GSTO2_CAEBR
ID GSTO2_CAEBR Reviewed; 253 AA.
AC A8XT16;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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 {ECO:0000312|EMBL:CAP35619.1}; ORFNames=CBG18105;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP35619.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP35619.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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:0000255}.
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DR EMBL; HE600963; CAP35619.1; -; Genomic_DNA.
DR RefSeq; XP_002642151.1; XM_002642105.1.
DR AlphaFoldDB; A8XT16; -.
DR SMR; A8XT16; -.
DR STRING; 6238.CBG18105; -.
DR EnsemblMetazoa; CBG18105.1; CBG18105.1; WBGene00037589.
DR GeneID; 8584146; -.
DR KEGG; cbr:CBG_18105; -.
DR CTD; 8584146; -.
DR WormBase; CBG18105; CBP10756; WBGene00037589; Cbr-gsto-2.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_9_2_1; -.
DR InParanoid; A8XT16; -.
DR OMA; ESMVICE; -.
DR OrthoDB; 1225872at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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 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; IPR005442; GST_omega.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13417; GST_N_3; 1.
DR PRINTS; PR01625; GSTRNSFRASEO.
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 3: Inferred from homology;
KW Oxidoreductase; Reference proteome; Transferase.
FT CHAIN 1..253
FT /note="Probable glutathione transferase omega-2"
FT /id="PRO_0000352791"
FT DOMAIN 25..105
FT /note="GST N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 110..238
FT /note="GST C-terminal"
FT /evidence="ECO:0000255"
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 253 AA; 28451 MW; 51F08F8D028C57A5 CRC64;
MPVLAGINSK VLKNGDSEPS PPPAGIYRIY NMRFCPWAQR ALIYASVKNV PSEVINIHLK
EKPDWYFSKH YKGQVPALEL DEGKKHVIES AHIPEYLDDL FPESRILPSD PYEKVQQKLL
LERLAAVAPA FYAAAQAANN PEGRDEKYAA LVKAFEDAEK LLTGDFFSGK AKPGFADYLI
FPNYQRVFWL SHILPNSPFS SESFPGPNFP KLAKWYRTLD SIPEVAAASQ PTEMGVGFFN
DYLKGTPNYD YGL
