KEGG   ENZYME: 2.7.4.25Help
Entry
EC 2.7.4.25                 Enzyme                                 

Name
(d)CMP kinase;
prokaryotic cytidylate kinase;
deoxycytidylate kinase;
dCMP kinase;
deoxycytidine monophosphokinase
Class
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with a phosphate group as acceptor
BRITE hierarchy
Sysname
ATP:(d)CMP phosphotransferase
Reaction(IUBMB)
ATP + (d)CMP = ADP + (d)CDP [RN:R00512 R01665]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
dCMP [CPD:C00239]
Product
ADP [CPD:C00008];
dCDP [CPD:C00705]
Comment
The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalysed in prokaryotes by EC 2.7.4.22, UMP kinase. The enzyme phosphorylates dCMP nearly as well as it does CMP [1].
History
EC 2.7.4.25 created 2011
Reference
1  [PMID:11827479]
  Authors
Bertrand T, Briozzo P, Assairi L, Ofiteru A, Bucurenci N, Munier-Lehmann H, Golinelli-Pimpaneau B, Barzu O, Gilles AM
  Title
Sugar specificity of bacterial CMP kinases as revealed by crystal structures and  mutagenesis of Escherichia coli enzyme.
  Journal
J. Mol. Biol. 315 (2002) 1099-110.
Reference
2  [PMID:19181797]
  Authors
Thum C, Schneider CZ, Palma MS, Santos DS, Basso LA
  Title
The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP.
  Journal
J. Bacteriol. 191 (2009) 2884-7.
  Sequence
[up:P63803]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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