GST26_FASHE
ID GST26_FASHE Reviewed; 218 AA.
AC P30112;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme 51;
DE Short=GST51;
DE EC=2.5.1.18;
DE AltName: Full=Fh51;
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 [MRNA] OF 10-218.
RX PubMed=7682383; DOI=10.4269/ajtmh.1993.48.457;
RA Muro A., Rodriguez-Medina J.R., Hillyer G.V.;
RT "Sequence analysis of a Fasciola hepatica glutathione S-transferase cDNA
RT clone.";
RL Am. J. Trop. Med. Hyg. 48:457-463(1993).
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; M77682; AAA29141.1; -; mRNA.
DR PIR; A48388; A48388.
DR PDB; 2WRT; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-218.
DR PDBsum; 2WRT; -.
DR AlphaFoldDB; P30112; -.
DR SMR; P30112; -.
DR EvolutionaryTrace; P30112; -.
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 /evidence="ECO:0000250"
FT CHAIN 2..218
FT /note="Glutathione S-transferase class-mu 26 kDa isozyme
FT 51"
FT /id="PRO_0000185807"
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 84
FT /note="T -> S (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="N -> D (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="P -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2WRT"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2WRT"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:2WRT"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2WRT"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:2WRT"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2WRT"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2WRT"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:2WRT"
FT HELIX 86..110
FT /evidence="ECO:0007829|PDB:2WRT"
FT HELIX 115..137
FT /evidence="ECO:0007829|PDB:2WRT"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2WRT"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:2WRT"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2WRT"
FT TURN 167..172
FT /evidence="ECO:0007829|PDB:2WRT"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:2WRT"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:2WRT"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2WRT"
SQ SEQUENCE 218 AA; 25373 MW; DF8A826E056A2196 CRC64;
MPAKLGYWKI RGLQQPVRLL LEYLGEEYEE HLYGRDDREK WFGDKFNMGL DLPNLPYYID
DKCKLTQSVA IMRYIADKHG MLGTTPEERA RISMIEGAAM DLRMGFVRVC YNPKFEEVKG
DYLKELPTTL KMWSNFLGDR HYLTGSPVSH VDFMVYEALD CIRYLAPQCL EDFPKLKEFK
SRIEDLPKIK AYMESEKFIK WPLNSWIASF GGGDAAPA
