Q9EQ76 · FMO3_RAT
- ProteinFlavin-containing monooxygenase 3
- GeneFmo3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids531 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential hepatic enzyme that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including drugs as well as dietary compounds (PubMed:3739217, PubMed:7736906).
Plays an important role in the metabolism of trimethylamine (TMA), via the production of trimethylamine N-oxide (TMAO) metabolite. TMA is generated by the action of gut microbiota using dietary precursors such as choline, choline containing compounds, betaine or L-carnitine. By regulating TMAO concentration, FMO3 directly impacts both platelet responsiveness and rate of thrombus formation
Plays an important role in the metabolism of trimethylamine (TMA), via the production of trimethylamine N-oxide (TMAO) metabolite. TMA is generated by the action of gut microbiota using dietary precursors such as choline, choline containing compounds, betaine or L-carnitine. By regulating TMAO concentration, FMO3 directly impacts both platelet responsiveness and rate of thrombus formation
Catalytic activity
- NADPH + O2 + trimethylamine = H2O + NADP+ + trimethylamine N-oxideThis reaction proceeds in the forward direction.
- (S)-nicotine + NADPH + O2 = H2O + NADP+ + trans-(S)-nicotine N(1')-oxideThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9-13 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GAGVS | ||||||
Binding site | 32 | FAD (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 40-41 | FAD (UniProtKB | ChEBI) | ||||
Sequence: LW | ||||||
Binding site | 60-61 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: TN | ||||||
Binding site | 61-62 | FAD (UniProtKB | ChEBI) | ||||
Sequence: NS | ||||||
Binding site | 195-198 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SGCD |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | albendazole monooxygenase activity | |
Molecular Function | amino acid binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | hypotaurine dehydrogenase activity | |
Molecular Function | monooxygenase activity | |
Molecular Function | N,N-dimethylaniline monooxygenase activity | |
Molecular Function | NADP binding | |
Molecular Function | trimethylamine monooxygenase activity | |
Biological Process | taurine biosynthetic process | |
Biological Process | xenobiotic metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFlavin-containing monooxygenase 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ9EQ76
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Microsome membrane ; Single-pass membrane protein
Endoplasmic reticulum membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 511-531 | Helical | ||||
Sequence: YSHFLRLLAVPVLIALFLVLI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000147659 | 1-531 | Flavin-containing monooxygenase 3 | |||
Sequence: MKRKVAVIGAGVSGLAAIRSCLEEGLEPTCFERSDDVGGLWKFSDHTEEGRASIYQSVFTNSSKEMMCFPDFPYPDDFPNFMHNSKLQEYITSFATEKNLLKYIQFETLVTRINKCPDFSTTGKWEVTTEKNSKKETAVFDAVMICSGHHVYPHLPKDSFPGLNRFKGKCFHSRDYKEPGTWKGKRVLVIGLGNSGCDIAAELSHVAQQVIISSRSGSWVMSRVWNDGYPWDMVVITRFQTFLKNNLPTAISDWWYMKQMNARFKHENYGLMPLNGTLRKEPVFNDELPARILCGTVSIKPNVKEFTETSAVFEDGTVFEGIDCVIFATGYGYAYPFLDDSIIKSRNNEVTLYKGIFPPQLEKPTMAVIGLVQSLGAAIPTTDLQARWAAQVIRGTCILPSVNDMMDDIDEKMGKKLKWFGNSTTIQTDYIVYMDELASFIGAKPNILWLFLKDPRLAIEVFFGPCSPYQFRLVGPGKWSGARNAILTQWDRSLKPMKTRVVGGIQKPCLYSHFLRLLAVPVLIALFLVLI | ||||||
Modified residue | 401 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in liver and kidney (at protein level) (PubMed:19307449).
Expressed in kidney and liver. Weakly expressed in lung. Does not seem to be expressed in brain, adipose tissue, or muscle
Expressed in kidney and liver. Weakly expressed in lung. Does not seem to be expressed in brain, adipose tissue, or muscle
Structure
Sequence
- Sequence statusComplete
- Length531
- Mass (Da)59,960
- Last updated2001-03-01 v1
- Checksum35A89988323B311F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JSI0 | A0A0G2JSI0_RAT | Fmo3 | 531 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 501 | in Ref. 2; AAH87008 | ||||
Sequence: V → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF286595 EMBL· GenBank· DDBJ | AAG44891.1 EMBL· GenBank· DDBJ | mRNA | ||
BC087008 EMBL· GenBank· DDBJ | AAH87008.1 EMBL· GenBank· DDBJ | mRNA |