Difference between revisions of "PfkA"

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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1MTO 1MTO] (mutant, complex with fructose-6-phosphate, Geobacillus stearothermophilus),  [http://www.rcsb.org/pdb/explore.do?structureId=4PFK 4PFK] (Geobacillus stearothermophilus),  ''Geobacillus stearothermophilus'' [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=58449 NCBI], Mutant form, complex with fructose-6-phosphate ''Geobacillus stearothermophilus'' [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=21480 NCBI]
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1MTO 1MTO] (mutant, complex with fructose-6-phosphate, Geobacillus stearothermophilus),  [http://www.rcsb.org/pdb/explore.do?structureId=4PFK 4PFK] (Geobacillus stearothermophilus),  ''Geobacillus stearothermophilus'' [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=58449 NCBI], Mutant form, complex with fructose-6-phosphate ''Geobacillus stearothermophilus'' [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=21480 NCBI]
  
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34529 O34529]
+
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34529 O34529]
  
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU29190]
 
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU29190]

Revision as of 14:05, 20 July 2009

  • Description: phosphofructokinase, glycolytic enzyme

Gene name pfkA
Synonyms pfk
Essential yes
Product 6-phosphofructokinase
Function catabolic enzyme in glycolysis
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism, Sugar catabolism
MW, pI 34,1 kDa, 6.14
Gene length, protein length 957 bp, 319 amino acids
Immediate neighbours accA, pyk
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PfkA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU29190

Phenotypes of a mutant

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:
  • 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
  • Localization: cytoplasm (according to Swiss-Prot), Cytoplasm (Homogeneous) PubMed

Database entries

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

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation: twofold induced by glucose PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector: pGP393 (N-terminal His-tag, in pWH844), pGP87 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
  • lacZ fusion: pGP511 (in pAC6), available in Stülke lab
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References