GSTA1_CHICK
ID GSTA1_CHICK Reviewed; 221 AA.
AC Q08392;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Glutathione S-transferase;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P08263};
DE AltName: Full=GST 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;
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: 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 -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; L15386; AAA16572.1; -; mRNA.
DR PIR; S43431; S43431.
DR RefSeq; NP_001001777.1; NM_001001777.1.
DR AlphaFoldDB; Q08392; -.
DR SMR; Q08392; -.
DR STRING; 9031.ENSGALP00000026286; -.
DR PaxDb; Q08392; -.
DR Ensembl; ENSGALT00000026336; ENSGALP00000026286; ENSGALG00000016325.
DR GeneID; 414896; -.
DR KEGG; gga:414896; -.
DR CTD; 2940; -.
DR VEuPathDB; HostDB:geneid_414896; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000154526; -.
DR HOGENOM; CLU_039475_4_0_1; -.
DR InParanoid; Q08392; -.
DR OMA; HLVEMIY; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q08392; -.
DR TreeFam; TF105321; -.
DR Reactome; R-GGA-156590; Glutathione conjugation.
DR Reactome; R-GGA-189483; Heme degradation.
DR Reactome; R-GGA-9748787; Azathioprine ADME.
DR SABIO-RK; Q08392; -.
DR PRO; PR:Q08392; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000016325; Expressed in colon and 11 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
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; 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 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 Reference proteome; Transferase.
FT CHAIN 1..221
FT /note="Glutathione S-transferase"
FT /id="PRO_0000185801"
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:P13745"
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 221 AA; 25299 MW; A6FB936D0E998C90 CRC64;
MSGKPVLHYA NTRGRMESVR WLLAAAGVEF EEKFLEKKED LQKLKSDGSL LFQQVPMVEI
DGMKMVQTRA ILNYIAGKYN LYGKDLKERA LIDMYVEGLA DLYELIMMNV VQPADKKEEH
LANALDKAAN RYFPVFEKVL KDHGHDFLVG NKLSRADVHL LETILAVEES KPDALAKFPL
LQSFKARTSN IPNIKKFLQP GSQRKPRLEE KDIPRLMAIF H
