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
| 1.4.99.6 |
D-arginine dehydrogenase.
based on mapping to UniProt Q9HXE3
D-arginine + acceptor + H(2)O = 5-guanidino-2-oxopentanoate + NH(3) + reduced acceptor.
-!- The enzyme, which has been isolated from the bacterium Pseudomonas aeruginosa PAO1, forms with EC 1.4.1.25 a two-enzyme complex involved in the racemization of D- and L-arginine. -!- The enzyme has a broad substrate range and can act on most D-amino acids with the exception of D-glutamate and D-aspartate. -!- However, activity is maximal with D-arginine and D-lysine. -!- Not active on glycine. -!- Formerly EC 1.4.99.1.
|
UniProtKB Entries (1)
| Q9HXE3 |
DAUA_PSEAE
Pseudomonas aeruginosa PAO1
FAD-dependent catabolic D-arginine dehydrogenase DauA
|
PDB Structure
| PDB | 3NYE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Conformational changes and substrate recognition in Pseudomonas aeruginosa D-arginine dehydrogenase.
Biochemistry
|
