ID   GSTP_DIRIM              Reviewed;         208 AA.
AC   P46426;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-pi;
OS   Dirofilaria immitis (Canine heartworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Dirofilaria.
OX   NCBI_TaxID=6287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   James E.R., McLean D.C., Venkatakrishnaiah L.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR   EMBL; U14753; AAA21585.1; -; mRNA.
DR   AlphaFoldDB; P46426; -.
DR   SMR; P46426; -.
DR   ChEMBL; CHEMBL2366475; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03076; GST_N_Pi; 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; 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; SFLDS00019; Glutathione_Transferase_(cytos; 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.
FT   CHAIN           1..208
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185913"
FT   DOMAIN          1..78
FT                   /note="GST N-terminal"
FT   DOMAIN          80..200
FT                   /note="GST C-terminal"
FT   BINDING         7
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         42
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         49..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         62..63
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
SQ   SEQUENCE   208 AA;  24146 MW;  698510856385AE6B CRC64;
     MSYKLTYFPI RGLAEPIRLL LVDQGIKFTD EHIPKDDFVS IKSQFQFGQL PCFYDGDQQI
     VQSGAILRHL ARKFNLNGEN NAETSYVDMF YEGIRDLHSK YTRMIYEAYE TQKDPFIKNI
     LPQELAKLEK LLATRDNGKN FILGDKISFA DYVLFEELDV QQILDPHCLE KFPLLKAFHQ
     RLGDKPKIKE YCAKRNASKM PVNGNGKQ
//