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InterPro: IPR018235 Bacterial luciferase, conserved site

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365 proteins

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Accession

IPR018235 Bacterial_luciferase_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00494	BACTERIAL_LUCIFERASE	365
Signatures in BioMart

InterPro Relationships Help

Found in

IPR002103 Bacterial luciferase
IPR011251 Luciferase-like
IPR016048 Luciferase-like, subgroup

InterPro annotation

Entry Details in BioMart

Abstract

The enzyme responsible for bioluminescence in motile Gram-negative luminous bacteria is bacterial luciferase [1, 2, 3] (EC:1.14.14.3), which catalyses the oxidation 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 alpha subunit (gene luxA) and a beta 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. More information about these proteins can be found at Protein of the Month: Luciferase [4].

This conserved site is located in the central part of the proteins in this entry.

Structural links Help

PDB - click here

SCOP: c.1.16.1 , c.1.16.2

CATH: 3.20.20.30

Database links Help

Enzyme: EC:1.14.14.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018235

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P07739 Alkanal monooxygenase beta chain

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018235	Bacterial luciferase, conserved site
IPR002103	Bacterial luciferase
IPR011251	Luciferase-like
IPR016048	Luciferase-like, subgroup
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
2.	Meighen EA. Bacterial bioluminescence: organization, regulation, and application of the lux genes. FASEB J. 7 1016-22 1993 [PubMed: 8370470] http://www.fasebj.org/cgi/content/abstract/7/11/1016
4.	McDowall J. Protein of the Month: Luciferase. 2006

Additional Reading Open in usermanual
	Meighen EA. Molecular biology of bacterial bioluminescence. Microbiol. Rev. 55 1991 123-42 [PubMed: 2030669] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2030669
	Kita A, Kasai S, Miyata M, Miki K. Structure of flavoprotein FP390 from a luminescent bacterium Photobacterium phosphoreum refined at 2.7 A resolution. Acta Crystallogr. D Biol. Crystallogr. 52 1996 77-86 [PubMed: 15299728] http://dx.doi.org/10.1107/S0907444995009796
	Tanner JJ, Miller MD, Wilson KS, Tu SC, Krause KL. Structure of bacterial luciferase beta 2 homodimer: implications for flavin binding. Biochemistry 36 1997 665-72 [PubMed: 9020763] http://dx.doi.org/10.1021/bi962511x
	Thoden JB, Holden HM, Fisher AJ, Sinclair JF, Wesenberg G, Baldwin TO, Rayment I. Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap. Protein Sci. 6 1997 13-23 [PubMed: 9007973] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9007973
	Fisher AJ, Thompson TB, Thoden JB, Baldwin TO, Rayment I. The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271 1996 21956-68 [PubMed: 8703001] http://dx.doi.org/10.1074/jbc.271.36.21956
	Moore SA, James MN. Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. J. Mol. Biol. 249 1995 195-214 [PubMed: 7776372] http://dx.doi.org/10.1006/jmbi.1995.0289

InterPro 23.1