IPR006094
FAD linked oxidase, N-terminal
InterPro entry
Short name | Oxid_FAD_bind_N |
Overlapping homologous superfamilies | |
domain relationships |
Description
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,
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. Other enzymes included in this family are MurB family members UDP-N-acetylenolpyruvoylglucosamine reductases involved in the biosynthesis of peptidoglycan
[2], D-lactate dehydrogenases among many others oxidoreductases.
References
1.Structural analysis of flavinylation in vanillyl-alcohol oxidase. Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A. J. Biol. Chem. 275, 38654-8, (2000). View articlePMID: 10984479
2.The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Benson TE, Walsh CT, Hogle JM. Structure 4, 47-54, (1996). View articlePMID: 8805513
GO terms
biological process
- None
molecular function
cellular component
- None
Cross References
ENZYME
- 1.1.1.-
- 1.1.1.436
- 1.1.2.-
- 1.1.2.4
- 1.1.3.-
- 1.1.3.20
- 1.1.3.29
- 1.1.3.37
- 1.1.3.38
- 1.1.3.41
- 1.1.3.42
- 1.1.3.45
- 1.1.3.5
- 1.1.3.8
- 1.1.5.12
- 1.1.98.3
- 1.1.99.-
- 1.1.99.14
- 1.1.99.39
- 1.1.99.40
- 1.1.99.6
- 1.17.9.1
- 1.21.3.-
- 1.21.3.3
- 1.21.3.7
- 1.21.3.8
- 1.21.99.-
- 1.3.1.72
- 1.3.1.98
- 1.3.2.3
- 1.3.3.12
- 1.3.3.14
- 1.3.3.8
- 1.5.3.-
- 1.5.3.6
- 1.5.99.12
- 2.5.1.26
- 5.5.1.-
- 5.5.1.20
Genome Properties
Contributing Member Database Entry
- Pfam:PF01565