ID   GSTF_SILVU              Reviewed;         217 AA.
AC   Q04522;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-phi;
GN   Name=GST;
OS   Silene vulgaris (Bladder campion) (Silene cucubalus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Sileneae; Silene;
OC   Silene subgen. Behenantha; Silene sect. Behenantha.
OX   NCBI_TaxID=42043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-40; 124-141 AND
RP   146-153.
RX   PubMed=16668960; DOI=10.1104/pp.99.2.789;
RA   Kutchan T.M., Hochberger A.;
RT   "Nucleotide sequence of a cDNA encoding a constitutively expressed
RT   glutathione-S-transferase from cell suspension cultures of Silene
RT   cucubalus.";
RL   Plant Physiol. 99:789-790(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16669104; DOI=10.1104/pp.99.4.1729;
RA   Praendl R., Kutchan T.M.;
RT   "Nucleotide sequence of the gene for a glutathione-S-transferase from cell
RT   suspension cultures of Silene cucubalus.";
RL   Plant Physiol. 99:1729-1731(1992).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR   EMBL; M84968; AAA33930.1; -; mRNA.
DR   EMBL; M84969; AAA33931.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q04522; -.
DR   SMR; Q04522; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
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:SF47; GLUTATHIONE S-TRANSFERASE F6-RELATED; 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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:16668960"
FT   CHAIN           2..217
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185855"
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT   DOMAIN          91..217
FT                   /note="GST C-terminal"
FT   BINDING         11
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  24599 MW;  51ABE9DA2FE23D67 CRC64;
     MTIKVHGNPR STATQRVLVA LYEKHLEFEF VPIDMGAGGH KQPSYLALNP FGQVPALEDG
     EIKLFESRAI TKYLAYTHDH QNEGTSLIHK EKHEMAAQLV WEEVEAHQFD PVASKLAWEL
     VFKGIFGMQT DTTVVEENEA KLAKVLDVYE ARLTESEYLG ANDSFTLVDL HHLPLLGYLM
     GTQVKKLFEE RAHVSAWCKK ILARPSWEKT LALQKQA
//