O32224 · AZOR2_BACSU
- ProteinFMN-dependent NADH:quinone oxidoreductase 2
- GeneazoR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids211 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones (Probable). Contributes to resistance to 2-methylhydroquinone (2-MHQ) and catechol (PubMed:17725564, PubMed:18208493).
Exhibits NADH-dependent 2,6-dichloroindophenol (DCIP) oxidoreductase activity (PubMed:17284825).
Exhibits NADH-dependent 2,6-dichloroindophenol (DCIP) oxidoreductase activity (PubMed:17284825).
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines (PubMed:17284825).
Can reduce methyl red (PubMed:17284825).
Can reduce methyl red (PubMed:17284825).
Catalytic activity
- 2 a quinone + NADH + H+ = 2 a 1,4-benzosemiquinone + NAD+
Cofactor
Note: Binds 1 FMN per subunit.
Activity regulation
Strongly inhibited by Pb2+ and weakly inhibited by Cu2+, Hg2+ and Fe2+. Stable in presence of Ag+.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
8 μM | 2,6-dichloroondophenol (DCIP) | 7.5 | 25 | |||
190 μM | NADH | 7.5 | 25 |
pH Dependence
Optimum pH is 7.5.
Temperature Dependence
Activity increases linearly up to 40 degrees Celsius. Stable up to 55 degrees Celsius after incubation for 30 minutes at pH 7.5. During incubation at 25 degrees Celsius for 16h, the enzyme is stable between pH 5.5 and 9.0, where 80% activity is observed.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | electron transfer activity | |
Molecular Function | FMN binding | |
Molecular Function | oxidoreductase activity, acting on NAD(P)H as acceptor | |
Molecular Function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor | |
Biological Process | catabolic process | |
Biological Process | response to toxic substance |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFMN-dependent NADH:quinone oxidoreductase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionO32224
Proteomes
Phenotypes & Variants
Disruption phenotype
Deletion mutant is sensitive to 2-MHQ and catechol.
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000166329 | 2-211 | FMN-dependent NADH:quinone oxidoreductase 2 | |||
Sequence: AKVLYITAHPHDEATSYSMATGKAFIESYKEANPNDEVVHIDLYKENIPHIDADVFSGWGKLQSGTGFEELSESEKAKVGRLGELSDQFASADKYVFVTPLWNFSFPPVMKAYLDSVAVAGKSFKYTEQGPVGLLTDKKAIHIQARGGYYSEGPAAEMEMGHRYIGIMMNFFGVPSFDGIFVEGHNAEPDKAQQIKEDAIARAKEAGKTF |
Proteomic databases
Expression
Induction
Repressed by MhqR. Induced by thiol specific stress conditions, such as exposure to 2-methylhydroquinone (2-MHQ), catechol or diamide. Not induced by oxidative stress due to hydrogen peroxide or methylglyoxal.
Interaction
Structure
Sequence
- Sequence statusComplete
- Length211
- Mass (Da)23,272
- Last updated1998-01-01 v1
- ChecksumDE8C5ABFDCA423C0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL009126 EMBL· GenBank· DDBJ | CAB15359.1 EMBL· GenBank· DDBJ | Genomic DNA |