FAD linked oxidase, N-terminal (IPR006094)

Short name: Oxid_FAD_bind_N

Overlapping homologous superfamilies

Domain relationships


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: has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 [PMID: 10984479]. 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.

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0050660 flavin adenine dinucleotide binding
GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.