ID   GSTF1_ARATH             Reviewed;         218 AA.
AC   P42769;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Glutathione S-transferase PM239X14;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-phi;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX   PubMed=8375395; DOI=10.1111/j.1432-1033.1993.tb18177.x;
RA   Bartling D., Radzio R., Steiner U., Weiler E.W.;
RT   "A glutathione S-transferase with glutathione-peroxidase activity from
RT   Arabidopsis thaliana. Molecular cloning and functional characterization.";
RL   Eur. J. Biochem. 216:579-586(1993).
RN   [2]
RP   ERRATUM OF PUBMED:8375395.
RA   Bartling D., Radzio R., Steiner U., Weiler E.W.;
RL   Eur. J. Biochem. 218:1096-1096(1993).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12090627; DOI=10.1023/a:1015557300450;
RA   Wagner U., Edwards R., Dixon D.P., Mauch F.;
RT   "Probing the diversity of the Arabidopsis glutathione S-transferase gene
RT   family.";
RL   Plant Mol. Biol. 49:515-532(2002).
CC   -!- FUNCTION: Specifically catalyzes the conjugation of synthetic 1-chloro-
CC       2,4-ditrobenzene to GSH. Also functions as a glutathione peroxidase,
CC       converting linoleate oxidation products into their corresponding
CC       hydroxyacids. This enzyme may thus serve to protect the cell from
CC       oxygen toxicity as well as from exogenous toxins such as herbicides.
CC       {ECO:0000269|PubMed:8375395}.
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, cytosol {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in vegetative rosettes.
CC   -!- DEVELOPMENTAL STAGE: Expressed up until the first flowering buds, after
CC       which, levels dramatically decrease.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
CC   -!- CAUTION: This protein probably does not originate from A.thaliana,
CC       rather it resembles fungal GTSs. {ECO:0000305}.
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DR   EMBL; X68304; CAA48376.1; -; mRNA.
DR   PIR; S36835; S36835.
DR   AlphaFoldDB; P42769; -.
DR   SMR; P42769; -.
DR   ExpressionAtlas; P42769; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009407; P:toxin catabolic process; 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:SF98; GLUTATHIONE S-TRANSFERASE 2; 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; SFLDG01154; Main.5:_Phi-like; 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   Cytoplasm; Detoxification; Oxidoreductase; Peroxidase; Stress response;
KW   Transferase.
FT   CHAIN           1..218
FT                   /note="Glutathione S-transferase PM239X14"
FT                   /id="PRO_0000185849"
FT   DOMAIN          2..85
FT                   /note="GST N-terminal"
FT   DOMAIN          93..218
FT                   /note="GST C-terminal"
FT   BINDING         12..13
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..42
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         55..56
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..70
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   218 AA;  24364 MW;  C7E6B6EC5320C33A CRC64;
     MVTVKLYGMA YSTCTKRVYT TAKEIGVDVK IVPVDLMKGE HKEPAYLDNY HPFGVIPVLE
     DEDGTKIYES RAISRYLVAK YGKGSSLLPS PSDPKAYGLF EQAASVEYSS FDPPASSLAY
     ERVFAGMRGL KTNEELAKKY VDTLNAKMDG YERILSKQKY LAGNDFTLAD LFHLPYGAMV
     AQLEPTVLDS KPHVKAWWAA SLRVIPGRLL RNSSKEFM
//