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.
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UniProtKB Entries (1)
Q9HXE3 |
DAUA_PSEAE
Pseudomonas aeruginosa PAO1
FAD-dependent catabolic D-arginine dehydrogenase DauA
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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
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