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InterPro: IPR011251 Luciferase-like

Protein matches Help

UniProtKB

Matches:

6189 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR011251 Luciferase-like

Secondary

IPR002103

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.20.20.30	Luciferase_like	6077
SuperFamily	SSF51679	Luciferase_like	6184
Signatures in BioMart

InterPro Relationships Help

Children

IPR016048 Luciferase-like, subgroup
IPR019919 Luciferase-like, F420-dependent oxidoreductase, MSMEG2256, predicted
IPR019922 Luciferase-like, F420-dependent oxidoreductase, MSMEG4141, predicted
IPR020020 Luciferase-type oxidoreductase

Found in

IPR016215 Nitrilotriacetate monooxygenase component A/pristinamycin IIA synthase subunit A

Contains

IPR002103 Bacterial luciferase
IPR018235 Bacterial luciferase, conserved site

InterPro annotation

Entry Details in BioMart

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].

More information about these proteins can be found at Protein of the Month: Luciferase [5].

Structural links Help

PDB - click here

SCOP: c.1.16.1 , c.1.16.2 , c.1.16.3 , c.1.16.4

CATH: 3.20.20.30

Database links Help

Enzyme: EC:1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011251

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O34974 Putative monooxygenase moxC

P48088 Phycobilisome linker polypeptide

Q50744 5,10-methylenetetrahydromethanopterin reductase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR019946	5,10-methylenetetrahydromethanopterin reductase
IPR009050	Globin-like
IPR012128	Phycobilisome, alpha/beta subunit
IPR016215	Nitrilotriacetate monooxygenase component A/pristinamycin IIA synthase subunit A
IPR011251	Luciferase-like
IPR016048	Luciferase-like, subgroup
IPR001297	Phycobilisome linker domain
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	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 21956-68 1996 [PubMed: 8703001] http://dx.doi.org/10.1074/jbc.271.36.21956
2.	Moore SA, James MN. Structural refinement of the non-fluorescent flavoprotein from Photobacterium leiognathi at 1.60 A resolution. J. Mol. Biol. 249 195-214 1995 [PubMed: 7776372] http://dx.doi.org/10.1006/jmbi.1995.0289
3.	Eichhorn E, Davey CA, Sargent DF, Leisinger T, Richmond TJ. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. J. Mol. Biol. 324 457-68 2002 [PubMed: 12445781] http://dx.doi.org/10.1016/S0022-2836(02)01069-0
4.	Shima S, Warkentin E, Grabarse W, Sordel M, Wicke M, Thauer RK, Ermler U. Structure of coenzyme F(420) dependent methylenetetrahydromethanopterin reductase from two methanogenic archaea. J. Mol. Biol. 300 935-50 2000 [PubMed: 10891279] http://dx.doi.org/10.1006/jmbi.2000.3909
5.	McDowall J. Protein of the Month: Luciferase. 2006

Additional Reading Open in usermanual
	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
	Aufhammer SW, Warkentin E, Berk H, Shima S, Thauer RK, Ermler U. Coenzyme binding in F420-dependent secondary alcohol dehydrogenase, a member of the bacterial luciferase family. Structure 12 2004 361-70 [PubMed: 15016352] http://dx.doi.org/10.1016/j.str.2004.02.010

InterPro 23.1