A3SLM3 · TMM_ROSNI
- ProteinTrimethylamine monooxygenase
- Genetmm
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids447 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the oxidation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) (PubMed:27997715).
TMA is the best substrate, but the enzyme can also oxidize methimazole, indole and dimethylamine (DMA) (PubMed:27997715).
TMA is the best substrate, but the enzyme can also oxidize methimazole, indole and dimethylamine (DMA) (PubMed:27997715).
Miscellaneous
The catalytic process consists of a reductive half-reaction and an oxidative half-reaction, via the formation of a C4a-hydroperoxyflavin intermediate (PubMed:27997715).
NADP+ undergoes a conformational change in the oxidative half-reaction (PubMed:27997715).
NADP+ undergoes a conformational change in the oxidative half-reaction (PubMed:27997715).
Catalytic activity
- NADPH + O2 + trimethylamine = H2O + NADP+ + trimethylamine N-oxide
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
110.5 μM | TMA | |||||
123.3 μM | methimazole | |||||
244 μM | indole | |||||
164.9 μM | DMA |
kcat is 0.53 sec-1 with TMA as substrate. kcat is 0.22 sec-1 with methimazole as substrate. kcat is 0.15 sec-1 with indole as substrate. kcat is 0.17 sec-1 with DMA as substrate.
pH Dependence
Optimum pH is 8.0.
Temperature Dependence
Optimum temperature is 30 degrees Celsius.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 13 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 38 | FAD (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 40 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 46 | FAD (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 47 | FAD (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 63 | FAD (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 71 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 73 | FAD (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 73 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 126 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 173 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 205 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 206 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 208 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 229 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 318 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 321 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 413 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | N,N-dimethylaniline monooxygenase activity | |
Molecular Function | NADP binding |
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 > Rhodobacterales > Roseobacteraceae > Roseovarius
Accessions
- Primary accessionA3SLM3
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 153-154 | Has little effect on catalytic properties. | ||||
Sequence: ED → AA | ||||||
Mutagenesis | 317 | Strong decrease in activity. | ||||
Sequence: D → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458079 | 1-447 | Trimethylamine monooxygenase | |||
Sequence: MTKRVAVIGAGPSGLAQLRAFQSAADQGAEIPEIVCFEKQANWGGLWNYTWRTGLDENGEPVHCSMYRYLWSNGPKEGLEFADYSFEEHFGKQIASYPPRAVLFDYIEGRVHKADVRKWIRFNSPVRWVSYDAETAKFTVTAHNHETDSTYSEDFDHVICASGHFSTPNVPFYEGFDTFNGRIVHAHDFRDAREFEGKDVLVMGASYSAEDIGSQCWKYGAKSITSCYRSAPMGYAWPDNWEEKPALEKLTGKTAHFADGSTRDVDAIILCTGYKHFFSFLPDDLRLKTANRLATADLYKGVAYVHNPAMFYLGMQDQWFTFNMFDAQAWWVRDAILGRITLPKDKAAMLADVAERETREEASDDVKYAIRYQADYVKELVAETDYPSFDIDGACDAFFEWKKHKAKDIMAFRDNSYKSVITGTMAPVHHTPWKEALDDSMEAYLQN |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length447
- Mass (Da)50,973
- Last updated2007-04-03 v1
- Checksum931CB93F4AB01643
Keywords
- Technical term