GSTP_DIRIM
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 03-AUG-2022, entry version 77.
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 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; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
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 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