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Database: UniProt
Entry: C3Z132_BRAFL
LinkDB: C3Z132_BRAFL
Original site: C3Z132_BRAFL 
ID   C3Z132_BRAFL            Unreviewed;       242 AA.
AC   C3Z132;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-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   ORFNames=BRAFLDRAFT_217390 {ECO:0000313|EMBL:EEN53731.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN53731.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN53731.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN53731.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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|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; GG666571; EEN53731.1; -; Genomic_DNA.
DR   RefSeq; XP_002597719.1; XM_002597673.1.
DR   AlphaFoldDB; C3Z132; -.
DR   STRING; 7739.C3Z132; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   InParanoid; C3Z132; -.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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:SF6; GLUTATHIONE-DEPENDENT DEHYDROASCORBATE REDUCTASE; 1.
DR   Pfam; PF13410; GST_C_2; 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          23..101
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          97..236
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   242 AA;  27444 MW;  AE0E96D4CB06E6E2 CRC64;
     MKCFIFDLQF YTGSTAPDPP APGVVRLISN RFCPYAHRTR LVLAAKGIDY ETVNVCLAKR
     PEWFFSINPL AKVPTLQHDG KVVYESLVCN EYVDRVFPGR KLLPEEPLEK ARIGMLQAIW
     DAKVITMTKG EERQKAFEVL KEGLSFFEKH LGTSEAPFFG GEQPGFLDYS IWPWFELLGL
     FLTDDDVKLQ EAEFPRVFAW QAAMFDRPEV KTCACELSVW TKYVASARAG NPDSDIGLDD
     SD
//
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