EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR005025 NADPH-dependent FMN reductase

Protein matches Help

UniProtKB

Matches:

3330 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
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

IPR005025 FMN_red

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03358	FMN_red	3330
Signatures in BioMart

InterPro Relationships Help

Children

IPR019912 FMN reductase, MsuE-like
IPR020048 NADPH-dependent ,FMN reductase, SsuE

Found in

IPR014063 Arsenate resistance ArsH

InterPro annotation

Entry Details in BioMart

Abstract

NADPH-dependent FMN reductase (EC:1.5.1.29) reduces FMN and also reduces riboflavin and FAD, although more slowly. Members of this entry catalyse the reaction

NAD(P)H + FMN = NAD(P)(+) + FMNH(2).

Structural links Help

PDB - click here

SCOP: c.23.5.4 , c.23.5.6

CATH: 3.40.50.360

Database links Help

PANDIT: PF03358

Blocks: IPB005025

Pfam Clan: CL0042.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005025

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O07529 FMN-dependent NADPH-azoreductase

O28383 Iron-sulfur flavoprotein AF_1896

Q07923 NAD(P)H-dependent FMN reductase LOT6

Q941Y8 Probable NADPH:quinone oxidoreductase 2

Q9LK88 NADPH:quinone oxidoreductase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005025	NADPH-dependent FMN reductase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Agarwal R, Bonanno JB, Burley SK, Swaminathan S. Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal. Acta Crystallogr. D Biol. Crystallogr. 62 2006 383-91 [PubMed: 16552139] http://dx.doi.org/10.1107/S0907444906001600
	van Der Ploeg JR, Iwanicka-Nowicka R, Bykowski T, Hryniewicz MM, Leisinger T. The Escherichia coli ssuEADCB gene cluster is required for the utilization of sulfur from aliphatic sulfonates and is regulated by the transcriptional activator Cbl. J. Biol. Chem. 274 1999 29358-65 [PubMed: 10506196] http://dx.doi.org/10.1074/jbc.274.41.29358
	Liger D, Graille M, Zhou CZ, Leulliot N, Quevillon-Cheruel S, Blondeau K, Janin J, van Tilbeurgh H. Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities. J. Biol. Chem. 279 2004 34890-7 [PubMed: 15184374] http://dx.doi.org/10.1074/jbc.M405404200
	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
	Vorontsov II, Minasov G, Brunzelle JS, Shuvalova L, Kiryukhina O, Collart FR, Anderson WF. Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity. Protein Sci. 16 2007 2483-90 [PubMed: 17962405] http://dx.doi.org/10.1110/ps.073029607

InterPro 23.1