Q9AL95 · NROR_CLOAB
- ProteinNADH-rubredoxin oxidoreductase
- GenenroR
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids379 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the NADH-dependent reduction of rubredoxin (Rd). NADPH is a very poor electron donor compared to NADH. Functions as an intermediate component in the electron transfer chain: NADH->NROR->Rd->FprA1/2. Also functions as an intermediate component in the electron transfer chains from NADH to revRbr and Dfx. Therefore, is a key electron carrier in an efficient multienzyme complex that can scavenge O2 and reactive oxygen species (ROS), and thus plays an important role in the oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium.
Miscellaneous
The disulfide bonds are not involved in the electron transfer from NADH to rubredoxin catalyzed by NROR.
Catalytic activity
- H+ + NAD+ + 2 reduced [rubredoxin] = NADH + 2 oxidized [rubredoxin]
Cofactor
Note: Binds 1 FAD per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1 μM | rubredoxin | |||||
17.4 μM | NADH | |||||
2070 μM | NADPH |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
570 μmol/min/mg | with rubredoxin and NADH as substrates |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | electron transfer activity | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | rubredoxin-NAD+ reductase activity | |
Biological Process | oxygen metabolic process | |
Biological Process | response to toxic substance |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADH-rubredoxin oxidoreductase
- EC number
- Short namesNROR
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionQ9AL95
Proteomes
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000405536 | 1-379 | NADH-rubredoxin oxidoreductase | |||
Sequence: MKSTKILILGAGPAGFSAAKAALGKCDDITMINSEKYLPYYRPRLNEIIAKNKSIDDILIKKNDWYEKNNIKVITSEFATSIDPNNKLVTLKSGEKIKYEKLIIASGSIANKIKVPHADEIFSLYSYDDALKIKDECKNKGKAFIIGGGILGIELAQAIIDSGTPASIGIILEYPLERQLDRDGGLFLKDKLDRLGIKIYTNSNFEEMGDLIRSSCVITAVGVKPNLDFIKDTEIASKRGILVNDHMETSIKDIYACGDVAEFYGKNPGLINIANKQGEVAGLNACGEDASYSEIIPSPILKVSGISIISCGDIENNKPSKVFRSTQEDKYIVCMLKENKIDAAAVIGDVSLGTKLKKAIDSSKSFDNISSLDAILNNL | ||||||
Disulfide bond | 26↔286 | |||||
Sequence: CDDITMINSEKYLPYYRPRLNEIIAKNKSIDDILIKKNDWYEKNNIKVITSEFATSIDPNNKLVTLKSGEKIKYEKLIIASGSIANKIKVPHADEIFSLYSYDDALKIKDECKNKGKAFIIGGGILGIELAQAIIDSGTPASIGIILEYPLERQLDRDGGLFLKDKLDRLGIKIYTNSNFEEMGDLIRSSCVITAVGVKPNLDFIKDTEIASKRGILVNDHMETSIKDIYACGDVAEFYGKNPGLINIANKQGEVAGLNAC | ||||||
Disulfide bond | 137↔216 | |||||
Sequence: CKNKGKAFIIGGGILGIELAQAIIDSGTPASIGIILEYPLERQLDRDGGLFLKDKLDRLGIKIYTNSNFEEMGDLIRSSC |
Keywords
- PTM
Expression
Induction
Up-regulated upon exposure to O2. Repressed by PerR.
Interaction
Structure
Family & Domains
Domain
Is composed of three domains: an FAD-binding domain (residues 2-107 and 223-297), an NADH-binding domain (residues 108-222), and a C-terminal domain (residues 298-379).
Sequence similarities
Belongs to the FAD-dependent oxidoreductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length379
- Mass (Da)41,286
- Last updated2001-06-01 v1
- Checksum08C83695DB7FE3E9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY026492 EMBL· GenBank· DDBJ | AAK08126.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE001437 EMBL· GenBank· DDBJ | AAK80402.1 EMBL· GenBank· DDBJ | Genomic DNA |