P16549 · FMO1_PIG
- ProteinFlavin-containing monooxygenase 1
- GeneFMO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids532 (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 (PubMed:7758472).
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 | NADPH oxidation | |
Biological Process | organic acid metabolic process | |
Biological Process | taurine biosynthetic process | |
Biological Process | toxin metabolic 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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionP16549
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 | 2-510 | Lumenal | ||||
Sequence: AKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYPDFPFPEDYPNYVPNSHFLEYLRMYANQFNLLKCIQFKTKVCSVTKHEDFNTTGQWDVVTLCEGKQESAVFDAVMVCTGFLTNPYLPLDSFPGINTFKGQYFHSRQYKHPDIFKDKSVLVVGMGNSGTDIAVEASHLAKKVFLSTTGGAWVISRVFDSGYPWDMVFMTRFQNMFRNSLPTPIVNWLIAKKMNSWFNHANYGLIPEDRIQLREPVLNDELPGRIITGKVLIKPSIKEVKENSVVFNSSPEEEPIDIIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAVIGLIKPLGSLLPTGDTQARWAVRVLKGVNKLPPSSVMIQEVNTRKENKPSGFGLCYCKALQSDYIAYIDELLTYIDAKPNMFSLLLTDPHLALTIFFGPCTPYQFRLTGPGKWEGARNAIMTQWDRTFKVTKTRIVKESPSP | ||||||
Transmembrane | 511-531 | Helical | ||||
Sequence: FASLLKLFSFLALLVAIFQIF | ||||||
Topological domain | 532 | Cytoplasmic | ||||
Sequence: L |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000147641 | 2-532 | Flavin-containing monooxygenase 1 | |||
Sequence: AKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYPDFPFPEDYPNYVPNSHFLEYLRMYANQFNLLKCIQFKTKVCSVTKHEDFNTTGQWDVVTLCEGKQESAVFDAVMVCTGFLTNPYLPLDSFPGINTFKGQYFHSRQYKHPDIFKDKSVLVVGMGNSGTDIAVEASHLAKKVFLSTTGGAWVISRVFDSGYPWDMVFMTRFQNMFRNSLPTPIVNWLIAKKMNSWFNHANYGLIPEDRIQLREPVLNDELPGRIITGKVLIKPSIKEVKENSVVFNSSPEEEPIDIIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAVIGLIKPLGSLLPTGDTQARWAVRVLKGVNKLPPSSVMIQEVNTRKENKPSGFGLCYCKALQSDYIAYIDELLTYIDAKPNMFSLLLTDPHLALTIFFGPCTPYQFRLTGPGKWEGARNAIMTQWDRTFKVTKTRIVKESPSPFASLLKLFSFLALLVAIFQIFL | ||||||
Glycosylation | 120 | N-linked (GlcNAc...) (high mannose) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length532
- Mass (Da)59,952
- Last updated2007-01-23 v3
- Checksum5E475E7F2F3B8A67
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A4X1V620 | A0A4X1V620_PIG | FMO1 | 469 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M32031 EMBL· GenBank· DDBJ | AAA31033.1 EMBL· GenBank· DDBJ | mRNA |