ID A0A2K5EBG8_AOTNA Unreviewed; 208 AA.
AC A0A2K5EBG8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=GSTO1 {ECO:0000313|Ensembl:ENSANAP00000030509.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000030509.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000030509.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR AlphaFoldDB; A0A2K5EBG8; -.
DR Ensembl; ENSANAT00000048548.1; ENSANAP00000030509.1; ENSANAG00000033006.1.
DR GeneTree; ENSGT00940000155351; -.
DR Proteomes; UP000233020; Unplaced.
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:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd03184; GST_C_Omega; 1.
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; IPR004046; GST_C.
DR InterPro; IPR005442; GST_omega.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43968; -; 1.
DR PANTHER; PTHR43968:SF5; GLUTATHIONE S-TRANSFERASE OMEGA-1; 1.
DR Pfam; PF14497; GST_C_3; 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:UP000233020};
KW Transferase {ECO:0000256|RuleBase:RU368071}.
FT DOMAIN 22..101
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 65..197
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 208 AA; 23764 MW; CCE2922B0C6A3395 CRC64;
MSGESARSLG KGSAPPGPVP EGLIRVYSMR FCPFAERTRL VLKAKGIRHE VININLKNKP
EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLFPDDPYEK ACQKMVFELF
SKVLTKKKTT FFGGSSISMI DYLIWPWFER LEAMKLNECV DHTPKLKLWM AAMKEDPTVS
ALLTSMKDWQ GFLELYLQNS PEACDYGL
//
