CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.60 | FAD/NAD(P)-binding domain |
Domain Context
CATH Clusters
| Superfamily | FAD/NAD(P)-binding domain |
| Functional Family |
Enzyme Information
| 1.4.3.16 |
L-aspartate oxidase.
based on mapping to UniProt Q972D2
L-aspartate + O(2) = iminosuccinate + H(2)O(2).
-!- L-aspartate oxidase catalyzes the first step in the de novo biosynthesis of NAD(+) in some bacteria. -!- O(2) can be replaced by fumarate as electron acceptor, yielding succinate. -!- The ability of the enzyme to use both O(2) and fumarate in cofactor reoxidation enables it to function under both aerobic and anaerobic conditions. -!- Iminosuccinate can either be hydrolyzed to form oxaloacetate and NH(3) or can be used by EC 2.5.1.72 in the production of quinolinate.
|
UniProtKB Entries (1)
| Q972D2 |
NADB_SULTO
Sulfurisphaera tokodaii str. 7
L-aspartate oxidase
|
PDB Structure
| PDB | 2E5V |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of l-aspartate oxidase from the hyperthermophilic archaeon Sulfolobus tokodaii
Biochim.Biophys.Acta
|