D0V3Y4 · NMO_PSESP
- ProteinNitronate monooxygenase
- GenepnoA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids349 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. Acts on propionate 3-nitronate (P3N), the presumed physiological substrate. Is likely involved in the degradation of P3N, that allows Pseudomonas sp. JS189 to grow on 3-nitropropionate/P3N as the sole source of nitrogen, carbon, and energy (PubMed:20382807).
Also probably functions in the detoxification of P3N, a metabolic poison produced by plants and fungi as a defense mechanism (By similarity).
Is not active against 3-nitropropionate, nor with neutral or nitronate forms of 1-nitropropane, 2-nitropropane, nitroethane, nitromethane, 1-nitropentane, and 2-nitroethanol (PubMed:20382807).
Also probably functions in the detoxification of P3N, a metabolic poison produced by plants and fungi as a defense mechanism (By similarity).
Is not active against 3-nitropropionate, nor with neutral or nitronate forms of 1-nitropropane, 2-nitropropane, nitroethane, nitromethane, 1-nitropentane, and 2-nitroethanol (PubMed:20382807).
Miscellaneous
At physiological pH, 3-nitropropionate (3-NPA) exists in equilibrium with its conjugate base, propionate-3-nitronate (P3N).
P3N is a potent irreversible inhibitor of the key enzyme succinate dehydrogenase in the Krebs cycle and electron transport chain. P3N has been shown to be a toxic metabolite to bacteria, plants, fungi, mammals or any organism that uses succinate dehydrogenase.
Catalytic activity
- 3 propionate 3-nitronate + 3 O2 + H2O = 3 3-oxopropanoate + 2 nitrate + nitrite + H2O2 + 3 H+
Cofactor
Note: Binds 1 FMN per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
30 μM | propionate 3-nitronate |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 69 | FMN (UniProtKB | ChEBI) | |||
Binding site | 176 | FMN (UniProtKB | ChEBI) | |||
Binding site | 181 | FMN (UniProtKB | ChEBI) | |||
Binding site | 217 | FMN (UniProtKB | ChEBI) | |||
Binding site | 236-239 | FMN (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | nitronate monooxygenase activity | |
Molecular Function | nucleotide binding | |
Biological Process | response to toxic substance |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNitronate monooxygenase
- EC number
- Short namesNMO
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionD0V3Y4
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000445423 | 1-349 | Nitronate monooxygenase | ||
Expression
Induction
Constitutively expressed.
Structure
Family & Domains
Sequence similarities
Belongs to the nitronate monooxygenase family. NMO class I subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length349
- Mass (Da)36,457
- Last updated2009-12-15 v1
- ChecksumE01472F50366F6FE
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GU014557 EMBL· GenBank· DDBJ | ACX83564.1 EMBL· GenBank· DDBJ | Genomic DNA |