ID E1BJ08_BOVIN Unreviewed; 344 AA.
AC E1BJ08;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Glutathione-dependent dehydroascorbate reductase {ECO:0000256|ARBA:ARBA00032186};
DE EC=1.20.4.2 {ECO:0000256|ARBA:ARBA00013060};
DE EC=1.8.5.1 {ECO:0000256|ARBA:ARBA00012436};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
DE AltName: Full=Monomethylarsonic acid reductase {ECO:0000256|ARBA:ARBA00032681};
GN Name=LOC785216 {ECO:0000313|Ensembl:ENSBTAP00000017435.6};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000017435.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000017435.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017435.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000017435.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017435.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000256|ARBA:ARBA00011067}.
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DR AlphaFoldDB; E1BJ08; -.
DR SMR; E1BJ08; -.
DR STRING; 9913.ENSBTAP00000017435; -.
DR PaxDb; 9913-ENSBTAP00000017435; -.
DR Ensembl; ENSBTAT00000017435.6; ENSBTAP00000017435.6; ENSBTAG00000038540.3.
DR VEuPathDB; HostDB:ENSBTAG00000038540; -.
DR eggNOG; KOG0406; Eukaryota.
DR GeneTree; ENSGT00940000155351; -.
DR HOGENOM; CLU_011226_9_2_1; -.
DR InParanoid; E1BJ08; -.
DR OMA; FGACFCP; -.
DR TreeFam; TF105325; -.
DR Reactome; R-BTA-156581; Methylation.
DR Reactome; R-BTA-156590; Glutathione conjugation.
DR Reactome; R-BTA-196836; Vitamin C (ascorbate) metabolism.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000038540; Expressed in liver and 105 other cell types or tissues.
DR ExpressionAtlas; E1BJ08; baseline and differential.
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-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IBA:GO_Central.
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; 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; PF00043; GST_C; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01625; GSTRNSFRASEO.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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 1: Evidence at protein level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proteomics identification {ECO:0007829|PeptideAtlas:E1BJ08};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 125..204
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 209..333
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 344 AA; 38033 MW; 332077C4E2550687 CRC64;
MYCKGACSGN IGCDLPPGAQ AAVVGSSFLE RVGNPPARWV GSPKGLCAQI SFQRPGSAGP
CAHSPGRADG CPSLALLRKI GEARPTSWLN FKLHWELGLC CAAMSGGTVR SLGKGSAPPG
PVPEGLIRVY SMRFCPYAKR TLLVLRAKGI RHEVININLK NKPEWFFKKN PLGLVPVLET
SLGQLIYESA ITCEYLDEAY PGKKLLPGDP YEKACQKMVF ESFSKVPSLM VSFLRKQNKE
DCSGLKEELH KEFSKLEEVL TNKKTTFFGG SSLSMIDYLI WPWFEWLEAL ELNECVDHTP
NLKLWMASMK NDPIVSSLPT DVKTLQDFFN LYLQNSPEAC DYGL
//
