PROSITE documentation PDOC00397Bacterial luciferase subunits signature
Luminous bacteria are abundant and widely distributed Gram-negative motile rods. The enzyme responsible for bioluminescence, bacterial luciferase [1,2,3] (EC 1.14.14.3), catalyzes the oxidation of reduced riboflavin phosphate (FMNH2) and a long chain fatty aldehyde with the emission of blue green light (490 nm). Luciferase is a heterodimeric enzyme composed of an α subunit (gene luxA) and a β subunit (gene luxB). The two subunits appear to have arisen by gene duplication.
The bioluminescence operon of some species of Photobacterium encodes a protein known as the non-fluorescent flavoprotein (NFP) (gene luxF). NFP, whose function is not yet known, contains an unusual non-covalently bound flavin. It is evolutionary related to the luxA/luxB subunits.
As a signature for this family, we selected a conserved region located in the central part of these proteins.
Last update:June 1994 / Text revised.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Meighen E.A. |
| Title | Molecular biology of bacterial bioluminescence. | |
| Source | Microbiol. Rev. 55:123-142(1991). | |
| PubMed ID | 2030669 |
| 2 | Authors | Meighen E.A. |
| Title | Bacterial bioluminescence: organization, regulation, and application of the lux genes. | |
| Source | FASEB J. 7:1016-1022(1993). | |
| PubMed ID | 8370470 |
| 3 | Authors | O'Kane D.J.O. Prasher D.C. |
| Source | Mol. Microbiol. 6:443-449(1992). |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)