The domain within your query sequence starts at position 2 and ends at position 532; the E-value for the FMO-like domain shown below is 1.5e-279.



PFAM accession number:PF00743
Interpro abstract (IPR020946):

Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes [(PUBMED: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 [(PUBMED:1712018), (PUBMED:2318837), (PUBMED:1542660), (PUBMED:1417778), (PUBMED: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 [(PUBMED:8311461)]. Following the determination of the complete nucleotide sequence of Saccharomyces cerevisiae (Baker's yeast) [(PUBMED: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 [(PUBMED:27166860)].

GO process:oxidation-reduction process (GO:0055114)
GO function:flavin adenine dinucleotide binding (GO:0050660), N,N-dimethylaniline monooxygenase activity (GO:0004499), NADP binding (GO:0050661)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry FMO-like