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 27-MAR-2024, entry version 90. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd03192; GST_C_Sigma_like; 1. DR CDD; cd03039; GST_N_Sigma_like; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. 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 PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF224; HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE; 1. DR Pfam; PF14497; GST_C_3; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDG01205; AMPS.1; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 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 //