GST1_ONCVO
ID GST1_ONCVO Reviewed; 235 AA.
AC P46434;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Glutathione S-transferase 1;
DE EC=2.5.1.18;
DE Flags: Fragment;
GN Name=GST1; Synonyms=GSTA;
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].
RX PubMed=8008026; DOI=10.1016/0166-6851(94)90067-1;
RA Liebau E., Walter R.D., Henkle-Duehrsen K.;
RT "Isolation, sequence and expression of an Onchocerca volvulus glutathione
RT S-transferase cDNA.";
RL Mol. Biochem. Parasitol. 63:305-309(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-235 IN COMPLEX WITH
RP GLUTATHIONE, AND SUBUNIT.
RX PubMed=18258257; DOI=10.1016/j.jmb.2008.01.029;
RA Perbandt M., Hoppner J., Burmeister C., Luersen K., Betzel C., Liebau E.;
RT "Structure of the extracellular glutathione S-transferase OvGST1 from the
RT human pathogenic parasite Onchocerca volvulus.";
RL J. Mol. Biol. 377:501-511(2008).
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:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; X75029; CAA52937.1; -; mRNA.
DR PDB; 2HNL; X-ray; 2.00 A; A/B=11-235.
DR PDBsum; 2HNL; -.
DR AlphaFoldDB; P46434; -.
DR SMR; P46434; -.
DR STRING; 6282.P46434; -.
DR HOGENOM; CLU_039475_1_2_1; -.
DR EvolutionaryTrace; P46434; -.
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; 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; Reference proteome; Transferase.
FT CHAIN <1..235
FT /note="Glutathione S-transferase 1"
FT /id="PRO_0000185969"
FT DOMAIN 36..113
FT /note="GST N-terminal"
FT DOMAIN 115..235
FT /note="GST C-terminal"
FT BINDING 42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18258257"
FT BINDING 73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18258257"
FT BINDING 77
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18258257"
FT BINDING 85
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18258257"
FT BINDING 97..98
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT NON_TER 1
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:2HNL"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2HNL"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2HNL"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2HNL"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 116..141
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:2HNL"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:2HNL"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:2HNL"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:2HNL"
SQ SEQUENCE 235 AA; 26838 MW; F28928E44102F63A CRC64;
FITMNFVVEA ASSNANQAIT SENSIKPKGK LQPQMEKYTL TYFNGRGRAE VIRLLFALAN
VSYEDNRITR DEWKYLKPRT PFGHVPMLNV SGNVLGESHA IELLLGGRFG LLGTNDWEEA
KIMAVVLNID ELFQKLIPWT HEKNTTKKAE LFRNLSESDV MPFLGRYEKF LKESTTGHIV
GNKVSVADLT VFNMLMTLDD EVKLEEYPQL ASFVNKIGQM PGIKEWIKKR PKTYF
