ID B6T033_MAIZE Unreviewed; 238 AA.
AC B6T033;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN Name=541850 {ECO:0000313|EnsemblPlants:Zm00001eb021600_P001};
GN ORFNames=ZEAMMB73_Zm00001d029699 {ECO:0000313|EMBL:ONL99382.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACG30466.1};
RN [1] {ECO:0000313|EMBL:ACG30466.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [2] {ECO:0000313|EMBL:ONL99382.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb021600_P001,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONL99382.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb021600_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb021600_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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; EU958348; ACG30466.1; -; mRNA.
DR EMBL; CM007647; ONL99382.1; -; Genomic_DNA.
DR RefSeq; NP_001306693.1; NM_001319764.1.
DR AlphaFoldDB; B6T033; -.
DR SMR; B6T033; -.
DR IntAct; B6T033; 1.
DR STRING; 4577.B6T033; -.
DR PaxDb; 4577-GRMZM2G025190_P01; -.
DR EnsemblPlants; Zm00001eb021600_T001; Zm00001eb021600_P001; Zm00001eb021600.
DR GeneID; 541850; -.
DR Gramene; Zm00001eb021600_T001; Zm00001eb021600_P001; Zm00001eb021600.
DR KEGG; zma:541850; -.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_0_1; -.
DR InParanoid; B6T033; -.
DR OMA; WIQMVER; -.
DR OrthoDB; 397381at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; B6T033; baseline and differential.
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; 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; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR PANTHER; PTHR11260:SF801; GLUTATHIONE TRANSFERASE; 1.
DR Pfam; PF13410; GST_C_2; 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 Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B6T033};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW Transferase {ECO:0000256|RuleBase:RU369102, ECO:0000313|EMBL:ACG30466.1}.
FT DOMAIN 5..84
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 91..223
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 238 AA; 25679 MW; E83D7F6B93A2D86A CRC64;
MAGGDDLKLL GLWASPYVLR VKLALSLKGL SYENVEEDLR DKSELLLKSN PVHQKVPVLI
HGGKPICESQ VILQYIDEAF AGTGPSLLPA DPYERAVARF WAAYIDDKML PAWNQSTMGK
TEEERAEGKK QSVVTVETLE GALRDCGGQG KPFFGGDSVG YVDVVLGGLL GWVRASEELH
GVRPFDPERT PLLAAWSERF GALDAVQTVM PDVGRLLEFG KALMARLAAA AAAGASNN
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