CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.140 | Butyryl-CoA Dehydrogenase, subunit A; domain 3 |
|
1.20.140.10 | Butyryl-CoA Dehydrogenase, subunit A, domain 3 |
Domain Context
CATH Clusters
| Superfamily | Butyryl-CoA Dehydrogenase, subunit A, domain 3 |
| Functional Family |
Enzyme Information
| 1.14.14.9 |
4-hydroxyphenylacetate 3-monooxygenase.
based on mapping to UniProt Q6Q272
4-hydroxyphenylacetate + FADH(2) + O(2) = 3,4-dihydroxyphenylacetate + FAD + H(2)O.
-!- The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. -!- The enzyme uses FADH(2) as a substrate rather than a cofactor. -!- FADH(2) is provided by EC 1.5.1.36. -!- Formerly EC 1.14.13.3.
|
UniProtKB Entries (1)
| Q6Q272 |
HPAH_ACIBA
Acinetobacter baumannii
P-hydroxyphenylacetate 3-hydroxylase, oxygenase component
|
PDB Structure
| PDB | 2JBR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of the Monooxygenase Component of a Two-Component Flavoprotein Monooxygenase.
Proc.Natl.Acad.Sci.USA
|
