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MGP000865

UniProt Annotations

Entry Information
Gene Namedihydropyrimidine dehydrogenase
Protein EntryDPYD_HUMAN
UniProt IDQ12882
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q12882-1; Sequence=Displayed; Name=2; IsoId=Q12882-2; Sequence=VSP_044929, VSP_044930; Note=No experimental confirmation available.;
Catalytic Activity5,6-dihydrouracil + NADP(+) = uracil + NADPH.
CofactorName=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms per subunit. {ECO:0000250};
CofactorName=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 2 FAD.;
CofactorName=FMN; Xref=ChEBI:CHEBI:58210; Note=Binds 2 FMN.;
DiseaseDihydropyrimidine dehydrogenase deficiency (DPYDD) [MIM:274270]: A metabolic disorder with large phenotypic variability, ranging from no symptoms to a convulsive disorder with motor and mental retardation. It is characterized by persistent urinary excretion of excessive amounts of uracil, thymine and 5-hydroxymethyluracil. Patients suffering from this disease show a severe reaction to the anticancer drug 5- fluorouracil. {ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:16710414, ECO:0000269|PubMed:9266349, ECO:0000269|PubMed:9439663}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionInvolved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.
PathwayAmino-acid biosynthesis; beta-alanine biosynthesis.
SimilarityBelongs to the dihydropyrimidine dehydrogenase family. {ECO:0000305}.
SimilarityContains 3 4Fe-4S ferredoxin-type domains. {ECO:0000255|PROSITE-ProRule:PRU00711}.
Subcellular LocationCytoplasm.
SubunitHomodimer.
Tissue SpecificityFound in most tissues with greatest activity found in liver and peripheral blood mononuclear cells.
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