Flavin monooxygenase (FMO) 1 (IPR002253)

Short name: Flavin_mOase_1

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, phosphorous 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].

Human FMO1 mRNA is more abundant in foetal than in adult liver, indicating that the enzyme is subject to developmental regulation in man [PMID: 1712018]. The deduced amino sequence contains putative FAD- (GxGxxG) and NADP+-binding (GxGxxA) sites, a 'FATGY' motif that has also been observed in a range of siderphore biosynthetic enzymes [PMID: 9538688], and a C-terminal hydrophobic segment that is believed to anchor the monooxygenase to the microsomal membrane [PMID: 2355001]. The human sequence shares 88 and 86% identity, respectively, with pig and rabbit 'hepatic' forms of FMO, but is only 58% similar to the abbit 'pulmonary' FMO [PMID: 1712018].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0004499 N,N-dimethylaniline monooxygenase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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