Q9AL95 · NROR_CLOAB

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

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1 μMrubredoxin
17.4 μMNADH
2070 μMNADPH
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
570 μmol/min/mgwith rubredoxin and NADH as substrates

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site33-35FAD (UniProtKB | ChEBI)
Binding site42FAD (UniProtKB | ChEBI)
Binding site79FAD (UniProtKB | ChEBI)
Binding site125FAD (UniProtKB | ChEBI)
Binding site259FAD (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionelectron transfer activity
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionrubredoxin-NAD+ reductase activity
Biological Processoxygen metabolic process
Biological Processresponse to toxic substance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NADH-rubredoxin oxidoreductase
  • EC number
  • Short names
    NROR
  • Alternative names
    • NADH:rubredoxin oxidoreductase

Gene names

    • Name
      nroR
    • Ordered locus names
      CA_C2448

Organism names

Accessions

  • Primary accession
    Q9AL95

Proteomes

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00004055361-379NADH-rubredoxin oxidoreductase
Disulfide bond26↔286
Disulfide bond137↔216

Keywords

Expression

Induction

Up-regulated upon exposure to O2. Repressed by PerR.

Interaction

Subunit

Monomer.

Protein-protein interaction databases

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    379
  • Mass (Da)
    41,286
  • Last updated
    2001-06-01 v1
  • Checksum
    08C83695DB7FE3E9
MKSTKILILGAGPAGFSAAKAALGKCDDITMINSEKYLPYYRPRLNEIIAKNKSIDDILIKKNDWYEKNNIKVITSEFATSIDPNNKLVTLKSGEKIKYEKLIIASGSIANKIKVPHADEIFSLYSYDDALKIKDECKNKGKAFIIGGGILGIELAQAIIDSGTPASIGIILEYPLERQLDRDGGLFLKDKLDRLGIKIYTNSNFEEMGDLIRSSCVITAVGVKPNLDFIKDTEIASKRGILVNDHMETSIKDIYACGDVAEFYGKNPGLINIANKQGEVAGLNACGEDASYSEIIPSPILKVSGISIISCGDIENNKPSKVFRSTQEDKYIVCMLKENKIDAAAVIGDVSLGTKLKKAIDSSKSFDNISSLDAILNNL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY026492
EMBL· GenBank· DDBJ
AAK08126.1
EMBL· GenBank· DDBJ
Genomic DNA
AE001437
EMBL· GenBank· DDBJ
AAK80402.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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