Function and Biology Details
Reactions catalysed:
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Thymidylate synthase
- Dihydrofolate reductase domain
- Thymidylate synthase/dCMP hydroxymethylase domain
- Thymidylate synthase/dCMP hydroxymethylase superfamily
- Dihydrofolate reductase-like domain superfamily
- Thymidylate synthase, active site
- Thymidylate synthase/dCMP hydroxymethylase
- Dihydrofolate reductase conserved site
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146816 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bifunctional dihydrofolate reductase-thymidylate synthase
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 33.13 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
Structure domains: Dihydrofolate Reductase, subunit A
Length: 280 amino acids
Theoretical weight: 33.13 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
- Canonical:
P13922 (Residues: 1-280; Coverage: 46%)
Structure domains: Dihydrofolate Reductase, subunit A
Bifunctional dihydrofolate reductase-thymidylate synthase
Molecule details ›
Chains: C, D
Length: 328 amino acids
Theoretical weight: 38.71 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain
Length: 328 amino acids
Theoretical weight: 38.71 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
- Canonical: P13922 (Residues: 281-608; Coverage: 54%)
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain
