Function and Biology

Plasmodium falciparum thymidylate kinase in complex with a urea-alpha- deoxythymidine inhibitor

Source organism: Plasmodium falciparum 3D7
Biochemical function: T2-induced deoxynucleotide kinase activity
Biological process: nucleoside monophosphate phosphorylation
Cellular component: cytosol

EC 2.7.4.9: dTMP kinase

Reaction catalysed:
ATP + dTMP = ADP + dTDP
Systematic name:
ATP:dTMP phosphotransferase
Alternative Name(s):
  • Deoxythymidine 5'-monophosphate kinase
  • TMPK
  • Thymidine 5'-monophosphate kinase
  • Thymidine monophosphate kinase
  • Thymidylate kinase
  • Thymidylate monophosphate kinase
  • Thymidylic acid kinase
  • Thymidylic kinase

EC 2.7.4.8: Guanylate kinase

Reaction catalysed:
ATP + GMP = ADP + GDP
Systematic name:
ATP:(d)GMP phosphotransferase
Alternative Name(s):
  • 5'-GMP kinase
  • ATP:GMP phosphotransferase
  • Deoxyguanylate kinase
  • GMP kinase
  • Guanosine monophosphate kinase

Sequence family

Pfam Protein family (Pfam)
PF02223
Domain description: Thymidylate kinase
Occurring in:
  1. Thymidylate kinase
The deposited structure of PDB entry 2yoh contains 2 copies of Pfam domain PF02223 (Thymidylate kinase) in Thymidylate kinase. Showing 1 copy in chain B.

InterPro InterPro annotations
IPR018094
Domain description: Thymidylate kinase
Occurring in:
  1. Thymidylate kinase
IPR027417
Domain description: P-loop containing nucleoside triphosphate hydrolase
Occurring in:
  1. Thymidylate kinase
IPR018095
Domain description: Thymidylate kinase, conserved site
Occurring in:
  1. Thymidylate kinase
IPR039430
Domain description: Thymidylate kinase-like domain
Occurring in:
  1. Thymidylate kinase

Structure domain

CATH CATH domain
3.40.50.300
Class: Alpha Beta
Architecture: 3-Layer(aba) Sandwich
Topology: Rossmann fold
Homology: P-loop containing nucleotide triphosphate hydrolases
Occurring in:
  1. Thymidylate kinase
The deposited structure of PDB entry 2yoh contains 2 copies of CATH domain 3.40.50.300 (Rossmann fold) in Thymidylate kinase. Showing 1 copy in chain B.