A0A6F8UPW0 · A0A6F8UPW0_9HYPH
- ProteinFMN dependent NADH:quinone oxidoreductase
- GeneazoR
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids201 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones.
Catalytic activity
- 2 a quinone + NADH + H+ = 2 a 1,4-benzosemiquinone + NAD+
Cofactor
Note: Binds 1 FMN per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 10 | FMN (UniProtKB | ChEBI) | |||
Binding site | 16-18 | FMN (UniProtKB | ChEBI) | |||
Binding site | 95-98 | FMN (UniProtKB | ChEBI) | |||
Binding site | 139-142 | FMN (UniProtKB | ChEBI) | |||
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 |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFMN dependent NADH:quinone oxidoreductase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Boseaceae > Bosea
Accessions
- Primary accessionA0A6F8UPW0
Proteomes
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length201
- Mass (Da)21,348
- Last updated2020-08-12 v1
- Checksum3C7E1292732EFE6B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP022848 EMBL· GenBank· DDBJ | BCB17859.1 EMBL· GenBank· DDBJ | Genomic DNA |