CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.120 | Four Helix Bundle (Hemerythrin (Met), subunit A) |
|
1.20.120.1320 | Aspartokinase, catalytic domain |
Domain Context
CATH Clusters
| Superfamily | Aspartokinase, catalytic domain |
| Functional Family | Aspartokinase |
Enzyme Information
| 2.7.2.4 |
Aspartate kinase.
based on mapping to UniProt P08660
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)
| P08660 |
AK3_ECOLI
Escherichia coli K-12
Lysine-sensitive aspartokinase 3
|
PDB Structure
| PDB | 2J0X |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structures of R- and T-State Escherichia Coli Aspartokinase III: Mechanisms of the Allosteric Transition and Inhibition by Lysine.
J.Biol.Chem.
|