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InterPro: IPR019911 Alkanesulphonate monooxygenase, FMN-dependent

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333 proteins

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Accession

IPR019911 Alkanesulphonate_mOase_FMN-dep

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR03565	Alk_sulf_monoox	333
Signatures in BioMart

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Parent

IPR016048 Luciferase-like, subgroup

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].

This entry represents a distinct group of proteins within the wider luciferase-like family of monooxygenases. They catalyse the desulphonation of aliphatic sulphonates such as methane sulphonate in an FMN-dependent fashion.

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PDB - click here

SCOP: c.1.16.4

CATH: 3.20.20.30

Database links Help

Enzyme: EC:1.14.14.5

CluSTr: ALLvsALL:36718:63.7

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Overlapping InterPro entries Help

IPR019911

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P80645 Alkanesulfonate monooxygenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR019911	Alkanesulphonate monooxygenase, FMN-dependent
IPR011251	Luciferase-like
IPR016048	Luciferase-like, subgroup
	PDB Chain
	ModBase
	SCOP Domain
	CATH 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
	Kertesz MA, Schmidt-Larbig K, Wuest T. A novel reduced flavin mononucleotide-dependent methanesulfonate sulfonatase encoded by the sulfur-regulated msu operon of Pseudomonas aeruginosa. J. Bacteriol. 181 1999 1464-73 [PubMed: 10049377] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=10049377

InterPro 23.1