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
| 1.14.19.9 |
Tryptophan 7-halogenase.
based on mapping to UniProt Q8KHZ8
Tryptophan + FADH(2) + chloride + O(2) + H(+) = 7-chloro-L-tryptophan + FAD + 2 H(2)O.
-!- A flavin-dependent halogenase. -!- The enzyme from the bacterium Lechevalieria aerocolonigenes catalyzes the initial step in the biosynthesis of rebeccamycin. -!- It utilizes molecular oxygen to oxidize the FADH(2) cofactor, giving C4a-hydroperoxyflavin, which then reacts with chloride to produce a hypochlorite ion. -!- The latter reacts with an active site lysine to generate a chloramine, which chlorinates the substrate. -!- Also acts on bromide ion. -!- Cf. EC 1.14.19.58 and EC 1.14.19.59.
|
UniProtKB Entries (1)
| Q8KHZ8 |
REBH_NOCAE
Lechevalieria aerocolonigenes
Flavin-dependent tryptophan halogenase RebH
|
PDB Structure
| PDB | 2OA1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of flavin-dependent tryptophan 7-halogenase RebH.
Proteins
|
