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.
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