Protein Domain : 5'-deoxynucleotidase YfbR IPR022971

Type	Family
Description	This entry contains Escherichia coli (strain K12) YfbR. It is a 5'-deoxynucleotidase that functions as a dCMP phosphohydrolase in a salvage pathway for the synthesis of dUMP in a dcd/deoA mutant [ ]. YfbR contains a conserved HD domain []. YfbR has phosphatase activity with deoxyribonucleoside 5'-monophosphates and does not hydrolyze ribonucleotides or deoxyribonucloside 3'-monophosphates []. Nucleotidase activity of YfbR was discovered in a high-throughput screen of purified proteins []. Crystal structures of YfbR have been solved; based on an analysis of crystal packing and size-exclusion chromatography, it was suggested that the biological unit is a dimer. Site-directed mutagenesis confirmed the importance of certain conserved active site residues, and mechanisms for substrate selectivity and catalysis were proposed [].This family also includes phage HD domain-containing hydrolase-like enzymes, such as A0A2H5BHG9 and A0A2L0V156 from Acinetobacter phage SH-Ab 15497 [ ], which are associated with PurZ, an enzyme that catalyses the synthesis of diaminopurine (Z), a DNA modification that gives phages an advantage for evading host restriction enzymes activity. They have 2'-deoxyadenine 5'-triphosphate triphosphohydrolase (dATPase) activity, and catalyse the hydrolysis of 2'-deoxyadenine 5'-triphosphate (dATP) to 2'-deoxyadenine (dA) and triphosphate, with the highest activity using Co2+ as the divalent metal cofactor. These enzymes are highly specific for dATP and also catalyse the hydrolysis of dADP and dAMP into dA, releasing pyrophosphate and phosphate, respectively. Thus, these dATPases facilitate the synthesis of Z-genome synthesis removing dATP and dADP from the nucleotide pool of the host [].
Short Name	YfbR