| Description | This entry represents the NUDIX domain from diphosphoinositol polyphosphate phosphohydrolases, such as NUDT3, NUDT4, NUDT11 from human, which cleave a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), P-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that they may play a role in signal transduction [, ]. NUT3/4/11 can also catalyse the hydrolysis of diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) but not diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A) and the major reaction products are ADP and p4a from Ap6A. They also hydrolyse 5-phosphoribose 1-diphosphate []. DDP1 and aps1, the orthologues from yeast, are also included in this entry [, ]. DDP1 also has endopolyphosphatase activity [].This domain is also found in some poorly characterised NUDIX hydrolases from plants, such as NUDT4 and NUDT16, and uncharacterised bacterial sequences.Members of the Nudix hydrolase superfamily catalyse the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. require a divalent cation, such as Mg2 or Mn2, for their activity and contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and 'house-cleaning' enzymes [ , , , ]. | Name | Diphosphoinositol polyphosphate phosphohydrolase-like, NUDIX domain |
| Short Name | DDP-like_NUDIX | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
