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Identification
HMDB Protein ID HMDBP00171
Secondary Accession Numbers
  • 5403
Name Dimethylaniline monooxygenase [N-oxide-forming] 3
Synonyms
  1. Dimethylaniline oxidase 3
  2. FMO 3
  3. FMO II
  4. FMO form 2
  5. Hepatic flavin-containing monooxygenase 3
  6. Trimethylamine monooxygenase
Gene Name FMO3
Protein Type Unknown
Biological Properties
General Function Involved in flavin-containing monooxygenase activity
Specific Function Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Plays an important role in the metabolism of trimethylamine (TMA), via the production of TMA N-oxide (TMAO). Is also able to perform S-oxidation when acting on sulfide compounds.
Pathways
  • Drug metabolism - cytochrome P450
  • Nicotine Action Pathway
  • Nicotine Metabolism Pathway
  • Tamoxifen Action Pathway
  • Tamoxifen Metabolism Pathway
Reactions
N,N-Dimethylaniline + NADPH + Oxygen → Dimethylaniline-N-oxide + NADP + Water details
Trimethylamine + NADPH + Oxygen → Trimethylamine N-oxide + NADP + Water details
Trimethylamine + NADPH + Hydrogen Ion + Oxygen → Trimethylamine N-oxide + NADP + Water details
Tamoxifen + Oxygen + NADPH + Hydrogen Ion → Tamoxifen N-oxide + NADP + Water details
GO Classification
Biological Process
small molecule metabolic process
drug metabolic process
xenobiotic metabolic process
Cellular Component
endoplasmic reticulum membrane
intrinsic to endoplasmic reticulum membrane
integral to membrane
Component
cell part
membrane part
intrinsic to membrane
intrinsic to organelle membrane
intrinsic to endoplasmic reticulum membrane
Function
binding
nucleotide binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
nadp or nadph binding
monooxygenase activity
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, nadh or nadph as one donor, and incorporation of one atom of oxygen
flavin-containing monooxygenase activity
oxidoreductase activity
fad or fadh2 binding
Molecular Function
NADP binding
flavin adenine dinucleotide binding
amino acid binding
N,N-dimethylaniline monooxygenase activity
trimethylamine monooxygenase activity
Process
metabolic process
oxidation reduction
Cellular Location
  1. Endoplasmic reticulum membrane
  2. Microsome membrane
Gene Properties
Chromosome Location 1
Locus 1q24.3
SNPs FMO3
Gene Sequence
>1599 bp
ATGGGGAAGAAAGTGGCCATCATTGGAGCTGGTGTGAGTGGCTTGGCCTCCATCAGGAGC
TGTCTGGAAGAGGGGCTGGAGCCCACCTGCTTTGAGAAGAGCAATGACATTGGGGGCCTG
TGGAAATTTTCAGACCATGCAGAGGAGGGCAGGGCTAGCATTTACAAATCAGTCTTTTCC
AACTCTTCCAAAGAGATGATGTGTTTCCCAGACTTCCCATTTCCCGATGACTTCCCCAAC
TTTATGCACAACAGCAAGATCCAGGAATATATCATTGCATTTGCCAAAGAAAAGAACCTC
CTGAAGTACATACAATTTAAGACATTTGTATCCAGTGTAAATAAACATCCTGATTTTGCA
ACTACTGGCCAGTGGGATGTTACCACTGAAAGGGATGGTAAAAAAGAATCGGCTGTCTTT
GATGCTGTAATGGTTTGTTCCGGACATCATGTGTATCCCAACCTACCAAAAGAGTCCTTT
CCAGGACTAAACCACTTTAAAGGCAAATGCTTCCACAGCAGGGACTATAAAGAACCAGGT
GTATTCAATGGAAAGCGTGTCCTGGTGGTTGGCCTGGGGAATTCGGGCTGTGATATTGCC
ACAGAACTCAGCCGCACAGCAGAACAGGTCATGATCAGTTCCAGAAGTGGCTCCTGGGTG
ATGAGCCGGGTCTGGGACAATGGTTATCCTTGGGACATGCTGCTCGTCACTCGATTTGGA
ACCTTCCTCAAGAACAATTTACCGACAGCCATCTCTGACTGGTTGTACGTGAAGCAGATG
AATGCAAGATTCAAGCATGAAAACTATGGCTTGATGCCTTTAAATGGAGTCCTGAGGAAA
GAGCCTGTATTTAACGATGAGCTCCCAGCAAGCATTCTGTGTGGCATTGTGTCCGTAAAG
CCTAACGTGAAGGAATTCACAGAGACCTCGGCCATTTTTGAGGATGGGACCATATTTGAG
GGCATTGACTGTGTAATCTTTGCAACAGGGTATAGTTTTGCCTACCCCTTCCTTGATGAG
TCTATCATCAAAAGCAGAAACAATGAGATCATTTTATTTAAAGGAGTATTTCCTCCTCTA
CTTGAGAAGTCAACCATAGCAGTGATTGGCTTTGTCCAGTCCCTTGGGGCTGCCATTCCC
ACAGTTGACCTCCAGTCCCGCTGGGCAGCACAAGTAATAAAGGGAACTTGTACTTTGCCT
TCTATGGAAGACATGATGAATGATATTAATGAGAAAATGGAGAAAAAGCGCAAATGGTTT
GGCAAAAGCGAGACCATACAGACAGATTACATTGTTTATATGGATGAACTCTCCTCCTTC
ATTGGGGCAAAGCCCAACATCCCATGGCTGTTTCTCACAGATCCCAAATTGGCCATGGAA
GTTTATTTTGGCCCTTGTAGTCCCTACCAGTTTAGGCTGGTGGGCCCAGGGCAGTGGCCA
GGAGCCAGAAATGCCATACTGACCCAGTGGGACCGGTCGTTGAAACCCATGCAGACACGA
GTGGTCGGGAGACTTCAGAAGCCTTGCTTCTTTTTCCATTGGCTGAAGCTCTTTGCAATT
CCTATTCTGTTAATCGCTGTTTTCCTTGTGTTGACCTAA
Protein Properties
Number of Residues 532
Molecular Weight 60032.975
Theoretical pI 7.783
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Dimethylaniline monooxygenase [N-oxide-forming] 3
MGKKVAIIGAGVSGLASIRSCLEEGLEPTCFEKSNDIGGLWKFSDHAEEGRASIYKSVFS
NSSKEMMCFPDFPFPDDFPNFMHNSKIQEYIIAFAKEKNLLKYIQFKTFVSSVNKHPDFA
TTGQWDVTTERDGKKESAVFDAVMVCSGHHVYPNLPKESFPGLNHFKGKCFHSRDYKEPG
VFNGKRVLVVGLGNSGCDIATELSRTAEQVMISSRSGSWVMSRVWDNGYPWDMLLVTRFG
TFLKNNLPTAISDWLYVKQMNARFKHENYGLMPLNGVLRKEPVFNDELPASILCGIVSVK
PNVKEFTETSAIFEDGTIFEGIDCVIFATGYSFAYPFLDESIIKSRNNEIILFKGVFPPL
LEKSTIAVIGFVQSLGAAIPTVDLQSRWAAQVIKGTCTLPSMEDMMNDINEKMEKKRKWF
GKSETIQTDYIVYMDELSSFIGAKPNIPWLFLTDPKLAMEVYFGPCSPYQFRLVGPGQWP
GARNAILTQWDRSLKPMQTRVVGRLQKPCFFFHWLKLFAIPILLIAVFLVLT
GenBank ID Protein 189053761
UniProtKB/Swiss-Prot ID P31513
UniProtKB/Swiss-Prot Entry Name FMO3_HUMAN
PDB IDs Not Available
GenBank Gene ID AK313197
GeneCard ID FMO3
GenAtlas ID FMO3
HGNC ID HGNC:3771
References
General References
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  4. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed:12527699 ]
  5. Lomri N, Gu Q, Cashman JR: Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1685-9. [PubMed:1542660 ]
  6. Dolphin CT, Cullingford TE, Shephard EA, Smith RL, Phillips IR: Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04. Eur J Biochem. 1996 Feb 1;235(3):683-9. [PubMed:8654418 ]
  7. Dolphin CT, Riley JH, Smith RL, Shephard EA, Phillips IR: Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA. Genomics. 1997 Dec 1;46(2):260-7. [PubMed:9417913 ]
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  14. Yeung CK, Adman ET, Rettie AE: Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria. Arch Biochem Biophys. 2007 Aug 15;464(2):251-9. Epub 2007 May 2. [PubMed:17531949 ]
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