ID A0A3B6MYZ1_WHEAT Unreviewed; 222 AA.
AC A0A3B6MYZ1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN ORFNames=CFC21_079869 {ECO:0000313|EMBL:KAF7075065.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5D02G432600.1.cds1};
RN [1] {ECO:0000313|EMBL:KAF7075065.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7075065.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5D02G432600.1.cds1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5D02G432600.1.cds1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5D02G432600.1.cds1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7075065.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7075065.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is involved in the conjugation of reduced glutathione to a
CC wide number of exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|RuleBase:RU369102}.
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 ECO:0000256|RuleBase:RU369102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU369102}.
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|RuleBase:RU369102}.
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DR EMBL; CM022225; KAF7075065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6MYZ1; -.
DR SMR; A0A3B6MYZ1; -.
DR STRING; 4565.A0A3B6MYZ1; -.
DR EnsemblPlants; TraesCS5D02G432600.1; TraesCS5D02G432600.1.cds1; TraesCS5D02G432600.
DR Gramene; TraesCAD_scaffold_076814_01G000100.1; TraesCAD_scaffold_076814_01G000100.1; TraesCAD_scaffold_076814_01G000100.
DR Gramene; TraesCLE_scaffold_216288_01G000100.1; TraesCLE_scaffold_216288_01G000100.1; TraesCLE_scaffold_216288_01G000100.
DR Gramene; TraesCS5D02G432600.1; TraesCS5D02G432600.1.cds1; TraesCS5D02G432600.
DR Gramene; TraesKAR5D01G0356110.1; cds.TraesKAR5D01G0356110.1; TraesKAR5D01G0356110.
DR Gramene; TraesPAR_scaffold_076835_01G000100.1; TraesPAR_scaffold_076835_01G000100.1; TraesPAR_scaffold_076835_01G000100.
DR Gramene; TraesROB_scaffold_201992_01G000100.1; TraesROB_scaffold_201992_01G000100.1; TraesROB_scaffold_201992_01G000100.
DR Gramene; TraesWEE_scaffold_012754_01G000500.1; TraesWEE_scaffold_012754_01G000500.1; TraesWEE_scaffold_012754_01G000500.
DR OMA; WVNACLE; -.
DR OrthoDB; 767442at2759; -.
DR Proteomes; UP000019116; Chromosome 5D.
DR Proteomes; UP000815260; Chromosome 5D.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260:SF732; GLUTATHIONE S-TRANSFERASE GSTU1-RELATED; 1.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transferase {ECO:0000256|RuleBase:RU369102}.
FT DOMAIN 5..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 91..211
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 222 AA; 25034 MW; 081979FDB5E6248F CRC64;
MAGEKGLVLL DFWVSPFGQR CRIALAEKGL PYEYVEENLM AGKSDRLLRS NPIHKKIPVL
LHDGRPVNES LIILNYLDDA FPDTPSLLPS DPYQRAQARF WADYVDKKVY DCGTRLWKLK
GEPHAQARAD MVEILKNLDG ALGDKAFFGG HAFGFVDAAF APFTSWFHSY EKYGEFSVAE
VAPKIAAWAK RCGERESVAK SLYSPDKIYE FIGVLKKMHG VE
//
