ID I3MKX6_ICTTR Unreviewed; 241 AA.
AC I3MKX6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:ENSSTOP00000012004.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000012004.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000012004.2}
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; AGTP01072606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005333641.1; XM_005333584.2.
DR AlphaFoldDB; I3MKX6; -.
DR STRING; 43179.ENSSTOP00000012004; -.
DR Ensembl; ENSSTOT00000013397.3; ENSSTOP00000012004.2; ENSSTOG00000013401.3.
DR GeneID; 101962781; -.
DR CTD; 9446; -.
DR eggNOG; KOG0406; Eukaryota.
DR GeneTree; ENSGT00940000155351; -.
DR HOGENOM; CLU_011226_9_2_1; -.
DR InParanoid; I3MKX6; -.
DR OMA; ADHYSHR; -.
DR OrthoDB; 103277at2759; -.
DR TreeFam; TF105325; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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: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:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0042178; P:xenobiotic catabolic process; IEA:Ensembl.
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; IPR045073; Omega/Tau-like.
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; PF13417; GST_N_3; 1.
DR PRINTS; PR01625; GSTRNSFRASEO.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU368071};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Transferase {ECO:0000256|RuleBase:RU368071}.
FT DOMAIN 22..101
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 106..228
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT COILED 136..163
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 241 AA; 27305 MW; 05A5A3587FF263E6 CRC64;
MSGGSAKSLA KGSAPPGPVP EGLIRLYSMR FCPFAQRTRL VLKAKGIEHE IININLRNKP
EWYFKKNPLG LVPVLENSQG QLISESTITC EYLDEAYPGK KLLPDDPYEK ACQKMVFELF
SKVPSLMANF IKGQNKENWS GLKEELKKEF SKLEEVLTNK ETTFFGGNSV SMIDYLIWPW
FERLEAVELN ECVAHTPKLK LWIAAMKKDP TVSALLHDVK THQGFLGLYL QNSLEAFDYG
L
//