InterPro domain: IPR036661
General Information
- Identifier IPR036661
- Description Luciferase-like domain superfamily
- Number of genes 6
- Gene duplication stats Loading...
- Associated GO terms GO:0016705
Abstract
Bacterial luciferase is a flavin monooxygenase that catalyses the oxidation of long-chain aldehydes and releases energy in the form of visible light, and which uses flavin as a substrate rather than a cofactor [ 1 ]. Bacterial luciferase is an alpha/beta (LuxA/LuxB) heterodimer, where each individual subunit folds into a single TIM (beta/alpha)8-barrel domain. There are structural similarities between bacterial luciferase and nonfluorescent flavoproteins (LuxF, FP390), alkanesulphonate monooxygenase (SsuD), and coenzyme F420-dependent terahydromethanopterin reductase, which make up clearly related families with somewhat different folds [ 2 , 3 , 4 ].
1. The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271, 21956-68
2. Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. J. Mol. Biol. 249, 195-214
3. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. J. Mol. Biol. 324, 457-68
4. Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. J. Mol. Biol. 300, 935-50