ID   GSTZ1_DIACA             Reviewed;         221 AA.
AC   P28342;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   24-JAN-2024, entry version 98.
DE   RecName: Full=Glutathione S-transferase 1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-zeta;
DE   AltName: Full=SR8;
GN   Name=GST1; Synonyms=CARSR8;
OS   Dianthus caryophyllus (Carnation) (Clove pink).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX   NCBI_TaxID=3570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. White Sim; TISSUE=Petal;
RX   PubMed=1863781; DOI=10.1007/bf00039505;
RA   Meyer R.C. Jr., Goldsbrough P.B., Woodson W.R.;
RT   "An ethylene-responsive flower senescence-related gene from carnation
RT   encodes a protein homologous to glutathione S-transferases.";
RL   Plant Mol. Biol. 17:277-281(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. White Sim; TISSUE=Petal;
RX   PubMed=8499618; DOI=10.1007/bf00038994;
RA   Itzhaki H., Woodson W.R.;
RT   "Characterization of an ethylene-responsive glutathione S-transferase gene
RT   cluster in carnation.";
RL   Plant Mol. Biol. 22:43-58(1993).
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   -!- DEVELOPMENTAL STAGE: Senescing flowers.
CC   -!- INDUCTION: Accumulates in response to the phytohormone ethylene.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000305}.
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DR   EMBL; M64268; AAA33277.1; -; mRNA.
DR   EMBL; X58390; CAA41279.1; -; mRNA.
DR   EMBL; L05915; AAA72320.1; -; Genomic_DNA.
DR   PIR; S16604; S16604.
DR   PIR; S33628; S33628.
DR   AlphaFoldDB; P28342; -.
DR   SMR; P28342; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009072; P:aromatic amino acid 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   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; IPR005955; GST_Zeta.
DR   InterPro; IPR034330; GST_Zeta_C.
DR   InterPro; IPR034333; GST_Zeta_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01262; maiA; 1.
DR   PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR   PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF13409; GST_N_2; 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   Transferase.
FT   CHAIN           1..221
FT                   /note="Glutathione S-transferase 1"
FT                   /id="PRO_0000186031"
FT   DOMAIN          7..88
FT                   /note="GST N-terminal"
FT   DOMAIN          93..221
FT                   /note="GST C-terminal"
FT   BINDING         17..22
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..118
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        187
FT                   /note="Missing (in Ref. 2; AAA72320)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   221 AA;  24930 MW;  13D03D0D4C8B3072 CRC64;
     MSSSETQKMQ LYSFSLSSCA WRVRIALHLK GLDFEYKAVD LFKGEHLTPE FLKLNPLGYV
     PVLVHGDIVI ADSLAIIMYL EEKFPENPLL PQDLQKRALN YQAANIVTSN IQPLQNLAVL
     NYIEEKLGSD EKLSWAKHHI KKGFSALEKL LKGHAGKYAT GDEVGLADLF LAPQIIASIT
     GFGMDMAEFP LLKSLNDAYL KYQHFRMRCQ RISPMLDEAK S
//