ID F7ANP0_XENTR Unreviewed; 234 AA.
AC F7ANP0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 70.
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=LOC100498493 {ECO:0000313|Ensembl:ENSXETP00000036868};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000036868};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000036868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000036868};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000036868}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) 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; F7ANP0; -.
DR PaxDb; 8364-ENSXETP00000027815; -.
DR Ensembl; ENSXETT00000036868; ENSXETP00000036868; ENSXETG00000016907.
DR AGR; Xenbase:XB-GENE-5824069; -.
DR Xenbase; XB-GENE-5824069; LOC100498493.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_9_2_1; -.
DR TreeFam; TF105325; -.
DR Bgee; ENSXETG00000016907; Expressed in testis.
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 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:SF6; GLUTATHIONE S-TRANSFERASE OMEGA; 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 Transferase {ECO:0000256|RuleBase:RU368071}.
FT DOMAIN 16..95
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 100..218
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 234 AA; 26601 MW; B2B47D9DB4F11224 CRC64;
LGSPTCSPAP GPVPDGLIRA YLMRFCPFAQ RAQLVLIARE INYEVVYVNT LNKPDWFFEK
SPFGLVPAIE TSEGQLIYES LIVCDYLDEV SPGKKLTPED PFQKAQQRML LEHFFKNLVF
KILGALKNNA DTSALKAEFL KKLILFDEIV SKLNTPYVGG SSVSMADYMM WPIFERFSIF
GVKDCLEKTP HLHQWYQLML QDPAVKATFT KPEVQEGFFK LYLQGIPEAV DYGI
//
