B8EIZ7 · TMM_METSB

Function

function

Catalyzes the oxidation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) (PubMed:22006322).
In vitro, has a broad substrate specificity, oxidizing many nitrogen- and sulfur-containing compounds, including dimethylamine (DMA), dimethylsulfide (DMS), dimethylsulfoxide (DMSO), cysteamine, methimazole and dimethylaniline (PubMed:22006322).

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
9.4 μMTMA
89.7 μMDMA
10.3 μMDMS
3575 μMDMSO
3139 μMcysteamine
28.2 μMmethimazole
35.7 μMdimethylaniline
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
29.4 nmol/min/mgwith TMA as substrate
6.9 nmol/min/mgwith DMA as substrate
34.6 nmol/min/mgwith DMS as substrate
4.8 nmol/min/mgwith DMSO as substrate
76.2 nmol/min/mgwith cysteamine as substrate
14.4 nmol/min/mgwith methimazole as substrate
29.2 nmol/min/mgwith dimethylaniline as substrate

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site12FAD (UniProtKB | ChEBI)
Binding site37FAD (UniProtKB | ChEBI)
Binding site39FAD (UniProtKB | ChEBI)
Binding site45FAD (UniProtKB | ChEBI)
Binding site46FAD (UniProtKB | ChEBI)
Binding site62FAD (UniProtKB | ChEBI)
Binding site70NADP+ (UniProtKB | ChEBI)
Binding site72FAD (UniProtKB | ChEBI)
Binding site72NADP+ (UniProtKB | ChEBI)
Binding site125FAD (UniProtKB | ChEBI)
Binding site204NADP+ (UniProtKB | ChEBI)
Binding site205NADP+ (UniProtKB | ChEBI)
Binding site207NADP+ (UniProtKB | ChEBI)
Binding site228NADP+ (UniProtKB | ChEBI)
Binding site317FAD (UniProtKB | ChEBI)
Binding site320FAD (UniProtKB | ChEBI)
Binding site411NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionhypotaurine dehydrogenase activity
Molecular FunctionN,N-dimethylaniline monooxygenase activity
Molecular FunctionNADP binding
Molecular Functiontrimethylamine monooxygenase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Trimethylamine monooxygenase
  • EC number
  • Short names
    TMA monooxygenase
    ; Tmm

Gene names

    • Name
      tmm
    • Ordered locus names
      Msil_3604

Organism names

Accessions

  • Primary accession
    B8EIZ7

Proteomes

Phenotypes & Variants

Disruption phenotype

Mutant cannot grow on TMA as a sole source of carbon and energy.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004580751-451Trimethylamine monooxygenase

Expression

Induction

Expression is induced by TMA.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the FMO family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    451
  • Mass (Da)
    51,699
  • Last updated
    2009-03-03 v1
  • Checksum
    E4856E54189574A3
MTRVAIIGAGPSGLAQLRAFQSAGKKGAAIPELVCFEKQSDWGGLWNYTWRTGVDEYGEPVHGSMYRYLWSNGPKECLEFADYSFEEHFGRPIPSYPPRAVLHDYIMGRVEKSDVRKFVRFSTVVRWIDFDETTQLFTVTVKDLKKDELYSETFDYVVVASGHFSTPNVPHFPGIEVFPGRVLHAHDFRDANEFVGKNLLVVGSSYSAEDIASQCYKYGAKSITFSYRSKPLNFDWPECFTVKPLLTKLTGKTAHFKDGSEAVVDAVLLCTGYLHHFPFLADNLRLKTNNRLYPAGLYKGIFWQDNPKLIYLGMQDQYFTFNMFDAQAWYARDVILGRIKLPAAEERQADIDHWRGLEEKLETAFDGIDFQTEYMRDLIPATDYPMFDLDKVAALFKEWEEDKVKSIMGYRDNSYVSIMTGNKAPPHHTKWMEALDDSFDAFQNRPEAAAE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001280
EMBL· GenBank· DDBJ
ACK52489.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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