CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.630 | Cytochrome p450 |
|
1.10.630.10 | Cytochrome P450 |
Domain Context
CATH Clusters
| Superfamily | Cytochrome P450 |
| Functional Family | Cytochrome P450 monooxygenase |
Enzyme Information
| 1.14.19.69 |
Biflaviolin synthase.
based on mapping to UniProt Q9FCA6
(1) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 3,3'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O. (2) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 3,8'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O.
-!- This cytochrome-P450 (heme-thiolate) enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyzes a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product. -!- The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation. -!- Formerly EC 1.14.21.7.
|
UniProtKB Entries (1)
| Q9FCA6 |
C1582_STRCO
Streptomyces coelicolor A3(2)
Biflaviolin synthase CYP158A2
|
PDB Structure
| PDB | 2D0E |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer
J.Biol.Chem.
|
