B8EIZ7 · TMM_METSB
- ProteinTrimethylamine monooxygenase
- Genetmm
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids451 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- NADPH + O2 + trimethylamine = H2O + NADP+ + trimethylamine N-oxideThis reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
9.4 μM | TMA | |||||
89.7 μM | DMA | |||||
10.3 μM | DMS | |||||
3575 μM | DMSO | |||||
3139 μM | cysteamine | |||||
28.2 μM | methimazole | |||||
35.7 μM | dimethylaniline |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
29.4 nmol/min/mg | with TMA as substrate | ||||
6.9 nmol/min/mg | with DMA as substrate | ||||
34.6 nmol/min/mg | with DMS as substrate | ||||
4.8 nmol/min/mg | with DMSO as substrate | ||||
76.2 nmol/min/mg | with cysteamine as substrate | ||||
14.4 nmol/min/mg | with methimazole as substrate | ||||
29.2 nmol/min/mg | with dimethylaniline as substrate |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 12 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 37 | FAD (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 39 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 45 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 46 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 62 | FAD (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 70 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 72 | FAD (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 72 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 125 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 204 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 205 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 207 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 228 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 317 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 320 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 411 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
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 |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTrimethylamine monooxygenase
- EC number
- Short namesTMA monooxygenase ; Tmm
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Beijerinckiaceae > Methylocella
Accessions
- Primary accessionB8EIZ7
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458075 | 1-451 | Trimethylamine monooxygenase | |||
Sequence: MTRVAIIGAGPSGLAQLRAFQSAGKKGAAIPELVCFEKQSDWGGLWNYTWRTGVDEYGEPVHGSMYRYLWSNGPKECLEFADYSFEEHFGRPIPSYPPRAVLHDYIMGRVEKSDVRKFVRFSTVVRWIDFDETTQLFTVTVKDLKKDELYSETFDYVVVASGHFSTPNVPHFPGIEVFPGRVLHAHDFRDANEFVGKNLLVVGSSYSAEDIASQCYKYGAKSITFSYRSKPLNFDWPECFTVKPLLTKLTGKTAHFKDGSEAVVDAVLLCTGYLHHFPFLADNLRLKTNNRLYPAGLYKGIFWQDNPKLIYLGMQDQYFTFNMFDAQAWYARDVILGRIKLPAAEERQADIDHWRGLEEKLETAFDGIDFQTEYMRDLIPATDYPMFDLDKVAALFKEWEEDKVKSIMGYRDNSYVSIMTGNKAPPHHTKWMEALDDSFDAFQNRPEAAAE |
Expression
Induction
Expression is induced by TMA.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length451
- Mass (Da)51,699
- Last updated2009-03-03 v1
- ChecksumE4856E54189574A3
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001280 EMBL· GenBank· DDBJ | ACK52489.1 EMBL· GenBank· DDBJ | Genomic DNA |