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 24-JAN-2024, entry version 101.
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.P30110; -.
DR PaxDb; 4565-Traes_4BS_615DE1514-1; -.
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; IBA:GO_Central.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03187; GST_C_Phi; 1.
DR CDD; cd03053; GST_N_Phi; 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; IPR004046; GST_C.
DR InterPro; IPR034347; GST_Phi_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43900:SF76; GLUTATHIONE S-TRANSFERASE 1; 1.
DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 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
//
