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Database: UniProt/TrEMBL
Entry: H2NBJ0_PONAB
LinkDB: H2NBJ0_PONAB
Original site: H2NBJ0_PONAB 
ID   H2NBJ0_PONAB            Unreviewed;       209 AA.
AC   H2NBJ0; A0A2J8XYT5; A0A2J8XYU7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   24-JAN-2024, entry version 57.
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   ORFNames=CR201_G0023626 {ECO:0000313|EMBL:PNJ87196.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000003065.2, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000003065.2, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ87196.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ87196.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000003065.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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; NDHI03003286; PNJ87196.1; -; Genomic_DNA.
DR   STRING; 9601.ENSPPYP00000003065; -.
DR   Ensembl; ENSPPYT00000003169.2; ENSPPYP00000003065.2; ENSPPYG00000033066.1.
DR   eggNOG; KOG0406; Eukaryota.
DR   GeneTree; ENSGT00940000162030; -.
DR   HOGENOM; CLU_011226_9_2_1; -.
DR   OMA; YESAIAX; -.
DR   OrthoDB; 103277at2759; -.
DR   TreeFam; TF105325; -.
DR   Proteomes; UP000001595; Chromosome 10.
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   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; PF13417; GST_N_3; 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:UP000001595};
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   209 AA;  24471 MW;  1A9B55D33D8BEEEA CRC64;
     MSEDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE VVNINLRNKP
     EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR KLFPYDPYER ARQKMLLELF
     CKILEYQNTT FFGGTCISMI DYLLWPWFER LDVYGILDCV SHTPALRLWI SAMKWDPTVC
     ALLMDKSIFQ GFLNLYFQNN PNAFDFGLC
//
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