CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.30 | Luciferase-like domain |
Domain Context
CATH Clusters
| Superfamily | Luciferase-like domain |
| Functional Family |
Enzyme Information
| 1.14.14.3 |
Bacterial luciferase.
based on mapping to UniProt P07739
A long-chain aldehyde + FMNH(2) + O(2) = a long-chain fatty acid + FMN + H(2)O + light.
-!- The reaction sequence starts with the incorporation of a molecule of oxygen into reduced FMN bound to the enzyme, forming luciferase peroxyflavin. -!- The peroxyflavin interacts with an aliphatic long-chain aldehyde, producing a highly fluorescent species believed to be luciferase hydroxyflavin. -!- The enzyme is highly specific for reduced FMN and for long-chain aliphatic aldehydes with eight carbons or more. -!- The highest efficiency is achieved with tetradecanal. -!- Cf. EC 1.13.12.18.
|
UniProtKB Entries (1)
| P07739 |
LUXB_VIBHA
Vibrio harveyi
Alkanal monooxygenase beta chain
|
PDB Structure
| PDB | 1BSL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap.
Protein Sci.
|
