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 | Adenylate kinase 1 |
Enzyme Information
| 2.7.4.14 |
UMP/CMP kinase.
based on mapping to UniProt P30085
(1) ATP + (d)CMP = ADP + (d)CDP. (2) ATP + UMP = ADP + UDP.
-!- This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency. -!- dCMP can also act as acceptor. -!- Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase. -!- This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency. -!- dCMP can also act as acceptor. -!- Different from the monofunctional prokaryotic enzymes EC 2.7.4.25 and EC 2.7.4.22. -!- Formerly EC 2.7.4.5.
|
| 2.7.4.6 |
Nucleoside-diphosphate kinase.
based on mapping to UniProt P30085
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
-!- Many nucleoside diphosphates can act as acceptors. -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors.
|
UniProtKB Entries (1)
| P30085 |
KCY_HUMAN
Homo sapiens
UMP-CMP kinase
|
PDB Structure
| PDB | 1TEV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Substrate-induced Conformational Changes in Human UMP/CMP Kinase.
J.Biol.Chem.
|
