ID   GST_PLAYO               Reviewed;         209 AA.
AC   Q7REH6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Glutathione S-transferase {ECO:0000250|UniProtKB:Q8ILQ7};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:Q8ILQ7};
GN   Name=GST {ECO:0000250|UniProtKB:Q8ILQ7}; ORFNames=PY05088;
OS   Plasmodium yoelii yoelii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=73239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17XNL;
RX   PubMed=12368865; DOI=10.1038/nature01099;
RA   Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA   Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA   Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA   Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA   Shoaibi A., Cummings L.M., Florens L., Yates J.R. III, Raine J.D.,
RA   Sinden R.E., Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W.,
RA   Vaidya A.B., van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA   Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA   Carucci D.J.;
RT   "Genome sequence and comparative analysis of the model rodent malaria
RT   parasite Plasmodium yoelii yoelii.";
RL   Nature 419:512-519(2002).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. May also function
CC       as a storage protein or ligandin for parasitotoxic ferriprotoporphyrin
CC       IX (hemin). {ECO:0000250|UniProtKB:Q8ILQ7}.
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         Evidence={ECO:0000250|UniProtKB:Q8ILQ7};
CC   -!- SUBUNIT: Homodimer. In the absence of ligands two homodimers may
CC       interact to form a tetramer. {ECO:0000250|UniProtKB:Q8ILQ7}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; AABL01001592; EAA17054.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7REH6; -.
DR   SMR; Q7REH6; -.
DR   STRING; 73239.Q7REH6; -.
DR   ChEMBL; CHEMBL1741263; -.
DR   EnsemblProtists; EAA17054; EAA17054; EAA17054.
DR   InParanoid; Q7REH6; -.
DR   OMA; TVYNVFM; -.
DR   BRENDA; 2.5.1.18; 4895.
DR   PRO; PR:Q7REH6; -.
DR   Proteomes; UP000008553; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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; 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   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..209
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000259969"
FT   DOMAIN          7..91
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          93..209
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255"
FT   BINDING         62..63
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ILQ7"
FT   BINDING         75..76
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ILQ7"
FT   BINDING         109
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ILQ7"
FT   BINDING         121
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ILQ7"
FT   BINDING         125
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ILQ7"
SQ   SEQUENCE   209 AA;  24693 MW;  A4A7FAB3AC69CF6D CRC64;
     MTYLYNFFFF FFFFFSRGKA ELIRLIFAYL QVKYTDIRFG VNGDAFAEFN NFKKEKEIPF
     NQVPILEIGG LILAQSQAIV RYLSKKYNIS GNGELNEFYA DMIFCGVQDI HYKFNNTNLF
     KQNETTFLNE ELPKWSGYFE KLLQKNNTNY FVGDTITYAD LAVFNLYDDI ESKYPNCLKN
     FPLLKAHIEL ISNIPNIKHY IANRKESVY