PfkA

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  • Description: phosphofructokinase, glycolytic enzyme

Gene name pfkA
Synonyms pfk
Essential no
Product 6-phosphofructokinase
Function catabolic enzyme in glycolysis
Gene expression levels in SubtiExpress: pfkA
Interactions involving this protein in SubtInteract: PfkA
Metabolic function and regulation of this protein in SubtiPathways:
pfkA
MW, pI 34,1 kDa, 6.14
Gene length, protein length 957 bp, 319 amino acids
Immediate neighbours pyk, accA
Sequences Protein DNA DNA_with_flanks
Genetic context
PfkA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PfkA expression.png

Contents















Categories containing this gene/protein

carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU29190

Phenotypes of a mutant

  • essential according to PubMed, non-essential according to PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate (according to Swiss-Prot)
  • Protein family: phosphofructokinase family (according to Swiss-Prot) phosphofructokinase family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Allosteric Regulation (Reversible) PubMed
  • Domains:
    • 3 x nucleotide binding domain (ATP) (21–25), (154–158), (171–187)
  • Modification:
    • phosphorylated on Arg-233 PubMed
  • Cofactor(s): Mg2+
  • Effectors of protein activity:
    • Inhibited by citrate, PEP (Hill Coefficient 3) and Ca2+ (competes with Mg2+) in B. licheniformes PubMed.
    • Inhibited by ATP (competitively) and f6p (non-competitively) in G. stearothermophillus PubMed
    • Activated by GDP and ADP in lower concentrations (1mM); above that inhibition, competing with the ATP for the binding site (in G. stearothermophillus) PubMed
    • Activated by NH4+ PubMed

Database entries

  • Structure:
    • 4A3S PubMed
    • 1MTO (mutant, complex with fructose-6-phosphate, Geobacillus stearothermophilus)
    • 4PFK (Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • twofold induced by glucose PubMed
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 863 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 3832 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1797 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1444 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1173 PubMed

Biological materials

  • Expression vector:
    • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP87, available in Jörg Stülke's lab
    • for expression/ purification from B. subtilis with C-terminal Strep-tag, for SPINE, in pGP382: pGP1266, available in Jörg Stülke's lab
    • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP393, available in Jörg Stülke's lab
    • for expression in B. subtilis, in pBQ200: pGP1422, available in Jörg Stülke's lab
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

Fabian M Commichau, Nico Pietack, Jörg Stülke
Essential genes in Bacillus subtilis: a re-evaluation after ten years.
Mol Biosyst: 2013, 9(6);1068-75
[PubMed:23420519] [WorldCat.org] [DOI] (I p)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc. Natl. Acad. Sci. U.S.A.: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Joseph A Newman, Lorraine Hewitt, Cecilia Rodrigues, Alexandra S Solovyova, Colin R Harwood, Richard J Lewis
Dissection of the network of interactions that links RNA processing with glycolysis in the Bacillus subtilis degradosome.
J. Mol. Biol.: 2012, 416(1);121-36
[PubMed:22198292] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Joseph Newman, Fabian M Rothe, Alexandra S Solovyova, Cecilia Rodrigues, Christina Herzberg, Fabian M Commichau, Richard J Lewis, Jörg Stülke
RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli.
J. Bacteriol.: 2011, 193(19);5431-41
[PubMed:21803996] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Henrike Pförtner, Leonie Rempeters, Nico Pietack, Christina Herzberg, Jörg Stülke
The RNA degradosome in Bacillus subtilis: identification of CshA as the major RNA helicase in the multiprotein complex.
Mol. Microbiol.: 2010;
[PubMed:20572937] [WorldCat.org] [DOI] (I a)

María-Enriqueta Muñoz-Márquez, Elizabeth Ponce-Rivas
Effect of pfkA chromosomal interruption on growth, sporulation, and production of organic acids in Bacillus subtilis.
J. Basic Microbiol.: 2010, 50(3);232-40
[PubMed:20473954] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol. Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol. Microbiol.: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] (P p)

X Zhu, M Byrnes, J W Nelson, S H Chang
Role of glycine 212 in the allosteric behavior of phosphofructokinase from Bacillus stearothermophilus.
Biochemistry: 1995, 34(8);2560-5
[PubMed:7873536] [WorldCat.org] (P p)

M Byrnes, X Zhu, E S Younathan, S H Chang
Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme.
Biochemistry: 1994, 33(11);3424-31
[PubMed:8136379] [WorldCat.org] (P p)

C K Marschke, R W Bernlohr
Purification and characterization of phosphofructokinase of Bacillus licheniformis.
Arch. Biochem. Biophys.: 1973, 156(1);1-16
[PubMed:4269800] [WorldCat.org] (P p)

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