CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.1160 | Carbamate kinase |
|
3.40.1160.10 | Acetylglutamate kinase-like |
Domain Context
CATH Clusters
| Superfamily | Acetylglutamate kinase-like |
| Functional Family | Bifunctional aspartokinase/homoserine dehydrogenase |
Enzyme Information
| 2.7.2.4 |
Aspartate kinase.
based on mapping to UniProt Q57991
ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
-!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3. -!- This is also the case for two of the four isoenzymes in Arabidopsis thaliana. -!- The equilibrium constant strongly favors the reaction from right to left, i.e. the non-physiological direction of reaction.
|
UniProtKB Entries (1)
| Q57991 |
AK_METJA
Methanocaldococcus jannaschii DSM 2661
Probable aspartokinase
|
PDB Structure
| PDB | 3C1N |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The Structural Basis for Allosteric Inhibition of a Threonine-sensitive Aspartokinase.
J.Biol.Chem.
|
