Flavin monooxygenase FMO (IPR000960)

Short name: Flavin_mOase

Overlapping homologous superfamilies

Family relationships


Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes [PMID: 8311461]. Using an NADPH cofactor and FAD prosthetic group, these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorus and selenium atoms in a range of structurally diverse compounds. FMOs have been implicated in the metabolism of a number of pharmaceuticals, pesticides and toxicants. In man, lack of hepatic FMO-catalysed trimethylamine metabolism results in trimethylaminuria (fish odour syndrome). Five mammalian forms of FMO are now known and have been designated FMO1-FMO5 [PMID: 1712018, PMID: 2318837, PMID: 1542660, PMID: 1417778, PMID: 8486656]. This is a recent nomenclature based on comparison of amino acid sequences, and has been introduced in an attempt to eliminate confusion inherent in multiple, laboratory-specific designations and tissue-based classifications [PMID: 8311461]. Following the determination of the complete nucleotide sequence of Saccharomyces cerevisiae (Baker's yeast) [PMID: 8091229], a novel gene was found to encode a protein with similarity to mammalian monooygenases. In Aspergillus, flavin-containing monooxygenases ustF1 and ustF2 are components in the biosynthesis of the antimitotic tetrapeptide ustiloxin B, a secondary metabolite. The monooxygenases modify the side chain of the intermediate S-deoxyustiloxin H [PMID: 27166860].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0004499 N,N-dimethylaniline monooxygenase activity
GO:0050661 NADP binding
GO:0050660 flavin adenine dinucleotide binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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