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

Gene ID: 946753, updated on 11-Apr-2024

Summary

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Gene symbol
nuoF
Gene description
NADH:quinone oxidoreductase subunit F
Primary source
ASAP:ABE-0007545
Locus tag
b2284
See related
ECOCYC:EG11774
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].
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Genomic context

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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

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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. 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

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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
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 iron-sulfur cluster binding IEA
Inferred from Electronic Annotation
more info
  
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 respiratory electron transport chain IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in 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 membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
part_of plasma membrane respiratory chain complex I IBA
Inferred from Biological aspect of Ancestor
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 IEA
Inferred from Electronic Annotation
more info
  
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 F
NP_416787.1

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
    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
    A0A5B9A8I1
    Conserved Domains (1) summary
    PRK11278
    Location:1 → 445
    PRK11278; NADH-quinone oxidoreductase subunit NuoF
Nucleotide Protein
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