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

Gene ID: 945540, updated on 6-Jul-2026
Official Symbol
nuoL
Official Full Name
NADH:quinone oxidoreductase subunit L
Primary source
ECOCYC:EG12092
Locus tag
b2278
See related
ASAP:ABE-0007532
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
ECK2272
Summary
NuoL and NuoM are located at the distal end of the membrane arm. the redox centers are in the peripheral arm. [More information is available at EcoGene: EG12092]. NuoL is part of the inner membrane component of NADH dehydrogenase I . [More information is available at EcoCyc: EG12092].
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Sequence:
NC_000913.3 (2393205..2395046, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene NADH:quinone oxidoreductase subunit N Neighboring gene NADH:quinone oxidoreductase subunit M Neighboring gene NADH:quinone oxidoreductase subunit K Neighboring gene NADH:quinone oxidoreductase subunit J Neighboring gene NADH:quinone oxidoreductase subunit I

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation. Zhu S, et al. J Biol Chem, 2015 Aug 21. PMID 26134569, Free PMC Article
  2. Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I. Steimle S, et al. FEBS Lett, 2012 Mar 23. PMID 22326235
  3. Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Narayanan M, et al. J Biochem, 2016 Oct. PMID 27118783, Free PMC Article
  4. Probing the mechanistic role of the long α-helix in subunit L of respiratory Complex I from Escherichia coli by site-directed mutagenesis. Belevich G, et al. Mol Microbiol, 2011 Dec. PMID 22060017, Free PMC Article
  5. Role of subunit NuoL for proton translocation by respiratory complex I. Steimle S, et al. Biochemistry, 2011 Apr 26. PMID 21417432

See all (86) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. NuoL is involved in the high efficiency pumping mechanism in complex I.
    Title: Roles of subunit NuoL in the proton pumping coupling mechanism of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.
  2. The results do not support the hypothesis that the lateral helix of the NuoL subunit functions like a piston.
    Title: Constraining the Lateral Helix of Respiratory Complex I by Cross-linking Does Not Impair Enzyme Activity or Proton Translocation.
  3. To explore the functional relevance of the pseudosymmetric inverted-repeat structures of the antiporter-like subunits NuoL/M/N, we constructed a symmetry-related structure of a possible alternate-access state.
    Title: Electrostatics, hydration, and proton transfer dynamics in the membrane domain of respiratory complex I.
  4. Data show that the mutation of the conserved amino acid D563(L), which is part of the horizontal helix of the Escherichia coli complex I subunit NuoL, leads to a reduced H(+)/e(-) stoichiometry.
    Title: Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I.
  5. NuoL was truncated at its C- and N-termini, which resulted in low production of a fragile Complex I with negligible activity.
    Title: Probing the mechanistic role of the long α-helix in subunit L of respiratory Complex I from Escherichia coli by site-directed mutagenesis.
  6. 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.
  7. 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.
  8. the membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I
    Title: The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I.
  9. Data show that subunits NuoL and M jointly occupy a distal half of the membrane domain of respiratory complex I, separated by about 10nm from the interface with the peripheral arm.
    Title: Single particle analysis confirms distal location of subunits NuoL and NuoM in Escherichia coli complex I.
  10. An antiporter related subunit of NADH dehydrogenase I produced in Saccharomyces cerevisiae functions as transporter of Na+ and K+.
    Title: Transport of Na(+) and K (+) by an antiporter-related subunit from the Escherichia coli NADH dehydrogenase I produced in Saccharomyces cerevisiae.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

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 activity IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in ATP synthesis coupled electron transport IEA
Inferred from Electronic Annotation
more info
  
involved_in electron transport coupled proton transport IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in 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 plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
part_of respiratory chain complex I IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of respiratory chain complex I IDA
Inferred from Direct Assay
more info
 PubMed 
part_of 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 
Preferred Names
NADH:quinone oxidoreductase subunit L
NP_416781.1

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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
    2393205..2395046 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416781.1 NADH:quinone oxidoreductase subunit L

    See identical proteins and their annotated locations for NP_416781.1

    Status: REVIEWED

    Conserved Domains (1) summary
    PRK06590
    Location:1 → 601
    PRK06590; NADH:ubiquinone oxidoreductase subunit L; Reviewed
Nucleotide Protein
Heading Accession and Version

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