYTCGRG; -.
DR   OrthoDB; 1162336at2759; -.
DR   PhylomeDB; Q08393; -.
DR   TreeFam; TF105321; -.
DR   Reactome; R-GGA-156590; Glutathione conjugation.
DR   PRO; PR:Q08393; -.
DR   Proteomes; UP000000539; Chromosome 3.
DR   Bgee; ENSGALG00000016328; Expressed in liver and 13 other tissues.
DR   ExpressionAtlas; Q08393; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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; IPR003080; GST_alpha.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
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; Reference proteome; Transferase.
FT   CHAIN           1..222
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185802"
FT   DOMAIN          3..83
FT                   /note="GST N-terminal"
FT   DOMAIN          85..208
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08263"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
SQ   SEQUENCE   222 AA;  25414 MW;  7B25B823051C9B8A CRC64;
     MAGKPKLHYT RGRGKMESIR WLLAAAGVEF EEEFIEKKED LEKLRNDGSL LFQQVPMVEI
     DGMKMVQSRA ILCYIAGKYN LYGKDLKERA WIDMYVEGTT DLMGMIMALP FQAADVKEKN
     IALITERATT RYFPVYEKAL KDHGQDYLVG NKLSWADIHL LEAILMTEEL KSDILSAFPL
     LQAFKGRMSN VPTIKKFLQP GSQRKPPLDE KSIANVRKIF SF