ID O04941_AEGTA Unreviewed; 230 AA.
AC O04941;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
OS Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=37682 {ECO:0000313|EMBL:AAD10129.1};
RN [1] {ECO:0000313|EMBL:AAD10129.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9276955; DOI=10.1104/pp.114.4.1461;
RA Riechers D.E., Irzyk G.P., Jones S.S., Fuerst E.P.;
RT "Partial characterization of glutathione S-transferases from wheat
RT (Triticum spp.) and purification of a safener-induced glutathione S-
RT transferase from Triticum tauschii.";
RL Plant Physiol. 114:1461-1470(1997).
RN [2] {ECO:0000313|EMBL:AAD10129.1}
RP NUCLEOTIDE SEQUENCE.
RA Riechers D.E., Irzyk G.P., Fuerst E.P., Jones S.S.;
RT "Nucleotide sequence of a cDNA encoding a safener-induced glutathione S-
RT transferase (Accession No. AF004358) from Triticum tauschii L. (PGR97-
RT 110).";
RL Plant Physiol. 114:1568-1568(1997).
RN [3] {ECO:0000313|EMBL:AAD10129.1}
RP NUCLEOTIDE SEQUENCE.
RA Riechers D.E., Kleinhofs A., Irzyk G.P., Jones S.S.;
RT "Chromosomal location and expression of a herbicide safener-regulated
RT glutathione S-transferase gene in Triticum aestivum and linkage relations
RT in Hordeum vulgare.";
RL Genome 41:368-372(1998).
RN [4] {ECO:0007829|PDB:1GWC}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH S-HEXYLGLUTATHIONE.
RX PubMed=12033934; DOI=10.1021/bi015964x;
RA Thom R., Cummins I., Dixon D.P., Edwards R., Cole D.J., Lapthorn A.J.;
RT "Structure of a tau class glutathione S-transferase from wheat active in
RT herbicide detoxification.";
RL Biochemistry 41:7008-7020(2002).
RN [5] {ECO:0000313|EMBL:AAM89393.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12226515; DOI=10.1104/pp.004796;
RA Xu F., Lagudah E.S., Moose S.P., Riechers D.E.;
RT "Tandemly duplicated Safener-induced glutathione S-transferase genes from
RT Triticum tauschii contribute to genome- and organ-specific expression in
RT hexaploid wheat.";
RL Plant Physiol. 130:362-373(2002).
RN [6] {ECO:0000313|EnsemblPlants:EMT06693}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2016) to UniProtKB.
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:0000256|ARBA:ARBA00000710};
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|RuleBase:RU003494}.
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DR EMBL; AF004358; AAD10129.1; -; mRNA.
DR EMBL; AY013753; AAM89393.1; -; Genomic_DNA.
DR PDB; 1GWC; X-ray; 2.25 A; A/B/C=1-230.
DR PDBsum; 1GWC; -.
DR AlphaFoldDB; O04941; -.
DR SMR; O04941; -.
DR EnsemblPlants; EMT06693; EMT06693; F775_30353.
DR OMA; ITHAMAN; -.
DR EvolutionaryTrace; O04941; -.
DR ExpressionAtlas; O04941; baseline.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03185; GST_C_Tau; 1.
DR CDD; cd03058; GST_N_Tau; 1.
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; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR PANTHER; PTHR11260:SF530; GLUTATHIONE TRANSFERASE; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 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 3D-structure {ECO:0007829|PDB:1GWC};
KW Transferase {ECO:0000313|EMBL:AAD10129.1}.
FT DOMAIN 5..84
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 91..228
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 230 AA; 24829 MW; B23994B740595D22 CRC64;
MAGGDDLKLL GAWPSPFVTR VKLALALKGL SYEDVEEDLY KKSELLLKSN PVHKKIPVLI
HNGAPVCESM IILQYIDEVF ASTGPSLLPA DPYERAIARF WVAYVDDKLV APWRQWLRGK
TEEEKSEGKK QAFAAVGVLE GALRECSKGG GFFGGDGVGL VDVALGGVLS WMKVTEALSG
DKIFDAAKTP LLAAWVERFI ELDAAKAALP DVGRLLEFAK AREAAAAASK
//
