| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.4 Phosphotransferases with a phosphate group as acceptor |
| ID: | 2.7.4.25 |
|---|---|
| Description: | (d)CMP kinase. |
| Alternative Name: |
Deoxycytidylate kinase. Deoxycytidine monophosphokinase. dCMP kinase. |
| Cath: | 3.40.50.300; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.7.4.25 |
| BRENDA Enzyme Link: | BRENDA 2.7.4.25 |
| KEGG Enzyme Link: | KEGG2.7.4.25 |
| BioCyc Enzyme Link: | BioCyc 2.7.4.25 |
| ExPASy Enzyme Link: | ExPASy2.7.4.25 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.4.25 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.4.25 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.4.25 |
| IntEnz Enzyme Link: | IntEnz 2.7.4.25 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.4.25 |
| RHEA:25094 | ATP + dCMP = ADP + dCDP |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural and catalytic properties of CMP kinase from Bacillus subtilis: a comparative analysis with the homologous enzyme from Escherichia coli. | Schultz CP, Ylisastigui-Pons L, Serina L, Sakamoto H, Mantsch HH, Neuhard J, Bârzu O, Gilles AM | 1997 Apr 1 | 9126287 |
| The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli. | Fricke J, Neuhard J, Kelln RA, Pedersen S | 1995 Feb | 7836281 |
| The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP. | Thum C, Schneider CZ, Palma MS, Santos DS, Basso LA | 2009 Apr | 19181797 |
| Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme. | Bertrand T, Briozzo P, Assairi L, Ofiteru A, Bucurenci N, Munier-Lehmann H, Golinelli-Pimpaneau B, Bârzu O, Gilles AM | 2002 Feb 1 | 11827479 |
| CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases. | Bucurenci N, Sakamoto H, Briozzo P, Palibroda N, Serina L, Sarfati RS, Labesse G, Briand G, Danchin A, Bărzu O, Gilles AM | 1996 Feb 2 | 8576266 |
| Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates. | Liou JY, Dutschman GE, Lam W, Jiang Z, Cheng YC | 2002 Mar 15 | 11912132 |
| RHEA:11600 | ATP + CMP = ADP + CDP |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural and catalytic properties of CMP kinase from Bacillus subtilis: a comparative analysis with the homologous enzyme from Escherichia coli. | Schultz CP, Ylisastigui-Pons L, Serina L, Sakamoto H, Mantsch HH, Neuhard J, Bârzu O, Gilles AM | 1997 Apr 1 | 9126287 |
| The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli. | Fricke J, Neuhard J, Kelln RA, Pedersen S | 1995 Feb | 7836281 |
| The Rv1712 Locus from Mycobacterium tuberculosis H37Rv codes for a functional CMP kinase that preferentially phosphorylates dCMP. | Thum C, Schneider CZ, Palma MS, Santos DS, Basso LA | 2009 Apr | 19181797 |
| Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme. | Bertrand T, Briozzo P, Assairi L, Ofiteru A, Bucurenci N, Munier-Lehmann H, Golinelli-Pimpaneau B, Bârzu O, Gilles AM | 2002 Feb 1 | 11827479 |