GSTA1_ANTST
ID GSTA1_ANTST Reviewed; 221 AA.
AC P80894;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glutathione S-transferase;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P08263};
DE AltName: Full=GST class-alpha;
DE Contains:
DE RecName: Full=Glutathione S-transferase, N-terminally processed;
OS Antechinus stuartii (Brown marsupial mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Antechinus.
OX NCBI_TaxID=9283;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX PubMed=9109421; DOI=10.1016/s0014-5793(97)00281-0;
RA Bolton R.M., Curstedt L., Cederlund E., Hjelmqvist L., Mannervik B.,
RA Ahokas J.T., Joernvall H.;
RT "Characterization of a marsupial glutathione transferase, a class Alpha
RT enzyme from Brown Antechinus (Antechinus stuartii).";
RL FEBS Lett. 406:216-219(1997).
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P80894; -.
DR SMR; P80894; -.
DR iPTMnet; P80894; -.
DR PRIDE; P80894; -.
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 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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Transferase.
FT CHAIN 1..221
FT /note="Glutathione S-transferase"
FT /id="PRO_0000185803"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT CHAIN 2..221
FT /note="Glutathione S-transferase, N-terminally processed"
FT /id="PRO_0000421784"
FT DOMAIN 3..82
FT /note="GST N-terminal"
FT DOMAIN 84..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 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-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:9109421"
FT MOD_RES 2
FT /note="N-acetylalanine; in Glutathione S-transferase, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P30115"
SQ SEQUENCE 221 AA; 25534 MW; 03B185BCC44B570F CRC64;
MAGEQNIKYF NIKGRMEAIR WLLAVAGVEF EEKFFETKEQ LQKLKETVLL FQQVPMVEID
GMKLVQTRAI LHYIAEKYNL LGKDMKEHAQ IIMYSEGTMD LMELIMIYPF LKGEEKKQRL
VEIANKAKGR YFPAFENVLK THGQNFLVGN QLSMADVQLF EAILMVEEKV PDALSGFPLL
QAFKTRISNI PTVKTFLAPG SKRKPVPDAK YVEDIIKIFY F
