CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.300 | P-loop containing nucleotide triphosphate hydrolases |
Domain Context
CATH Clusters
| Superfamily | P-loop containing nucleotide triphosphate hydrolases |
| Functional Family | Cytidylate kinase |
Enzyme Information
| 2.7.4.25 |
(d)CMP kinase.
based on mapping to UniProt P0A6I0
ATP + (d)CMP = ADP + (d)CDP.
-!- 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 catalyzed in prokaryotes by EC 2.7.4.22. -!- The enzyme phosphorylates dCMP nearly as well as it does CMP.
|
UniProtKB Entries (1)
| P0A6I0 |
KCY_ECOLI
Escherichia coli K-12
Cytidylate kinase
|
PDB Structure
| PDB | 1CKE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structures of escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity.
Structure
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