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   27-MAR-2024, entry version 84.
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.A8XT16; -.
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; MWPWCER; -.
DR   OrthoDB; 103277at2759; -.
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   CDD; cd03055; GST_N_Omega; 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; 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; 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; 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
//