Function and Biology Details
Reaction catalysed:
5,6-dihydrouracil + NADP(+) = uracil + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- 4Fe-4S ferredoxin-type, iron-sulphur binding domain
- Dihydroorotate dehydrogenase, catalytic
- FAD/NAD(P)-binding domain superfamily
- 4Fe-4S ferredoxin, iron-sulphur binding, conserved site
- Aldolase-type TIM barrel
- FAD/NAD(P)-binding domain
- Dihydroprymidine dehydrogenase domain II
- Alpha-helical ferredoxin
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Dihydropyrimidine dehydrogenase [NADP(+)] (preferred)
PDBe Complex ID:
PDB-CPX-173320 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropyrimidine dehydrogenase [NADP(+)]
Molecule details ›
Chains: A, B, C, D
Length: 1025 amino acids
Theoretical weight: 111.6 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli DH5[alpha]
UniProt:
Sequence domains:
Length: 1025 amino acids
Theoretical weight: 111.6 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli DH5[alpha]
UniProt:
- Canonical:
Q28943 (Residues: 1-1025; Coverage: 100%)
Sequence domains:
- Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster
- Pyridine nucleotide-disulphide oxidoreductase
- Dihydroorotate dehydrogenase
- 4Fe-4S dicluster domain
