GSTZ_EUPES
ID GSTZ_EUPES Reviewed; 225 AA.
AC P57108; Q9M4Q6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Glutathione S-transferase zeta class;
DE EC=2.5.1.18;
OS Euphorbia esula (Leafy spurge).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Euphorbioideae; Euphorbieae;
OC Euphorbia; Euphorbia subgen. Esula; Euphorbia sect. Esula.
OX NCBI_TaxID=3993;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Underground adventitious buds;
RA Anderson J.V., Horvath D.P.;
RT "Identification of mRNAs expressed in underground adventitious buds of
RT Euphorbia esula (leafy spurge).";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF263737; AAF72197.1; -; mRNA.
DR AlphaFoldDB; P57108; -.
DR SMR; P57108; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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; IPR004046; GST_C.
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; PF14497; GST_C_3; 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 TIGRFAMs; TIGR01262; maiA; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Transferase.
FT CHAIN 1..225
FT /note="Glutathione S-transferase zeta class"
FT /id="PRO_0000186033"
FT DOMAIN 10..91
FT /note="GST N-terminal"
FT DOMAIN 96..221
FT /note="GST C-terminal"
FT BINDING 20..25
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 75..76
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 119..121
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 225 AA; 25348 MW; 50D171F9FF346F32 CRC64;
MASVEQPNKP KLKLYSYFRS SCSFRVRIAL NLKGLDYEYV PVNLLKGEQF TPEFLKINPI
GYVPALVDGE DVISDSFAIL MYLEEKYPEH PILPADIHKK AINYQAANIV SSSIQPLQNL
AVLNFIGEKV SPDEKVPWVQ RHISKGFAAL EKLLQGHAGR FATGDEVYLA DLFLEPQIHA
AITRFNVDMT QFPLLLRLHE AYSQLPEFQN AMPDKQPDST SPTAS