ID   GST_PLAVI               Reviewed;         205 AA.
AC   Q0ZS46;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Glutathione S-transferase {ECO:0000303|Ref.1};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:Q8ILQ7};
GN   Name=GST {ECO:0000303|Ref.1};
OS   Plasmodium vivax.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX   NCBI_TaxID=5855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Na B.-K., Kong Y., Kim T.-S.;
RT   "Identification and characterization of glutathione S-transferase from
RT   Plasmodium vivax.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; DQ156544; ABA40394.1; -; mRNA.
DR   RefSeq; XP_001616766.1; XM_001616716.1.
DR   AlphaFoldDB; Q0ZS46; -.
DR   SMR; Q0ZS46; -.
DR   GeneID; 5476074; -.
DR   KEGG; pvx:PVX_085515; -.
DR   VEuPathDB; PlasmoDB:PVP01_1329600; -.
DR   VEuPathDB; PlasmoDB:PVX_085515; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   HOGENOM; CLU_039475_1_0_1; -.
DR   OMA; TVYNVFM; -.
DR   BRENDA; 2.5.1.18; 4894.
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; 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   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           1..205
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000259968"
FT   DOMAIN          3..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          89..205
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000255"
FT   BINDING         58..59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ILQ7"
FT   BINDING         71..72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ILQ7"
FT   BINDING         105
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q8ILQ7"
FT   BINDING         117
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"
SQ   SEQUENCE   205 AA;  24212 MW;  EF4AA17C428624FA CRC64;
     MAEEIVLYYF DARGKAELIR LIFAYLGIQY TDKRFGENGD AFIEFKNFKK EKETPFNQVP
     ILEMDNIIFA QSQAIVRYLS KKYKISGNSE LNEFYADMIF CGVQDIHYKF NNTNLFKQNE
     TTFLNEELPK WSGYFENILK KNNCNYFVGD DLTYADLAVF NLYDDIETKY PNSLKNFPLL
     KAHNEFISNL PNIKNYISNR KESVY