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
| 1.14.13.7 |
Phenol 2-monooxygenase (NADPH).
based on mapping to UniProt P15245
Phenol + NADPH + O(2) = catechol + NADP(+) + H(2)O.
-!- The enzyme from the fungus Trichosporon cutaneum has a broad substrate specificity, and has been reported to catalyze the hydroxylation of a variety of substituted phenols, such as fluoro-, chloro-, amino- and methyl-phenols and also dihydroxybenzenes. -!- Cf. EC 1.14.14.20.
|
UniProtKB Entries (1)
| P15245 |
PHHY_TRICU
Cutaneotrichosporon cutaneum
Phenol hydroxylase
|
PDB Structure
| PDB | 1FOH |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis.
Structure
|
