GSTZ_WHEAT
ID GSTZ_WHEAT Reviewed; 213 AA.
AC O04437;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glutathione S-transferase;
DE EC=2.5.1.18;
DE AltName: Full=GST class-zeta;
GN Name=GSTZ1;
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 / MRNA], AND CHARACTERIZATION.
RC STRAIN=cv. Arthur71, and cv. Oasis;
RX PubMed=10542338; DOI=10.1016/s0167-4781(99)00176-1;
RA Subramaniam K., Ye Z., Buechley G., Shaner G., Solomos T., Ueng P.P.;
RT "Isolation of a zeta class wheat glutathione S-transferase gene.";
RL Biochim. Biophys. Acta 1447:348-356(1999).
CC -!- FUNCTION: Has a glutathione transferase activity with ethacrynic acid
CC and nitrophenyl acetate. Has low glutathione peroxidase activity with
CC cumene hydroperoxide.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR EMBL; AF002211; AAB60886.1; -; mRNA.
DR EMBL; AF109714; AAD09190.1; -; Genomic_DNA.
DR PIR; T06333; T06333.
DR AlphaFoldDB; O04437; -.
DR SMR; O04437; -.
DR STRING; 4565.Traes_5AL_72929F651.1; -.
DR eggNOG; KOG0868; Eukaryota.
DR BRENDA; 2.5.1.18; 6500.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; O04437; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0016034; F:maleylacetoacetate isomerase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03191; GST_C_Zeta; 1.
DR CDD; cd03042; GST_N_Zeta; 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; IPR005955; GST_Zeta.
DR InterPro; IPR034330; GST_Zeta_C.
DR InterPro; IPR034333; GST_Zeta_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01262; maiA; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..213
FT /note="Glutathione S-transferase"
FT /id="PRO_0000186034"
FT DOMAIN 4..81
FT /note="GST N-terminal"
FT DOMAIN 86..211
FT /note="GST C-terminal"
SQ SEQUENCE 213 AA; 23752 MW; CA235D0AC66F0A54 CRC64;
MATAKPILYG AWISSCSHRV RIALNLKGVD YEYKAVNPRT DPDYEKINPI KYIPALVDGD
FVLSDSLAIM LYLEDKYPQH PLVPKDIKTK GLDLQIANIV CSSIQPLQGY GVIGLHEGRL
SPDESLEVVQ RYIDKGFRAI EKLLDGCDSK YCVGDEVHLG DVCLAPQIHA AINRFQIDMT
KYPILSRLHD AYMKIPAFQA ALPQNQPDAP SAK