PF00296

Luciferase-like monooxygenase

Pfam entry
Member databasePfam
Pfam typedomain
Short nameBac_luciferase
ClanTIM_barrel
Author Bateman A;0000-0002-6982-4660 Finn RD;0000-0001-8626-2148 Griffiths-Jones SR;0000-0001-6043-807X
Sequence Ontology0000417

Description
Imported from IPR011251

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
[2]
. Bacterial luciferase is an alpha/beta (LuxA/LuxB) heterodimer, where each individual subunit folds into a single TIM (β/α)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
[3, 4, 1]
.

References
Imported from IPR011251

1.Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. Shima S, Warkentin E, Grabarse W, Sordel M, Wicke M, Thauer RK, Ermler U. J. Mol. Biol. 300, 935-50, (2000). View articlePMID: 10891279

2.The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. Fisher AJ, Thompson TB, Thoden JB, Baldwin TO, Rayment I. J. Biol. Chem. 271, 21956-68, (1996). View articlePMID: 8703001

3.Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. Moore SA, James MN. J. Mol. Biol. 249, 195-214, (1995). View articlePMID: 7776372

4.Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. Eichhorn E, Davey CA, Sargent DF, Leisinger T, Richmond TJ. J. Mol. Biol. 324, 457-68, (2002). View articlePMID: 12445781

Wikipedia

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.