ID   GSTF_BRAOT              Reviewed;          76 AA.
AC   P48438;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-phi;
DE   Flags: Fragments;
OS   Brassica oleracea var. italica (Broccoli).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=36774;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8142481; DOI=10.1016/0167-4838(94)90088-4;
RA   Lopez M.F., Patton W.F., Sawlivich W.B., Erdjument-Bromage H., Barry P.,
RA   Gmyrek K., Hines T., Tempst P., Skea W.M.;
RT   "A glutathione S-transferase (GST) isozyme from broccoli with significant
RT   sequence homology to the mammalian theta-class of GSTs.";
RL   Biochim. Biophys. Acta 1205:29-38(1994).
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. Theta family.
CC       {ECO:0000305}.
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DR   PIR; S43401; S43401.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 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   CHAIN           <1..>76
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185840"
FT   DOMAIN          <1..40
FT                   /note="GST N-terminal"
FT   DOMAIN          41..>76
FT                   /note="GST C-terminal"
FT   NON_CONS        40..41
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         76
SQ   SEQUENCE   76 AA;  8268 MW;  F62C58C6AD3543E7 CRC64;
     XVAFETVPVD LMKGEHKQPA YLALQPFGTV PAVVDGDYXL LSAVLDVYEA HLHGYLAGDF
     VSLADLAHLP FTDYLV