P17636 · FMO1_RABIT

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).

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site9-13FAD (UniProtKB | ChEBI)
Binding site32FAD (UniProtKB | ChEBI)
Binding site40-41FAD (UniProtKB | ChEBI)
Binding site60-61NADP+ (UniProtKB | ChEBI)
Binding site61-62FAD (UniProtKB | ChEBI)
Binding site195-198NADP+ (UniProtKB | ChEBI)
Site208Important for substrate binding

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionhypotaurine dehydrogenase activity
Molecular FunctionN,N-dimethylaniline monooxygenase activity
Molecular FunctionNADP binding
Molecular Functiontrimethylamine monooxygenase activity
Biological Processtaurine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Flavin-containing monooxygenase 1
  • EC number
  • Alternative names
    • Dimethylaniline monooxygenase [N-oxide-forming] 1
    • Dimethylaniline oxidase 1
    • FMO 1A1
    • FMO form 1 (FMO 1)
    • Hepatic flavin-containing monooxygenase 1
    • Trimethylamine monooxygenase

Gene names

    • Name
      FMO1

Organism names

  • Taxonomic identifier
  • Strain
    • New Zealand white
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    P17636

Proteomes

Subcellular Location

Endoplasmic reticulum membrane
; Single-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain2-513Lumenal
Transmembrane514-534Helical
Topological domain535Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001476422-535Flavin-containing monooxygenase 1

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Liver.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the FMO family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    535
  • Mass (Da)
    60,183
  • Last updated
    2007-01-23 v3
  • Checksum
    8EE95683FC3E43D5
MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYSDFPFPEDYPNYVPNSQFLDYLKMYADRFSLLKSIQFKTTVFSITKCQDFNVSGQWEVVTLHEGKQESAIFDAVMVCTGFLTNPHLPLGCFPGIKTFKGQYFHSRQYKHPDIFKDKRVLVVGMGNSGTDIAVEASHVAKKVFLSTTGGAWVISRVFDSGYPWDMVFTTRFQNFIRNSLPTPIVTWLVAKKMNSWFNHANYGLVPKDRIQLKEPVLNDELPGRIITGKVFIRPSIKEVKENSVVFGNAHNTPSEEPIDVIVFATGYTFAFPFLDESVVKVEDGQASLYKYIFPAHLQKPTLAVIGLIKPLGSMLPTGETQARYTVQVFKGVIKLPPTSVMIKEVNERKENKHNGFGLCYCKALQADYITYIDDLLTSINAKPNLFSLLLTDPLLALTMFFGPYSPYQFRLTGPGKWKGARNAIMTQWDRTFKVTKTRIVQESSSPFESLLKLFAVLALLVSVFLIFL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict20in Ref. 2; AA sequence and 3; AA sequence
Sequence conflict27in Ref. 2; AA sequence and 3; AA sequence
Sequence conflict99in Ref. 2; AA sequence
Sequence conflict103in Ref. 2; AA sequence
Sequence conflict116in Ref. 2; AA sequence
Sequence conflict126in Ref. 2; AA sequence
Sequence conflict279in Ref. 2; AA sequence
Sequence conflict340in Ref. 2; AA sequence
Sequence conflict406in Ref. 2; AA sequence
Sequence conflict455in Ref. 2; AA sequence
Sequence conflict457in Ref. 2; AA sequence
Sequence conflict535in Ref. 2; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M32030
EMBL· GenBank· DDBJ
AAA31278.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp