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GSTF1_WHEAT
ID   GSTF1_WHEAT             Reviewed;         229 AA.
AC   P30110;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Glutathione S-transferase 1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-phi;
GN   Name=GSTA1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Cheyenne;
RX   PubMed=1799693; DOI=10.1094/mpmi-4-014;
RA   Dudler R., Hertig C., Rebmann G., Bull J., Mauch F.;
RT   "A pathogen-induced wheat gene encodes a protein homologous to glutathione-
RT   S-transferases.";
RL   Mol. Plant Microbe Interact. 4:14-18(1991).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
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   -!- INDUCTION: By pathogen infection.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR   EMBL; X56012; CAA39487.1; -; Genomic_DNA.
DR   PIR; T06509; T06509.
DR   AlphaFoldDB; P30110; -.
DR   SMR; P30110; -.
DR   STRING; 4565.Traes_4BS_615DE1514.1; -.
DR   PRIDE; P30110; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   BRENDA; 2.5.1.18; 6500.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P30110; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043295; F:glutathione binding; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   CDD; cd03187; GST_C_Phi; 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; IPR004046; GST_C.
DR   InterPro; IPR034347; GST_Phi_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
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   2: Evidence at transcript level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..229
FT                   /note="Glutathione S-transferase 1"
FT                   /id="PRO_0000185858"
FT   DOMAIN          2..83
FT                   /note="GST N-terminal"
FT   DOMAIN          93..223
FT                   /note="GST C-terminal"
FT   BINDING         41..42
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   VARIANT         34
FT                   /note="M -> V"
FT   VARIANT         171
FT                   /note="T -> S (in strain: cv. Fidel)"
FT   VARIANT         195
FT                   /note="D -> E (in strain: cv. Fidel)"
FT   VARIANT         226
FT                   /note="G -> R (in strain: cv. Fidel)"
SQ   SEQUENCE   229 AA;  25828 MW;  C6A2543D53678570 CRC64;
     MSPVKVFGHP MLTNVARVLL FLEEVGAEYE LVPMDFVAGE HKRPQHVQLN PFAKMPGFQD
     GDLVLFESRA IAKYILRKYG GTAGLDLLGE NSGIEELAMV DVWTEVEAQQ YYPAISPVVF
     ECIIIPFIIP GGGAAPNQTV VDESLERLRG VLGIYEARLE KSRYLAGDSI TFADLNHIPF
     TFYFMTTPYA KVFDDYPKVK AWWEMLMARP AVQRVCKHMP TEFKLGAQY
 
 
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