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0FMO3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameFMO3
DescriptionDimethylaniline monooxygenase 3 (ec 1.14.13.8) (hepatic flavin-containing monooxygenase 3) (fmo 3) (dimethylaniline oxidase 3) (fmo form 2) (fmo ii).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005792 microsome (TAS)
0004499 dimethylaniline monooxygenase (N-oxide-form... (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes . Using an NADPH cofactor and FAD prosthetic group.hese microsomal proteins catalyse the oxygenation of nucleophilic nitrogen.ulphur.hosphorous and selenium atoms in a range of structurally diverse compounds. FMOs have been implicated in the metabolism of a number of pharmaceuticals.esticides and toxicants. In man.ack 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 . This is a recent nomenclature based on comparison of amino acid sequences.nd has been introduced in an attempt to eliminate confusion inherent in multiple.aboratory-specific designations and tissue-based classifications . Following the determination of the complete nucleotide sequence of S. cerevisiae . novel gene was found to encode a protein with similarity to mammalian monooygenases.
  IPR000960:Flavin-containing monooxygenase FMO
Mitochondrial P450-containing systems comprise 3 components.n FAD-containing flavoprotein NADPH:adrenodoxin reductase (AR); an iron-sulphur protein.drenodoxin; and P450 . The direction of electron flow is NADPH to AR to adrenodoxin to P450. FAD can be reduced by 2 electrons from NADPH.hich are transferred one at a time to adrenodoxin. one-electron carrier. Both AR and adrenodoxin are soluble proteins located on the matrix side of the inner mitochondrial membrane. Despite functional parallels.R shows no global similarity either to flavoprotein pyridine nucleotide cytochrome reductases (FPNCR) or to FAD-dependent pyridine nucleotide reductases (FADPNR) . However.LAST searches reveal local similarity of the N-terminal region of AR to glutamate synthase and NADH peroxidase.specially in the nucleotide-binding regions.uggesting that AR and FADPNR may be distantly related.
  IPR000759:Adrenodoxin reductase
The pyridine nucleotide-disulphide reductases (PNDR) use the isoalloxazine ring of FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step.he reduced disulphide reduces the substrate. On the basis of sequence and structural similarities .NDR can be categorised into 2 groups. Class I includes glutathione reductase.rypanothione reductase.ipoamide dehydrogenase and mercuric reductase. They cover a wide range of catalytic functions: glutathione reductase ensures that the cell has enough reduced glutathione to maintain protein thiol groups in the reduced state ; trypanothione reductase carries out the analogous reaction in trypanosomal cells (trypanothione is an analogue of glutathione) ; lipoamide dehydrogenase.he E3 component of alpha-ketoacid dehydrogenase multienzyme complex.xidises the dihydrolypoyl groups of lipoate acyltransferase.nd so couples glycolysis to the tricarboxylic acid cycle ; and mercuric reductase enables bacteria to detoxify the mercuric ion by reducing it to elemental mercury.hich evaporates from the cell .
  IPR001100:Pyridine nucleotide-disulphide oxidoreductase, class I
Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic-metabolising enzymes . Using an NADPH cofactor and FAD prosthetic group.hese microsomal proteins catalyse the oxygenation of nucleophilic nitrogen.ulphur.hosphorous and selenium atoms in a range of structurally diversecompounds. Five mammalian forms of FMO are now known and have been designatedFMO1-FMO5 .The mRNA encoding FMO3 is abundant in adult liver and is also present.nlow abundance.n some foetal tissues. Thus.ike FMO1.MO3 is subjectto developmental and tissue-specific regulation.ith a developmental switchin the expression of the genes taking place in the liver . The deduced amino acid sequence of human FM03 includes the putative FAD-(GxGxxG) and NADP+ pyrophosphate-binding (GxGxxA) sites characteristic ofmammalian FMOs . FATGY motif that has also been observed in a rangeof siderphore biosynthetic enzymes .nd a C-terminal hydrophobic segment that is believed to anchor the monooxygenase to the microsomal membrane .Mutations in human FMO3 impair N-oxygenation of xenobiotics and are responsible for the trimethylaminuria phenotype . Three disease-causingmutations have been identified. Nonsense and missense mutations are associated with a severe phenotype and are also implicated in impairedmetabolism of other nitrogen- and sulphur-containing substrates.ncludingbiogenic amines.oth clinically and when mutated proteins expressed fromcDNA are studied in vitro . Human FMO3 thus plays a critical role in themetabolism of xenobiotic substrates and endogenous amines.
  IPR002255:Flavin-containing monooxygenase (FMO) 3
Homeodomain proteins are transcription factors that share a related DNA binding homeodomain . The homeodomain was first identified in a number of Drosophila homeotic and segmentation proteins.ut is now known to be well conserved in many other animals.ncluding vertebrates. The domain binds DNA through a helix-turn-helix (HTH) structure. The HTH motif is characterised by two alpha-helices.hich make intimate contacts with the DNA and are joined by a short turn. The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions.hich occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA. The first helix helps to stabilise the structure. Many proteins contain homeodomains.ncluding Drosophila Engrailed.east mating type proteins.epatocyte nuclear factor 1a and HOX proteins.The homeodomain motif is very similar in sequence and structure to domains in a wide range of DNA-binding proteins.ncluding recombinases.yb proteins.ARP response regulators.uman telomeric proteins (hTRF1).aired domain proteins (PAX).east RAP1.entromere-binding proteins CENP-B and ABP-1.ranscriptional regulators (TyrR).raC-type transcriptional activators.nd tetracycline repressor-like proteins (TetR.acR.cdC) .
  IPR009057:Homeodomain-like
This group represents dimethylaniline monooxygenase (N-oxide-forming) .
  IPR012143:Dimethylaniline monooxygenase, N-oxide-forming
This entry describes both class I and class II oxidoreductases. FAD flavoproteins belonging to the family of pyridine nucleotide-disulphide oxidoreductases (glutathione reductase.rypanothione reductase.ipoamide dehydrogenase.ercuric reductase.hioredoxin reductase.lkyl hydroperoxide reductase) share sequence similarity with a number of other flavoprotein oxidoreductases.n particular with ferredoxin-NAD+ reductases involved in oxidative metabolism of a variety of hydrocarbons (rubredoxin reductase.utidaredoxin reductase.erpredoxin reductase.erredoxin-NAD+ reductase components of benzene 1.-dioxygenase.oluene 1.-dioxygenase.hlorobenzene dioxygenase.iphenyl dioxygenase).ADH oxidase and NADH peroxidase . Comparison of the crystal structures of human glutathione reductase and Escherichia coli thioredoxin reductase reveals different locations of their active sites.uggesting that the enzymes diverged from an ancestral FAD/NAD(P)H reductase and acquired their disulphide reductase activities independently . Despite functional similarities.xidoreductases of this family show no sequence similarity with adrenodoxin reductases and flavoprotein pyridine nucleotidecytochrome reductases (FPNCR) . Assuming that disulphide reductase activity emerged later.uring divergent evolution.he family can be referred to as FAD-dependent pyridine nucleotide reductases.ADPNR.To date.D structures of glutathione reductase .hioredoxin reductase .ercuric reductase .ipoamide dehydrogenase .rypanothione reductase and NADH peroxidase have been solved. The enzymes share similar tertiary structures based on a doubly-wound alpha/beta fold.ut the relative orientations of their FAD- and NAD(P)H-binding domains may vary significantly. By contrast with the FPNCR family.he folds of the FAD- and NAD(P)H-binding domains are similar.uggesting that the domains evolved by gene duplication .
  IPR013027:FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR000960:FMO-like 
Evalue:-1e+125 
Location:1-531
SequencesProtein: FMO3_HUMAN (531 aa)
mRNA: NM_001002294
Local Annotation
Synapse Ontology
Microglias, one kind of glias in CNS, are responsible for removing most of the waste and cellular debris from the CNS
sdb:0267 removing metabolic mass  (Evidence:keywords)
KO assignmentK00485
  Level 3 annotation:
    dimethylaniline monooxygenase (N-oxide forming)
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 30 residues, 169326659-169326746Exon2: 48 residues, 169328417-169328555Exon3: 65 residues, 169339549-169339738Exon4: 56 residues, 169343439-169343602Exon5: 49 residues, 169343843-169343986Exon6: 68 residues, 169346562-169346762Exon7: 120 residues, 169349770-169350126Exon8: 26 residues, 169351971-169352044Exon9: 241 residues, 169352863-169353581Exon10: 2 residues, -Jump to FMO3_HUMAN  
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