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Database: UniProt
Entry: I3MKX6_ICTTR
LinkDB: I3MKX6_ICTTR
Original site: I3MKX6_ICTTR 
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}.
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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
//
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