| Type: | Domain | Name: | FAD linked oxidase, N-terminal |
| 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, ) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110 []. The FAD molecule is covalently bound in the knownstructure, 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. | Short Name: | Oxid_FAD_bind_N |
| DB identifier | Type | Name |
|---|---|---|
| IPR003170 | Family | UDP-N-acetylenolpyruvoylglucosamine reductase |
| IPR010030 | Family | L-gulonolactone oxidase, plant |
| IPR010029 | Family | Galactonolactone dehydrogenase |
| IPR010031 | Family | L-gulonolactone/D-arabinono-1,4-lactone oxidase |
| IPR004490 | Family | Glycolate oxidase subunit GlcD |
| IPR012256 | Family | D-lactate dehydrogenase |
| GO Term | Gene Name |
|---|---|
| GO:0016491 | IPR006094 |
| GO:0050660 | IPR006094 |
| GO:0055114 | IPR006094 |
