Deoxyuridine triphosphate nucleotidohydrolase/Deoxycytidine triphosphate deaminase (IPR008180)
Short name: dUTPase/dCTP_deaminase
- Deoxyuridine triphosphate nucleotidohydrolase/Deoxycytidine triphosphate deaminase (IPR008180)
- Deoxycytidine triphosphate deaminase (IPR011962)
- Deoxyuridine triphosphate nucleotidohydrolase (IPR008181)
- Deoxyuridine triphosphate nucleotidohydrolase, archaeal (IPR023537)
The essential enzyme deoxyuridine triphosphate nucleotidohydrolase (dUTPase) (EC:188.8.131.52) is specific for dUTP and is critical for the fidelity of DNA replication and repair. dUTPase hydrolyzes dUTP to dUMP and pyrophosphate, simultaneously reducing dUTP levels and providing the dUMP for dTTP biosynthesis. dUTPase decreases the intracellular concentration of dUPT so that uracil cannot be incorporated into DNA [PMID: 8805593].
The crystal structure of human dUTPase reveals that each subunit of the dUTPase trimer folds into an eight-stranded jelly-roll beta barrel, with the C-terminal beta strands interchanged among the subunits. The structure is similar to that of the Escherichia coli enzyme, despite low sequence homology between the two enzymes [PMID: 8805593].
Other enzymes like deoxycytidine triphosphate deaminase (dCTP) (EC:184.108.40.206) that specifically bind uridine also belong to this group suggesting that the signature may recognise a putative uridine-binding motif.
Some retroviruses encode dUTPases. Retroviral dUTPase is synthesised as part of POL polyprotein that contains; an aspartyl protease, a reverse transcriptase, dUTPase and RNase H.
- PF00692 (dUTPase)