ID   Q945W8_ORYSJ            Unreviewed;       177 AA.
AC   Q945W8;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:AAK98538.1};
RN   [1] {ECO:0000313|EMBL:AAK98538.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:AAK98538.1};
RX   PubMed=15069639; DOI=10.1007/s00438-004-1006-8;
RA   Soranzo N., Sari Gorla M., Mizzi L., De Toma G., Frova C.;
RT   "Organisation and structural evolution of the rice glutathione S-
RT   transferase gene family.";
RL   Mol. Genet. Genomics 271:511-521(2004).
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|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; AF402797; AAK98538.1; -; mRNA.
DR   AlphaFoldDB; Q945W8; -.
DR   SMR; Q945W8; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03058; GST_N_Tau; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260:SF326; GLUTATHIONE S-TRANSFERASE GSTU6-RELATED; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW   Transferase {ECO:0000256|RuleBase:RU369102, ECO:0000313|EMBL:AAK98538.1}.
FT   DOMAIN          5..84
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   REGION          140..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   177 AA;  19018 MW;  E9ACB01AE4D26C5D CRC64;
     MAGDGELKLL GMWTSAFVLR VRFVLNLKSL PYEFVEENLG DKSDLLLASN PVNKTVPVLL
     HAGRPVNESQ VILQYIDEAW PDRPPAVLPS DPYERAVARF WAAYVDDKVR LAWLGILFRR
     TEEERAAAVA QADAALETLR ARSGSAPGGS PSSAATASGS STSCSAATSG GSRRSRS
//