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InterPro: IPR006094 FAD linked oxidase, N-terminal

Protein matches Help

UniProtKB

Matches:

9517 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

IPR006094 Oxid_FAD_bind_N

Secondary

IPR001575

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01565	FAD_binding_4	9517
Signatures in BioMart

InterPro Relationships Help

Parent

IPR016166 FAD-binding, type 2

Found in

IPR003170 UDP-N-acetylenolpyruvoylglucosamine reductase
IPR004490 Glycolate oxidase subunit GlcD
IPR010029 Galactonolactone dehydrogenase
IPR010030 Plant-specific FAD-dependent oxidoreductase
IPR010031 Sugar 1,4-lactone oxidase
IPR010032 FAD-linked oxidoreductase
IPR012256 D-lactate dehydrogenase

Contains

IPR006093 Oxygen oxidoreductase covalent FAD-binding site
IPR016167 FAD-binding, type 2, subdomain 1
IPR016168 FAD-linked oxidase, FAD-binding, subdomain 2
IPR016169 CO dehydrogenase flavoprotein-like, FAD-binding, subdomain 2

GO Term annotation Help

Function

GO:0016491 oxidoreductase activity
GO:0050660 FAD binding

InterPro annotation

Entry Details in BioMart

Abstract

Various enzymes use FAD as a co-factor, most of these enzymes are oxygen-dependent oxidoreductases, containing a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. One of the enzymes Vanillyl-alcohol oxidase (VAO, EC:1.1.3.38) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [1]. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging from aromatic amines to 4-alkylphenols.

Structural links Help

PDB - click here

SCOP: d.145.1.1 , d.145.1.2

CATH: 3.30.43.10 , 3.30.465.10 , 3.30.465.20

Database links Help

Enzyme: EC:1.1.1.158

PANDIT: PF01565

Blocks: IPB006094

Pfam Clan: CL0077.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006094

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00116 Alkyldihydroxyacetonephosphate synthase, peroxisomal

O17397 Diminuto-like protein

P32891 D-lactate dehydrogenase [cytochrome] 1, mitochondrial

P58710 L-gulonolactone oxidase

Q9V778 Alkyldihydroxyacetonephosphate synthase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR007173	D-arabinono-1,4-lactone oxidase
IPR006093	Oxygen oxidoreductase covalent FAD-binding site
IPR016168	FAD-linked oxidase, FAD-binding, subdomain 2
IPR016167	FAD-binding, type 2, subdomain 1
IPR004113	FAD-linked oxidase, C-terminal
IPR016166	FAD-binding, type 2
IPR006094	FAD linked oxidase, N-terminal
IPR016164	FAD-linked oxidase-like, C-terminal
IPR010031	Sugar 1,4-lactone oxidase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A. Structural analysis of flavinylation in vanillyl-alcohol oxidase. J. Biol. Chem. 275 38654-8 2000 [PubMed: 10984479] http://dx.doi.org/10.1074/jbc.M004753200

Additional Reading Open in usermanual
	Mattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ. Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity. Structure 5 1997 907-20 [PubMed: 9261083] http://dx.doi.org/10.1016/S0969-2126(97)00245-1
	Benson TE, Harris MS, Choi GH, Cialdella JI, Herberg JT, Martin JP Jr, Baldwin ET. A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB). Biochemistry 40 2001 2340-50 [PubMed: 11327854] http://dx.doi.org/10.1021/bi002162d
	Lim L, Molla G, Guinn N, Ghisla S, Pollegioni L, Vrielink A. Structural and kinetic analyses of the H121A mutant of cholesterol oxidase. Biochem. J. 400 2006 13-22 [PubMed: 16856877] http://dx.doi.org/10.1042/BJ20060664
	Cunane LM, Chen ZW, McIntire WS, Mathews FS. p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit. Biochemistry 44 2005 2963-73 [PubMed: 15723539] http://dx.doi.org/10.1021/bi048020r
	Benson TE, Walsh CT, Hogle JM. The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Structure 4 1996 47-54 [PubMed: 8805513] http://dx.doi.org/10.1016/S0969-2126(96)00008-1
	Malito E, Coda A, Bilyeu KD, Fraaije MW, Mattevi A. Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis. J. Mol. Biol. 341 2004 1237-49 [PubMed: 15321719] http://dx.doi.org/10.1016/j.jmb.2004.06.083
	van den Heuvel RH, van den Berg WA, Rovida S, van Berkel WJ. Laboratory-evolved vanillyl-alcohol oxidase produces natural vanillin. J. Biol. Chem. 279 2004 33492-500 [PubMed: 15169773] http://dx.doi.org/10.1074/jbc.M312968200

InterPro 24.0