InterPro domain: IPR039356

Escherichia coli YfbR is a conserved HD-domain-containing protein with orthologues found in bacteria, archaea, and eukaryotes. YfbR shows strict specificity towards deoxyribonucleoside 5'-monophosphates [ 1 , 2 ], and has been established as an essential component of the deoxycytidine pathway for de novo synthesis of thymidylate [ 3 ]. The human genome encodes one YfbR orthologue, the uncharacterized HD-domain-containing protein HDDC2. In yeast, HD-domain proteins YGK1 (YGL101W) and YB92 (YBR242W) from Saccharomyces cerevisiae are nucleoside 5'-monophosphatases, with substrate preference for deoxyribonucleoside 5'-monophosphatase over ribonucleoside 5'-monophosphatase [ 4 ].

1. General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG. J. Biol. Chem. 279, 54687-94
2. Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli. J. Mol. Biol. 378, 215-26
3. The deoxycytidine pathway for thymidylate synthesis in Escherichia coli. J. Bacteriol. 189, 7922-6
4. Structural and biochemical characterization of the yeast HD domain containing protein YGK1 reveals a metal-dependent nucleoside 5'-monophosphatase. Biochem. Biophys. Res. Commun.