U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

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

    Gene ID: 946753, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    nuoF
    Official Full Name
    NADH:quinone oxidoreductase subunit F
    Primary source
    ECOCYC:EG11774
    Locus tag
    b2284
    See related
    ASAP:ABE-0007545
    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
    ECK2278
    Summary
    NuoF is part of the soluble fragment of NADH dehydrogenase I, which represents the electron input part of the enzyme . [More information is available at EcoCyc: EG11774].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (2400218..2401555, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene NADH:quinone oxidoreductase subunit I Neighboring gene NADH:quinone oxidoreductase subunit H Neighboring gene NADH:quinone oxidoreductase subunit G Neighboring gene NADH:quinone oxidoreductase subunit E Neighboring gene NADH:quinone oxidoreductase subunit CD Neighboring gene NADH:quinone oxidoreductase subunit B

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Real-time optical studies of respiratory Complex I turnover. Belevich N, et al. Biochim Biophys Acta, 2014 Dec. PMID 25283488
    2. Stress-induced evolution of Escherichia coli points to original concepts in respiratory cofactor selectivity. Auriol C, et al. Proc Natl Acad Sci U S A, 2011 Jan 25. PMID 21205901, Free PMC Article
    3. Amino acid residues associated with cluster N3 in the NuoF subunit of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli. Velazquez I, et al. FEBS Lett, 2005 Jun 6. PMID 15922336
    4. Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I). Pohl T, et al. Biochim Biophys Acta, 2010 Dec. PMID 20959113
    5. Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli. Moreno-Bruna B, et al. Proc Natl Acad Sci U S A, 2001 Jul 3. PMID 11416161, Free PMC Article

    See all (64) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Data indicate that the NADH:ubiquinone oxidoreductase chain F (NuoF) E95Q variant of Complex I shows that the single amino acid replacement in the catalytic site caused a strong decrease of NADH binding.
      Title: Real-time optical studies of respiratory Complex I turnover.
    2. Data show that both NuoF mutations E183A and E183G having NADH and NADPH oxidizing ability.
      Title: Stress-induced evolution of Escherichia coli points to original concepts in respiratory cofactor selectivity.
    3. Study determined the distance between a MTSL labeled complex I variant and the bound quinone by continuous-wave (cw) EPR allowing an inference on the location of the quinone binding site.
      Title: Spin labeling of the Escherichia coli NADH ubiquinone oxidoreductase (complex I).
    4. N-terminus verified by Edman degradation on complete protein
      Title: Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli.
    5. two distinct Electron Spin Resonance Spectroscopy, arising from a [4Fe-4S] cluster (g(x,y,z)=1.90, 1.95, and 2.05) in NuoF
      Title: Amino acid residues associated with cluster N3 in the NuoF subunit of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli.
    Submit: New GeneRIF Correction

    Pathways from PubChem

    Go to the top of the page

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables 4 iron, 4 sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 4 iron, 4 sulfur cluster binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    contributes_to FMN binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables FMN binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables FMN binding ISS
    Inferred from Sequence or Structural Similarity
    more info
    		 PubMed 
    enables NAD binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables NAD binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables NAD binding ISS
    Inferred from Sequence or Structural Similarity
    more info
    		 PubMed 
    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 IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    contributes_to NADH dehydrogenase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables quinone binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in aerobic respiration IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in cellular respiration IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in proton transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 
    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 

    General protein information

    Go to the top of the page Help
    Preferred Names
    NADH:quinone oxidoreductase subunit F
    NP_416787.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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
      2400218..2401555 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416787.1 NADH:quinone oxidoreductase subunit F [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416787.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9AKU3
      Conserved Domains (1) summary
      PRK11278
      Location:1 → 445
      PRK11278; NADH-quinone oxidoreductase subunit NuoF
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.