InterPro domain: IPR033704

Trimeric dUTP diphosphatases (dUTP nucleotidohydrolases or dUTPases), are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface [ 1 , 2 ].

This entry represents the main structural domain, which folds into an eight-stranded jelly-roll beta barrel.

1. Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP. Curr. Protein Pept. Sci. 2, 287-300
2. Crystal structure of a dUTPase. Nature 355, 740-3