ID   Q0H8U8_TRISP            Unreviewed;       205 AA.
AC   Q0H8U8;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU368105};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU368105};
DE   AltName: Full=GST class-pi {ECO:0000256|RuleBase:RU368105};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:ABA42914.1};
RN   [1] {ECO:0000313|EMBL:ABA42914.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ISS 534 {ECO:0000313|EMBL:ABA42914.1};
RA   Bahuon C., Blaga R., Fu B., Le Guerhier F., Le Rhun D., Le Naour E.,
RA   Cozma V., Liu M., Boireau P.;
RT   "Molecular cloning and identification of glutathione S-transferase from
RT   Trichinella spp.";
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.
CC       {ECO:0000256|RuleBase:RU368105}.
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:0000256|RuleBase:RU368105};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU368105}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Pi family.
CC       {ECO:0000256|ARBA:ARBA00007297, ECO:0000256|RuleBase:RU368105}.
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DR   EMBL; DQ159094; ABA42914.1; -; mRNA.
DR   AlphaFoldDB; Q0H8U8; -.
DR   SMR; Q0H8U8; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1050.130; -; 1.
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; IPR003082; GST_pi.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF141; GLUTATHIONE S-TRANSFERASE P; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01268; GSTRNSFRASEP.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 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   Transferase {ECO:0000256|RuleBase:RU368105, ECO:0000313|EMBL:ABA42914.1}.
FT   DOMAIN          2..79
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          80..199
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   205 AA;  23977 MW;  768B8F32D09B39BE CRC64;
     MPLYKLVYFP IRGLAEPIRL LLHDQRVEFL DNRIQQKDWP EIKSQMLFGQ VPCLYEDDQP
     IVQSGAIMRH LGRRFGLYGN AEEMTYVDQI YEGVVDLRLK YARLIYSDSF HESKGKFINE
     VLPDELAKFE KILTGKKYIL DDEITFADYA LAELLDVLLI LSSSCLENFT ALTIYHSRFM
     NRPNLKRYLS SDIRKNAKIN GNENK
//