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InterPro: IPR001155 NADH:flavin oxidoreductase/NADH oxidase, N-terminal

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UniProtKB

Matches:

4378 proteins

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

Accession

IPR001155 OxRdtase_FMN_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00724	Oxidored_FMN	4378
Signatures in BioMart

InterPro Relationships Help

Parent

IPR013785 Aldolase-type TIM barrel

GO Term annotation Help

Function

GO:0010181 FMN binding
GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

The TIM-barrel fold is a closed barrel structure composed of an eight-fold repeat of beta-alpha units, where the eight parallel beta strands on the inside are covered by the eight alpha helices on the outside [1]. It is a widely distributed fold which has been found in many enzyme families that catalyse completely unrelated reactions [2]. The active site is always found at the C-terminal end of this domain.

Proteins in this entry are a variety of NADH:flavin oxidoreductase/NADH oxidase enzymes, found mostly in bacteria or fungi, that contain a TIM-barrel fold. They commonly use FMN/FAD as cofactor and include:

dimethylamine dehydrogenase
trimethylamine dehydrogenase
12-oxophytodienoate reductase
NADPH dehydrogenase
NADH oxidase

Structural links Help

PDB - click here

SCOP: c.1.4.1

CATH: 3.20.20.70

Database links Help

Enzyme: EC:1

PANDIT: PF00724

Blocks: IPB001155

Pfam Clan: CL0036.20

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001155

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P16099 Trimethylamine dehydrogenase

P41816 NADPH dehydrogenase 3

Q02899 NADPH dehydrogenase 1

Q8LAH7 12-oxophytodienoate reductase 1

Q9FEW9 12-oxophytodienoate reductase 3

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR001155	NADH:flavin oxidoreductase/NADH oxidase, N-terminal
IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Wierenga RK. The TIM-barrel fold: a versatile framework for efficient enzymes. FEBS Lett. 492 193-8 2001 [PubMed: 11257493] http://dx.doi.org/10.1016/S0014-5793(01)02236-0
2.	Nagano N, Orengo CA, Thornton JM. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J. Mol. Biol. 321 741-65 2002 [PubMed: 12206759] http://dx.doi.org/10.1016/S0022-2836(02)00649-6

Additional Reading Open in usermanual
	Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr. Ensemble refinement of protein crystal structures: validation and application. Structure 15 2007 1040-52 [PubMed: 17850744] http://dx.doi.org/10.1016/j.str.2007.06.019
	Breithaupt C, Kurzbauer R, Lilie H, Schaller A, Strassner J, Huber R, Macheroux P, Clausen T. Crystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerization. Proc. Natl. Acad. Sci. U.S.A. 103 2006 14337-42 [PubMed: 16983071] http://dx.doi.org/10.1073/pnas.0606603103
	Malone TE, Madson SE, Wrobel RL, Jeon WB, Rosenberg NS, Johnson KA, Bingman CA, Smith DW, Phillips GN Jr, Markley JL, Fox BG. X-ray structure of Arabidopsis At2g06050, 12-oxophytodienoate reductase isoform 3. Proteins 58 2005 243-5 [PubMed: 15468319] http://dx.doi.org/10.1002/prot.20162
	Fox BG, Malone TE, Johnson KA, Madson SE, Aceti D, Bingman CA, Blommel PG, Buchan B, Burns B, Cao J, Cornilescu C, Doreleijers J, Ellefson J, Frederick R, Geetha H, Hruby D, Jeon WB, Kimball T, Kunert J, Markley JL, Newman C, Olson A, Peterson FC, Phillips GN Jr, Primm J, Ramirez B, Rosenberg NS, Runnels M, Seder K, Shaw J, Smith DW, Sreenath H, Song J, Sussman MR, Thao S, Troestler D, Tyler E, Tyler R, Ulrich E, Vinarov D, Vojtik F, Volkman BF, Wesenberg G, Wrobel RL, Zhang J, Zhao Q, Zolnai Z. X-ray structure of Arabidopsis At1g77680, 12-oxophytodienoate reductase isoform 1. Proteins 61 2005 206-8 [PubMed: 16080145] http://dx.doi.org/10.1002/prot.20533
	van den Hemel D, Brige A, Savvides SN, Van Beeumen J. Ligand-induced conformational changes in the capping subdomain of a bacterial old yellow enzyme homologue and conserved sequence fingerprints provide new insights into substrate binding. J. Biol. Chem. 281 2006 28152-61 [PubMed: 16857682] http://dx.doi.org/10.1074/jbc.M603946200

InterPro 23.1