Difference between revisions of "PfkA"

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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [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]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34529 O34529]

Revision as of 21:57, 5 May 2009

  • Description: phosphofructokinase, glycolytic enzyme

Gene name pfkA
Synonyms pfk
Essential yes
Product 6-phosphofructokinase
Function catabolic enzyme in glycolysis
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

  • Coordinates: 2985630 - 2986586

Phenotypes of a mutant

essential 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
  • Protein family: phosphofructokinase family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • 3 x nucleotide binding domain (ATP) (21–25), (154–158), (171–187)
  • Modification:
  • Cofactor(s): ATP
  • Effectors of protein activity: inhibited by citrate, ATP, PEP, Ca2+, and others (in B. licheniformes) 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

  1. Meile et al. (2006) Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory Proteomics 6: 2135-2146. PubMed
  2. Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. (2009) Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. Mol. Cell. Proteomics in press PubMed
  3. Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol Microbiol 41, 409-422. PubMed