GST29_FASHE
ID GST29_FASHE Reviewed; 221 AA.
AC P56598;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme 1;
DE Short=GST1;
DE EC=2.5.1.18;
DE AltName: Full=Fh1;
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 23-221.
RA Crameri S.;
RL Patent number WO9008819, 09-AUG-1990.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 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 -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; A00993; CAA00118.1; -; Unassigned_RNA.
DR PDB; 2FHE; X-ray; 2.30 A; A/B=2-216.
DR PDBsum; 2FHE; -.
DR AlphaFoldDB; P56598; -.
DR SMR; P56598; -.
DR BRENDA; 2.5.1.18; 2230.
DR EvolutionaryTrace; P56598; -.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IEA:UniProt.
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; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
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; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..221
FT /note="Glutathione S-transferase class-mu 26 kDa isozyme 1"
FT /id="PRO_0000185810"
FT DOMAIN 2..82
FT /note="GST N-terminal"
FT DOMAIN 84..202
FT /note="GST C-terminal"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9367777,
FT ECO:0007744|PDB:2FHE"
FT BINDING 40..44
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9367777,
FT ECO:0007744|PDB:2FHE"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9367777,
FT ECO:0007744|PDB:2FHE"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:9367777,
FT ECO:0007744|PDB:2FHE"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 23
FT /note="Y -> V (in Ref. 3; CAA00118)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..112
FT /note="DP -> VS (in Ref. 3; CAA00118)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> P (in Ref. 3; CAA00118)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2FHE"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2FHE"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:2FHE"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2FHE"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:2FHE"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2FHE"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:2FHE"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:2FHE"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:2FHE"
FT HELIX 85..109
FT /evidence="ECO:0007829|PDB:2FHE"
FT HELIX 114..136
FT /evidence="ECO:0007829|PDB:2FHE"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2FHE"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:2FHE"
FT TURN 166..171
FT /evidence="ECO:0007829|PDB:2FHE"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:2FHE"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:2FHE"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2FHE"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2FHE"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:2FHE"
SQ SEQUENCE 221 AA; 25730 MW; 17EAF460F750895F CRC64;
MPAKLGYWKI RGLQQPVRLL LEYGEKYEEQ IYERDDGEKW FSKKFELGLD LPNLPYYIDD
KCKLTQSLAI LRYIADKHGM IGSTPEERAR VSMIEGAAVD LRQGLSRISY DPKFEQLKEG
YLKDLPTTMK MWSDFLGKNP YLRGTSVSHV DFMVYEALDA IRYLEPHCLD HFPNLQQFMS
RIEALPSIKA YMESNRFIKW PLNGWHAQFG GGDAPPSHEK K
