P17636 · FMO1_RABIT
- ProteinFlavin-containing monooxygenase 1
- GeneFMO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids535 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics (By similarity).
Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes (By similarity).
In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine (By similarity).
Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes (By similarity).
In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine (By similarity).
Catalytic activity
- H+ + hypotaurine + NADPH + O2 = H2O + NADP+ + taurineThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site, 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: SN | ||||||
Binding site | 61-62 | FAD (UniProtKB | ChEBI) | ||||
Sequence: NS | ||||||
Binding site | 195-198 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SGTD | ||||||
Site | 208 | Important for substrate binding | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | hypotaurine dehydrogenase activity | |
Molecular Function | N,N-dimethylaniline monooxygenase activity | |
Molecular Function | NADP binding | |
Molecular Function | trimethylamine monooxygenase activity | |
Biological Process | taurine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFlavin-containing monooxygenase 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionP17636
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-513 | Lumenal | ||||
Sequence: AKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYSDFPFPEDYPNYVPNSQFLDYLKMYADRFSLLKSIQFKTTVFSITKCQDFNVSGQWEVVTLHEGKQESAIFDAVMVCTGFLTNPHLPLGCFPGIKTFKGQYFHSRQYKHPDIFKDKRVLVVGMGNSGTDIAVEASHVAKKVFLSTTGGAWVISRVFDSGYPWDMVFTTRFQNFIRNSLPTPIVTWLVAKKMNSWFNHANYGLVPKDRIQLKEPVLNDELPGRIITGKVFIRPSIKEVKENSVVFGNAHNTPSEEPIDVIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAVIGLIKPLGSMLPTGETQARYTVQVFKGVIKLPPTSVMIKEVNERKENKHNGFGLCYCKALQADYITYIDDLLTSINAKPNLFSLLLTDPLLALTMFFGPYSPYQFRLTGPGKWKGARNAIMTQWDRTFKVTKTRIVQESSSP | ||||||
Transmembrane | 514-534 | Helical | ||||
Sequence: FESLLKLFAVLALLVSVFLIF | ||||||
Topological domain | 535 | Cytoplasmic | ||||
Sequence: L |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000147642 | 2-535 | Flavin-containing monooxygenase 1 | |||
Sequence: AKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYSDFPFPEDYPNYVPNSQFLDYLKMYADRFSLLKSIQFKTTVFSITKCQDFNVSGQWEVVTLHEGKQESAIFDAVMVCTGFLTNPHLPLGCFPGIKTFKGQYFHSRQYKHPDIFKDKRVLVVGMGNSGTDIAVEASHVAKKVFLSTTGGAWVISRVFDSGYPWDMVFTTRFQNFIRNSLPTPIVTWLVAKKMNSWFNHANYGLVPKDRIQLKEPVLNDELPGRIITGKVFIRPSIKEVKENSVVFGNAHNTPSEEPIDVIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAVIGLIKPLGSMLPTGETQARYTVQVFKGVIKLPPTSVMIKEVNERKENKHNGFGLCYCKALQADYITYIDDLLTSINAKPNLFSLLLTDPLLALTMFFGPYSPYQFRLTGPGKWKGARNAIMTQWDRTFKVTKTRIVQESSSPFESLLKLFAVLALLVSVFLIFL |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Liver.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length535
- Mass (Da)60,183
- Last updated2007-01-23 v3
- Checksum8EE95683FC3E43D5
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 20 | in Ref. 2; AA sequence and 3; AA sequence | ||||
Sequence: C → S | ||||||
Sequence conflict | 27 | in Ref. 2; AA sequence and 3; AA sequence | ||||
Sequence: E → K | ||||||
Sequence conflict | 99 | in Ref. 2; AA sequence | ||||
Sequence: S → D | ||||||
Sequence conflict | 103 | in Ref. 2; AA sequence | ||||
Sequence: S → E | ||||||
Sequence conflict | 116 | in Ref. 2; AA sequence | ||||
Sequence: C → E | ||||||
Sequence conflict | 126 | in Ref. 2; AA sequence | ||||
Sequence: E → K | ||||||
Sequence conflict | 279 | in Ref. 2; AA sequence | ||||
Sequence: L → M | ||||||
Sequence conflict | 340 | in Ref. 2; AA sequence | ||||
Sequence: F → S | ||||||
Sequence conflict | 406 | in Ref. 2; AA sequence | ||||
Sequence: S → C | ||||||
Sequence conflict | 455 | in Ref. 2; AA sequence | ||||
Sequence: L → S | ||||||
Sequence conflict | 457 | in Ref. 2; AA sequence | ||||
Sequence: L → G | ||||||
Sequence conflict | 535 | in Ref. 2; AA sequence | ||||
Sequence: L → LES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M32030 EMBL· GenBank· DDBJ | AAA31278.1 EMBL· GenBank· DDBJ | mRNA |