Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:
acid phosphatase / phosphotransferaseInferred from experiment: aphA
5'-deoxyribonucleotidaseInferred from experiment: ushA
CPS-53 (KpLE1) prophage; deoxyribonucleoside 5'-monophosphate phosphataseInferred from experiment: yfdR
dCMP phosphohydrolaseInferred from experiment: yfbR

Reaction Locations: periplasm (sensu Gram-negative Bacteria), cytosol

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Instance reactions:
dCMP + H2O → 2'-deoxycytidine + phosphate (

dUMP + H2O → 2'-deoxyuridine + phosphate (

dAMP + H2O → 2'-deoxyadenosine + phosphate (

dGMP + H2O → 2'-deoxyguanosine + phosphate (

dTMP + H2O → thymidine + phosphate (

Enzyme Commission Primary Name: 5′-deoxynucleotidase

Enzyme Commission Synonyms: yfbR (gene name)

Enzyme Commission Summary:
The enzyme, characterized from the bacterium Escherichia coli, shows strict specificity towards deoxyribonucleoside 5'-monophosphates and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates. A divalent metal cation is required for activity, with cobalt providing the highest activity.

Citations: [Proudfoot04, Zimmerman08]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


Proudfoot04: Proudfoot M, Kuznetsova E, Brown G, Rao NN, Kitagawa M, Mori H, Savchenko A, Yakunin AF (2004). "General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG." J Biol Chem 279(52);54687-94. PMID: 15489502

Zimmerman08: Zimmerman MD, Proudfoot M, Yakunin A, Minor W (2008). "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(1);215-26. PMID: 18353368

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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