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2.7.3.8

Accepted name:

ammonia kinase

Reaction:

ATP + NH₃ = ADP + phosphoramide

Other name(s):

phosphoramidate-adenosine diphosphate phosphotransferase; phosphoramidate-ADP-phosphotransferase

Systematic name:

ATP:ammonia phosphotransferase

Comments:

Has a wide specificity. In the reverse direction, N-phosphoglycine and N-phosphohistidine can also act as phosphate donors, and ADP, dADP, GDP, CDP, dTDP, dCDP, IDP and UDP can act as phosphate acceptors (in decreasing order of activity).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-16-3

References:

1.	Dowler, M.J. and Nakada, H.I. Yeast phosphoramidate-adenosine diphosphate phosphotransferase. J. Biol. Chem. 243 (1968) 1434–1440. [PMID: 5647264]

[EC 2.7.3.8 created 1972]

2.7.4.19

Accepted name:

5-methyldeoxycytidine-5′-phosphate kinase

Reaction:

ATP + 5-methyldeoxycytidine 5′-phosphate = ADP + 5-methyldeoxycytidine diphosphate

Systematic name:

ATP:5-methyldeoxycytidine-5′-phosphate phosphotransferase

Comments:

The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts m⁵dCMP into m⁵dCDP and then into m⁵dCTP.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81032-53-3

References:

1.	Wang, R.Y.-H., Huang, L.-H. and Ehrlich, M. A bacteriophage-induced 5-methyldeoxycytidine 5′-monophosphate kinase. Biochim. Biophys. Acta 696 (1982) 31–36. [DOI] [PMID: 7082669]

[EC 2.7.4.19 created 1984]

2.7.4.25

Accepted name:

(d)CMP kinase

Reaction:

ATP + (d)CMP = ADP + (d)CDP

Glossary:

CMP = cytidine monophosphate
dCMP = deoxycytidine monophosphate
CDP = cytidine diphosphate
dCDP = deoxycytidine diphosphate
UMP = uridine monophosphate
UDP = uridine diphosphate

Other name(s):

cmk (gene name); prokaryotic cytidylate kinase; deoxycytidylate kinase (misleading); dCMP kinase (misleading); deoxycytidine monophosphokinase (misleading)

Systematic name:

ATP:(d)CMP phosphotransferase

Comments:

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].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Bertrand, T., Briozzo, P., Assairi, L., Ofiteru, A., Bucurenci, N., Munier-Lehmann, H., Golinelli-Pimpaneau, B., Barzu, O. and Gilles, A.M. Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme. J. Mol. Biol. 315 (2002) 1099–1110. [DOI] [PMID: 11827479]
2.	Thum, C., Schneider, C.Z., Palma, M.S., Santos, D.S. and Basso, L.A. The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP. J. Bacteriol. 191 (2009) 2884–2887. [DOI] [PMID: 19181797]

[EC 2.7.4.25 created 2011]