ID GSTO2_CAEEL Reviewed; 254 AA.
AC P34277; Q2L6Y9; Q304F1; Q304F2; Q8I7N0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 5.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Probable glutathione transferase omega-2;
DE EC=2.5.1.18;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE EC=1.8.5.1;
DE AltName: Full=Monomethylarsonic acid reductase;
DE Short=MMA(V) reductase;
DE EC=1.20.4.2;
GN Name=gsto-2; ORFNames=C02D5.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activity.
CC Has dehydroascorbate reductase activity and may contribute to the
CC recycling of ascorbic acid. Participates in the biotransformation of
CC inorganic arsenic and reduces monomethylarsonic acid (MMA) (By
CC similarity). {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000305}.
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DR EMBL; FO080279; CCD62560.1; -; Genomic_DNA.
DR PIR; S44745; S44745.
DR RefSeq; NP_871705.3; NM_181976.3.
DR AlphaFoldDB; P34277; -.
DR SMR; P34277; -.
DR BioGRID; 57458; 3.
DR STRING; 6239.C02D5.3.2; -.
DR PaxDb; 6239-C02D5-3; -.
DR PeptideAtlas; P34277; -.
DR EnsemblMetazoa; C02D5.3.1; C02D5.3.1; WBGene00015337.
DR GeneID; 353420; -.
DR KEGG; cel:CELE_C02D5.3; -.
DR AGR; WB:WBGene00015337; -.
DR WormBase; C02D5.3; CE39555; WBGene00015337; gsto-2.
DR eggNOG; KOG0406; Eukaryota.
DR GeneTree; ENSGT00940000163896; -.
DR HOGENOM; CLU_011226_9_2_1; -.
DR InParanoid; P34277; -.
DR OMA; NMRYCPF; -.
DR OrthoDB; 103277at2759; -.
DR PhylomeDB; P34277; -.
DR Reactome; R-CEL-156590; Glutathione conjugation.
DR Reactome; R-CEL-196836; Vitamin C (ascorbate) metabolism.
DR PRO; PR:P34277; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015337; Expressed in pharyngeal muscle cell (C elegans) and 2 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; IPR005442; GST_omega.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43968; -; 1.
DR PANTHER; PTHR43968:SF12; GLUTATHIONE S-TRANSFERASE OMEGA-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR PRINTS; PR01625; GSTRNSFRASEO.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 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 3: Inferred from homology;
KW Oxidoreductase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..254
FT /note="Probable glutathione transferase omega-2"
FT /id="PRO_0000185890"
FT DOMAIN 25..105
FT /note="GST N-terminal"
FT DOMAIN 110..239
FT /note="GST C-terminal"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 62
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Y5"
FT BINDING 75
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 89..90
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Y5"
SQ SEQUENCE 254 AA; 28799 MW; C648FE7E6889CCB5 CRC64;
MSVLSGLNTK VVKNGDPAPA PPASGTIRIY NMRYCPWAQR ALIFASLKKI PTEVINIHLD
QKPDWFFTKH YKGQVPALEH DEGKKIVIES AVIPEYLDDI YPEPRIIPTD HYEKVQQKLL
LDRISGQLSS AFYGVVQAAK ISDLLKEKLV ELAKAYDTAE ELLTGDFYSG TSKPGFVDYL
IYPNIQRAFW TSHIIKDFPL KVESFPGPNY PKLSKWYKRL DSIPEVIATS QPTETAVEFF
KSWIIGAPNF DYGL
//
