GST27_FASHE
ID GST27_FASHE Reviewed; 218 AA.
AC P31670;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme 47;
DE Short=GST47;
DE EC=2.5.1.18;
DE AltName: Full=Fh47;
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 OF 8-106.
RA Crameri S.;
RL Patent number WO9008819, 09-AUG-1990.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND
RP SUBUNIT.
RX PubMed=9367777; DOI=10.1006/jmbi.1997.1338;
RA Rossjohn J., Feil S.C., Wilce M.C.J., Sexton J.L., Spithill T.W.,
RA Parker M.W.;
RT "Crystallization, structural determination and analysis of a novel parasite
RT vaccine candidate: Fasciola hepatica glutathione S-transferase.";
RL J. Mol. Biol. 273:857-872(1997).
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. {ECO:0000269|PubMed:9367777}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; M77681; AAA29140.1; -; mRNA.
DR EMBL; A00996; CAA00121.1; -; Unassigned_RNA.
DR PDB; 1FHE; X-ray; 3.00 A; A=2-218.
DR PDBsum; 1FHE; -.
DR AlphaFoldDB; P31670; -.
DR SMR; P31670; -.
DR EvolutionaryTrace; P31670; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..218
FT /note="Glutathione S-transferase class-mu 26 kDa isozyme
FT 47"
FT /id="PRO_0000185808"
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:0000269|PubMed:9367777,
FT ECO:0007744|PDB:1FHE"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9367777,
FT ECO:0007744|PDB:1FHE"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9367777,
FT ECO:0007744|PDB:1FHE"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 66
FT /note="T -> I (in Ref. 3; CAA00121)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..106
FT /note="RIGF -> FEEL (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1FHE"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:1FHE"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1FHE"
FT TURN 43..47
FT /evidence="ECO:0007829|PDB:1FHE"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1FHE"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1FHE"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 86..107
FT /evidence="ECO:0007829|PDB:1FHE"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:1FHE"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1FHE"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:1FHE"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:1FHE"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:1FHE"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1FHE"
SQ SEQUENCE 218 AA; 25412 MW; 3FF8B667232663B3 CRC64;
MPAKLGYWKL RGLAQPVRLF LEYLGEEYEE HLYGRDDREK WMSEKFNMGL DLPNLPYYID
DKCKLTQSVA IMRYIADKHG MLGTTPEERA RISMIEGAAM DLRIGFGRVC YNPKFEEVKE
EYVKELPKTL KMWSDFLGDR HYLTGSSVSH VDFMLYETLD SIRYLAPHCL DEFPKLKEFK
SRIEALPKIK AYMESKRFIK WPLNGWAASF GAGDAPPS
