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pfkB 6-phosphofructokinase 2 [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946230, updated on 23-Nov-2023

Summary

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Gene symbol
pfkB
Gene description
6-phosphofructokinase 2
Primary source
ECOCYC:EG10700
Locus tag
b1723
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
ECK1721
Summary
A promoter activation mutation increases expression and suppresses pfkA mutations. [More information is available at EcoGene: EG10700]. Phosphofructokinase (Pfk) catalyzes the phosphorylation of fructose-6-phosphate on the C1 carbon during glycolysis. [More information is available at EcoCyc: EG10700].
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Genomic context

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Sequence:
NC_000913.3 (1806370..1807299)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein YniD Neighboring gene acid-inducible putative outer membrane protein YdiY Neighboring gene putative endoribonuclease YdiZ Neighboring gene putative kinase YniA

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. Regulatory network of the allosteric ATP inhibition of E. coli phosphofructokinase-2 studied by hybrid dimers. Villalobos P, et al. Biochimie, 2016 Sep-Oct. PMID 27591700
  2. Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization. Baez M, et al. FEBS Lett, 2011 Jul 21. PMID 21627967
  3. Ribokinase family evolution and the role of conserved residues at the active site of the PfkB subfamily representative, Pfk-2 from Escherichia coli. Cabrera R, et al. Arch Biochem Biophys, 2010 Oct 1. PMID 20599671
  4. Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability. Baez M, et al. FEBS Lett, 2009 Jun 18. PMID 19465020
  5. Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition. Cabrera R, et al. J Mol Biol, 2008 Nov 14. PMID 18762190

See all (46) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Data show that interactions between fructose-6-P and allosteric sites for ATP are operating within and between the phosphofructokinase-2 (Pfk-2) subunits.
    Title: Regulatory network of the allosteric ATP inhibition of E. coli phosphofructokinase-2 studied by hybrid dimers.
  2. Data show an unstructured monomeric phosphofructokinase-2 intermediate and that most part of the dimer structure is reached as a slow concerted folding/association step with a quite folded transition state in terms of solvent exposure.
    Title: Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization.
  3. Site-directed mutagenesis of R90 and D256 indicate that R90 participates in the binding of the phosphorylated substrate and that D256 is involved in the phosphoryl transfer mechanism.
    Title: Ribokinase family evolution and the role of conserved residues at the active site of the PfkB subfamily representative, Pfk-2 from Escherichia coli.
  4. Pfk-2 undergoes a cooperative unfolding/dissociation process with the accumulation of an expanded and unstructured monomeric intermediate with a marginal stability and a large solvent accessibility with respect to the native dimer.
    Title: Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability.
  5. Results describe the structure of phosphofructokinase-2 in its inhibited tetrameric form, with each subunit bound to two ATP molecules and two Mg ions.
    Title: Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition.
  6. N-terminus verified by Edman degradation on mature peptide
    Title: Molecular cloning of the gene for phosphofructokinase-2 of Escherichia coli and the nature of a mutation, pfkB1, causing a high level of the enzyme.
  7. the dimeric state of Pfk-2 is critical for the stability and the activity of the enzyme
    Title: Role of Cys-295 on subunit interactions and allosteric regulation of phosphofructokinase-2 from Escherichia coli.
  8. Subunit contacts are critical for the maintenance of the overall structure of Pfk-2 and for the binding of ligands, explaining the reported importance of the dimeric state for enzymatic activity.
    Title: Unfolding pathway of the dimeric and tetrameric forms of phosphofructokinase-2 from Escherichia coli.
  9. The structure of E. coli phosphofructokinase Pfk-2 has been solved by X-ray diffraction.
    Title: Crystallization and preliminary crystallographic analysis of the tetrameric form of phosphofructokinase-2 from Escherichia coli, a member of the ribokinase family.
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 6-phosphofructokinase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 6-phosphofructokinase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 6-phosphofructokinase activity IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables kinase activity IEA
Inferred from Electronic Annotation
more info
  
enables magnesium ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables phosphotransferase activity, alcohol group as acceptor IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tagatose-6-phosphate kinase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables transferase activity IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity, transferring phosphorus-containing groups IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within DNA damage response IEP
Inferred from Expression Pattern
more info
 PubMed 
involved_in carbohydrate metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in glycolytic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within glycolytic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in glycolytic process through fructose-6-phosphate IEA
Inferred from Electronic Annotation
more info
  
involved_in phosphorylation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
6-phosphofructokinase 2
NP_416237.3

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
    1806370..1807299
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416237.3 6-phosphofructokinase 2 [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416237.3

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A1X3JGL3, A0A376WXW1
    Conserved Domains (1) summary
    PRK10294
    Location:1 → 309
    PRK10294; 6-phosphofructokinase 2; Provisional
Nucleotide Protein
Heading Accession and Version

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