CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 |
| Functional Family |
Enzyme Information
| 4.1.1.12 |
Aspartate 4-decarboxylase.
based on mapping to UniProt Q93QX0
L-aspartate = L-alanine + CO(2).
-!- Also catalyzes the decarboxylation of aminomalonate and the desulfination of 3-sulfino-L-alanine to sulfite and alanine. -!- Formerly EC 4.1.1.10.
|
| 2.6.1.1 |
Aspartate transaminase.
based on mapping to UniProt Q93QX0
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
-!- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. -!- This activity can be formed from EC 2.6.1.57 by controlled proteolysis.
|
UniProtKB Entries (1)
| Q93QX0 |
ASDA_COMTE
Comamonas testosteroni
Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase
|
PDB Structure
| PDB | 2ZY4 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure, Assembly, and Mechanism of a PLP-Dependent Dodecameric l-Aspartate beta-Decarboxylase
Structure
|
