ID   GST28_FASHE             Reviewed;         218 AA.
AC   P31671;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme 7;
DE            Short=GST7;
DE            EC=2.5.1.18;
DE   AltName: Full=Fh7;
OS   Fasciola hepatica (Liver fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC   Fasciola.
OX   NCBI_TaxID=6192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1740183; DOI=10.1016/0014-4894(92)90051-b;
RA   Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W.;
RT   "Molecular characterization of cDNA sequences encoding glutathione S-
RT   transferases of Fasciola hepatica.";
RL   Exp. Parasitol. 74:232-237(1992).
RN   [2]
RP   ERRATUM OF PUBMED:1740183.
RX   PubMed=8224094; DOI=10.1006/expr.1993.1097;
RA   Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W.;
RL   Exp. Parasitol. 77:385-385(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-218.
RA   Crameri S.;
RL   Patent number WO9008819, 09-AUG-1990.
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC   -!- FUNCTION: GST isoenzymes appear to play a central role in the parasite
CC       detoxification system. Other functions are also suspected including a
CC       role in increasing the solubility of haematin in the parasite gut.
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.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR   EMBL; M77680; AAA29139.1; -; mRNA.
DR   EMBL; A00994; CAA00119.1; -; Unassigned_RNA.
DR   AlphaFoldDB; P31671; -.
DR   SMR; P31671; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..218
FT                   /note="Glutathione S-transferase class-mu 26 kDa isozyme 7"
FT                   /id="PRO_0000185809"
FT   DOMAIN          2..83
FT                   /note="GST N-terminal"
FT   DOMAIN          85..203
FT                   /note="GST C-terminal"
FT   BINDING         7..8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         41..45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        36..43
FT                   /note="NDREKWLG -> MIGRNGWA (in Ref. 3; CAA00119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189..197
FT                   /note="IKEYMKSER -> SRYMSRA (in Ref. 3; CAA00119)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   218 AA;  25327 MW;  30D9EC6CDE6D592E CRC64;
     MPAKLGYWKI RGLQQPVRLF LEYLGEEYEE HLYGRNDREK WLGDKFNMGL DLPNLPYYID
     DKCKLTQSVA IMRYIADKHG MLGSTPEERA RISMIEGAAM DLRIGFGLTC YNPKFEELKG
     DYLKGLPTTL KMWSDFLGDR QYLIGSSVSH VDFMVYEALD CIRYLAPQCL DDFPKLKEFK
     SRIEDLPKIK EYMKSERFIK WPLHSWTSPF GGGDAPPA