ID   GSTA1_CAVPO             Reviewed;         218 AA.
AC   P81706;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Glutathione S-transferase A;
DE            Short=GST A;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P08263};
DE   AltName: Full=Class-alpha;
DE   AltName: Full=GGST A1-1;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RC   STRAIN=Hartley; TISSUE=Liver;
RX   PubMed=8138540; DOI=10.1093/oxfordjournals.jbchem.a124265;
RA   Kamei-Hayashi K., Oshino R., Hara S.;
RT   "Amino acid sequence of glutathione S-transferase a from guinea pig
RT   liver.";
RL   J. Biochem. 114:835-841(1993).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=Hartley; TISSUE=Liver;
RX   PubMed=2332412; DOI=10.1093/oxfordjournals.jbchem.a122991;
RA   Oshino R., Kamei K., Nishioka M., Shin M.;
RT   "Purification and characterization of glutathione S-transferases from
RT   guinea pig liver.";
RL   J. Biochem. 107:105-110(1990).
CC   -!- FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic
CC       attack of the sulfur atom of glutathione on the electrophilic groups of
CC       a wide range of exogenous and endogenous compounds. Involved in the
CC       formation of glutathione conjugates of both prostaglandin A2 (PGA2) and
CC       prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5-
CC       androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may
CC       therefore play an important role in hormone biosynthesis. Through its
CC       glutathione-dependent peroxidase activity toward the fatty acid
CC       hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it
CC       is also involved in the metabolism of oxidized linoleic acid.
CC       {ECO:0000250|UniProtKB:P08263}.
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:0000250|UniProtKB:P08263};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
CC         glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC         glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione =
CC         (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide +
CC         H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
CC         Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
CC         Evidence={ECO:0000250|UniProtKB:P08263};
CC   -!- SUBUNIT: Homodimer or heterodimer of GSTA1 and GSTA2.
CC       {ECO:0000250|UniProtKB:P08263}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
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DR   PIR; JX0294; JX0294.
DR   AlphaFoldDB; P81706; -.
DR   SMR; P81706; -.
DR   STRING; 10141.ENSCPOP00000021161; -.
DR   iPTMnet; P81706; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   InParanoid; P81706; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF107; GLUTATHIONE S-TRANSFERASE A2; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Reference proteome;
KW   Transferase.
FT   CHAIN           1..218
FT                   /note="Glutathione S-transferase A"
FT                   /id="PRO_0000185782"
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT   DOMAIN          84..206
FT                   /note="GST C-terminal"
FT   BINDING         8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         44
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P30711"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P13745"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:8138540"
FT   MOD_RES         3
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
SQ   SEQUENCE   218 AA;  25191 MW;  ADAF1F5661B88B2F CRC64;
     SGKPVLHYFN VQGRMESIRW LLAAAGVEFE EKLIMCQEDL DKLKNDGLLM FQQVPMVEMD
     GMKMVQSRAI LNYIATKYNL YGKDTKERLL IDMYTEGMTD LYELFFKVIL APPEEKDAAK
     SLIKDRAKNR FLPAFEKVLK SHGQGYLVGN KLSKADILLT ELLYMVEEFD ASLLANFTLL
     QALKTRVSNL PNVKKFLQPG SQRKPFPTQE MFEEMRKF
//