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ndh NADH:quinone oxidoreductase II [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946792, updated on 19-Nov-2025
Official Symbol
ndh
Official Full Name
NADH:quinone oxidoreductase II
Primary source
ECOCYC:EG10649
Locus tag
b1109
See related
ASAP:ABE-0003746
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1095
Summary
NADH:ubiquinone oxidoreductase II (NDH-2) is a type IIA NADH dehydrogenase that catalyzes the transfer of electrons from NADH to the quinone pool in the cytoplasmic membrane. [More information is available at EcoCyc: EG10649].
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Sequence:
NC_000913.3 (1166085..1167389)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene beta-N-acetylglucosaminidase Neighboring gene PF05728 family protein YcfP Neighboring gene PF05433 family protein YcfJ Neighboring gene DNA-binding transcriptional repressor ComR

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. In vitro synthesis of the respiratory NADH dehydrogenase of Escherichia coli. Role of UUG as initiation codon. Poulis MI, et al. Biochemistry, 1981 Jul 7. PMID 7025892
  2. Evidence for Cu(I)-thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2. Rapisarda VA, et al. Arch Biochem Biophys, 2002 Sep 1. PMID 12176061
  3. Quenching of bathocuproine disulfonate fluorescence by Cu(I) as a basis for copper quantification. Rapisarda VA, et al. Anal Biochem, 2002 Aug 1. PMID 12137786
  4. Purification of the 45 kDa, membrane bound NADH dehydrogenase of Escherichia coli (NDH-2) and analysis of its interaction with ubiquinone analogues. Björklöf K, et al. FEBS Lett, 2000 Feb 4. PMID 10664466
  5. Characterization of an NADH-linked cupric reductase activity from the Escherichia coli respiratory chain. Rapisarda VA, et al. Arch Biochem Biophys, 1999 Oct 15. PMID 10510271

See all (54) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Because of the specific stabilization of substrate complexes of EcNDH-2 immobilized on electrodes, it was possible to demonstrate the presence of two distinct substrate binding sites for NADH and the quinone and to identify a bound semiprotonated quinol as a catalytic intermediate.
    Title: Substrate-Protein Interactions of Type II NADH:Quinone Oxidoreductase from Escherichia coli.
  2. Improved poly(3-hydroxybutyrate) production in Escherichia coli by inactivation of cytochrome bd-II oxidase or/and NDH-II dehydrogenase in low efficient respiratory chains
    Title: Improved poly(3-hydroxybutyrate) production in Escherichia coli by inactivation of cytochrome bd-II oxidase or/and NDH-II dehydrogenase in low efficient respiratory chains.
  3. The paper reports that the maintenance of NDH-2 activity and ndh expression in the stationary phase when cells were grown in media containing at least 37 mM phosphate.
    Title: A critical phosphate concentration in the stationary phase maintains ndh gene expression and aerobic respiratory chain activity in Escherichia coli.
  4. N-terminus verified by Edman degradation on mature peptide
    Title: Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. UUG initiation codon.
Submit: New GeneRIF Correction

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables NADH dehydrogenase (quinone) (non-electrogenic) activity IEA
Inferred from Electronic Annotation
more info
  
enables NADH dehydrogenase (ubiquinone) (non-electrogenic) activity IEA
Inferred from Electronic Annotation
more info
  
enables NADH dehydrogenase (ubiquinone) activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables NADH dehydrogenase (ubiquinone) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables cupric reductase (NADH) activity IEA
Inferred from Electronic Annotation
more info
  
enables flavin adenine dinucleotide binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables oxidoreductase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within aerobic electron transport chain IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within aerobic respiration IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within anaerobic respiration IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within copper ion homeostasis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in proton transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
part_of NADH dehydrogenase complex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
Preferred Names
NADH:quinone oxidoreductase II
NP_415627.1

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1166085..1167389
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415627.1 NADH:quinone oxidoreductase II

    See identical proteins and their annotated locations for NP_415627.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A1X3JJI2, A0AAN3SDJ5
    Conserved Domains (1) summary
    COG1252
    Location:6 → 423
    Ndh; NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]
Nucleotide Protein
Heading Accession and Version

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