ID H0XFC9_OTOGA Unreviewed; 243 AA.
AC H0XFC9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Glutathione S-transferase omega {ECO:0000256|RuleBase:RU368071};
DE Short=GSTO {ECO:0000256|RuleBase:RU368071};
DE EC=1.20.4.2 {ECO:0000256|RuleBase:RU368071};
DE EC=1.8.5.1 {ECO:0000256|RuleBase:RU368071};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU368071};
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase {ECO:0000256|RuleBase:RU368071};
DE AltName: Full=Monomethylarsonic acid reductase {ECO:0000256|RuleBase:RU368071};
GN Name=GSTO2 {ECO:0000313|Ensembl:ENSOGAP00000014710.2};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000014710.2, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000014710.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activity.
CC Has high 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).
CC {ECO:0000256|RuleBase:RU368071}.
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 Evidence={ECO:0000256|ARBA:ARBA00001437,
CC ECO:0000256|RuleBase:RU368071};
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 Evidence={ECO:0000256|ARBA:ARBA00000509,
CC ECO:0000256|RuleBase:RU368071};
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 Evidence={ECO:0000256|ARBA:ARBA00000710,
CC ECO:0000256|RuleBase:RU368071};
CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000256|ARBA:ARBA00011067, ECO:0000256|RuleBase:RU368071}.
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; AAQR03047034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03047035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03047036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003787238.1; XM_003787190.2.
DR AlphaFoldDB; H0XFC9; -.
DR STRING; 30611.ENSOGAP00000014710; -.
DR Ensembl; ENSOGAT00000016440.2; ENSOGAP00000014710.2; ENSOGAG00000016437.2.
DR GeneID; 100952495; -.
DR KEGG; oga:100952495; -.
DR CTD; 119391; -.
DR eggNOG; KOG0406; Eukaryota.
DR GeneTree; ENSGT00940000162030; -.
DR HOGENOM; CLU_011226_9_2_1; -.
DR InParanoid; H0XFC9; -.
DR OMA; PDADIHP; -.
DR OrthoDB; 103277at2759; -.
DR TreeFam; TF105325; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IEA:Ensembl.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
DR CDD; cd03184; GST_C_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:SF4; GLUTATHIONE S-TRANSFERASE OMEGA-2; 1.
DR Pfam; PF13409; GST_N_2; 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 {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU368071};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Transferase {ECO:0000256|RuleBase:RU368071}.
FT DOMAIN 22..101
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 106..236
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 243 AA; 28131 MW; 89E549E2852970F5 CRC64;
MAGDATKALE KGSCPPGPVP EGLIRVYSMR FCPFSHRTRL VLRAKGIRHE IININLRNKP
EWYYTKHPFG RIPVLENSRC QLIYESIVAC EYLDDAYPGR KLFPNDPYER ARQKMLLELF
CKVPQLTKEC LVALRYGRDC TNLKVALRQE FCNLEEILDY QNTCFFGGDC ISMIDYLLWP
WFERLDVYGI ADCVSHTPAL RLWIAAMKQD PVVCALLLEK SVFQGYLSLY FQNNPSAFDY
GLC
//
