cd03425: MutT_pyrophosphohydrolase (this model, PSSM-Id:239517 is obsolete and has been replaced by 467531)
The MutT pyrophosphohydrolase is a prototypical Nudix hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the Nudix motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.
Structure:1TUM; Escherichia coli MutT binds AMPCPP (a non hydrolyzable substrate analog), Mg2+, and Co2+; defined at 3.5A contacts. - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",