Flavin monooxygenase (FMO) 4 (IPR002256)

Short name: Flavin_mOase_4

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. Five mammalian forms of FMO are now known and have been designated FMO1-FMO5 [PMID: 1712018, PMID: 2318837, PMID: 1542660, PMID: 1417778, PMID: 8486656].

FMO4 mRNA is present in low abundance in several foetal and adult tissues and the corresponding gene thus appears to be expressed constitutively [PMID: 8654418]. Sequence analysis reveals that FMO4 is 56% identical to FMO3; each is encoded by a single gene [PMID: 8188717]. The deduced amino acid sequence of human FM04 includes the putative FAD- (GxGxxG) and NADP+ pyrophosphate-binding (GxGxxA) sites characteristic of mammalian FMOs, 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].

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.