GSTP_ONCVO
ID GSTP_ONCVO Reviewed; 208 AA.
AC P46427;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glutathione S-transferase 2;
DE EC=2.5.1.18;
DE AltName: Full=GST class-pi;
GN Name=GST2;
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Guatemala;
RX PubMed=7984170; DOI=10.1016/0166-6851(94)90030-2;
RA Salinas G., Braun G., Taylor D.W.;
RT "Molecular characterisation and localisation of an Onchocerca volvulus pi-
RT class glutathione S-transferase.";
RL Mol. Biochem. Parasitol. 66:1-9(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8050528; DOI=10.1006/expr.1994.1062;
RA Liebau E., Walter R.D., Henkle-Duehrsen K.;
RT "Onchocerca volvulus: isolation and sequence of a second glutathione S-
RT transferase cDNA.";
RL Exp. Parasitol. 79:68-71(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE, AND
RP SUBUNIT.
RX PubMed=15640152; DOI=10.1074/jbc.m413551200;
RA Perbandt M., Hoppner J., Betzel C., Walter R.D., Liebau E.;
RT "Structure of the major cytosolic glutathione S-transferase from the
RT parasitic nematode Onchocerca volvulus.";
RL J. Biol. Chem. 280:12630-12636(2005).
CC -!- FUNCTION: Appears to play a central role in the parasite detoxification
CC system.
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:15640152}.
CC -!- TISSUE SPECIFICITY: Hypodermis, wall of the seminal receptacle and
CC spermatozoa of adult worms.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR EMBL; L28771; AAA53575.1; -; mRNA.
DR EMBL; X77393; CAA54568.1; -; mRNA.
DR PIR; S41933; S41933.
DR PDB; 1TU7; X-ray; 1.50 A; A/B=1-208.
DR PDB; 1TU8; X-ray; 1.80 A; A/B/C/D=1-208.
DR PDBsum; 1TU7; -.
DR PDBsum; 1TU8; -.
DR AlphaFoldDB; P46427; -.
DR SMR; P46427; -.
DR STRING; 6282.P46427; -.
DR HOGENOM; CLU_039475_2_1_1; -.
DR BRENDA; 2.5.1.18; 4401.
DR EvolutionaryTrace; P46427; -.
DR Proteomes; UP000024404; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..208
FT /note="Glutathione S-transferase 2"
FT /id="PRO_0000185914"
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:0000305|PubMed:15640152"
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:0000305|PubMed:15640152"
FT BINDING 62..63
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000305|PubMed:15640152"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:1TU7"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1TU7"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1TU7"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1TU7"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 81..107
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1TU7"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1TU7"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1TU7"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:1TU7"
FT TURN 166..171
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:1TU7"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:1TU7"
SQ SEQUENCE 208 AA; 24232 MW; D3A76450AE7A1321 CRC64;
MSYKLTYFSI RGLAEPIRLF LVDQDIKFID DRIAKDDFSS IKSQFQFGQL PCLYDGDQQI
VQSGAILRHL ARKYNLNGEN EMETTYIDMF CEGVRDLHVK YTRMIYMAYE TEKDPYIKSI
LPGELAKFEK LLATRGNGRN LILGDKISYA DYALFEELDV HQILDPHCLD KFPLLKAFHQ
RMKDRPKLKE YCEKRDAAKV PVNGNGKQ
