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nuoN NADH:quinone oxidoreductase subunit N [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945136, updated on 25-Apr-2024

Summary

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Gene symbol
nuoN
Gene description
NADH:quinone oxidoreductase subunit N
Primary source
ASAP:ABE-0007526
Locus tag
b2276
See related
ECOCYC:EG12093
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK2270
Summary
Revised ATG start codon supported by mutagenesis and sequence conservation. [More information is available at EcoGene: EG12093]. NuoN is part of the inner membrane component of NADH dehydrogenase I . [More information is available at EcoCyc: EG12093].
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Genomic context

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Sequence:
NC_000913.3 (2390048..2391505, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein YfbO Neighboring gene uncharacterized protein YfbP Neighboring gene NADH:quinone oxidoreductase subunit M Neighboring gene NADH:quinone oxidoreductase subunit L Neighboring gene NADH:quinone oxidoreductase subunit K

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Energy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2). Sato M, et al. J Biol Chem, 2013 Aug 23. PMID 23864658, Free PMC Article
  2. The transmembrane helices of the L, M, and N subunits of Complex I from E. coli can be assigned on the basis of conservation and hydrophobic moment analysis. Vik SB. FEBS Lett, 2011 Apr 20. PMID 21420404
  3. Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function. Michel J, et al. PLoS One, 2011 Feb 28. PMID 21387012, Free PMC Article
  4. Electrostatics, hydration, and proton transfer dynamics in the membrane domain of respiratory complex I. Kaila VR, et al. Proc Natl Acad Sci U S A, 2014 May 13. PMID 24778264, Free PMC Article
  5. High affinity cation-binding sites in Complex I from Escherichia coli. Euro L, et al. Biochim Biophys Acta, 2009 Aug. PMID 19261245

See all (77) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. We observe spontaneous hydration of a putative proton entry channel at the NuoN/K interface, which is sensitive to the protonation state of buried glutamic acid residues.
    Title: Electrostatics, hydration, and proton transfer dynamics in the membrane domain of respiratory complex I.
  2. Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function.
    Title: Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function.
  3. Data show that in L, M, and N subunits of Complex I, transmembrane helices 9 and 12 are predicted to form the discontinuous helices, which are likely to play a key role in function.
    Title: The transmembrane helices of the L, M, and N subunits of Complex I from E. coli can be assigned on the basis of conservation and hydrophobic moment analysis.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
contributes_to NADH dehydrogenase (ubiquinone) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables NADH dehydrogenase (ubiquinone) activity IEA
Inferred from Electronic Annotation
more info
  
contributes_to NADH dehydrogenase (ubiquinone) activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
contributes_to NADH dehydrogenase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables NADH:ubiquinone reductase (non-electrogenic) activity IEA
Inferred from Electronic Annotation
more info
  
enables quinone binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in ATP synthesis coupled electron transport IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within aerobic respiration IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within electron transport coupled proton transport IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in respiratory electron transport chain IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
part_of NADH dehydrogenase complex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
part_of plasma membrane respiratory chain complex I IDA
Inferred from Direct Assay
more info
 PubMed 
part_of plasma membrane respiratory chain complex I IMP
Inferred from Mutant Phenotype
more info
 PubMed 
part_of respiratory chain complex I NAS
Non-traceable Author Statement
more info
 PubMed 

General protein information

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Preferred Names
NADH:quinone oxidoreductase subunit N
NP_416779.2

NCBI Reference Sequences (RefSeq)

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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
    2390048..2391505 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416779.2 NADH:quinone oxidoreductase subunit N [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416779.2

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5D8MWC2, A0A6C9QAT4, A0A7D7HQ74, A0AA87EQJ8
    Conserved Domains (1) summary
    PRK05777
    Location:1 → 483
    PRK05777; NADH-quinone oxidoreductase subunit NuoN
Nucleotide Protein
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Gene LinkOut

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Other Literature Sources
Molecular Biology Databases