Difference between revisions of "PfkA"

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(Database entries)
(Labs working on this gene/protein)
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=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
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[[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
  
 
=Your additional remarks=
 
=Your additional remarks=

Revision as of 18:23, 13 January 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
Gene sequence (+200bp) Protein sequence
Genetic context
PfkA context.gif












The gene

Basic information

  • Coordinates: 2985630 - 2986586

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
  • 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:
  • Interactions: Pyk-PfkA
  • Localization: cytoplasm PubMed

Database entries

  • Structure: Geobacillus stearothermophilus NCBI, Mutant form, complex with fructose-6-phosphate Geobacillus stearothermophilus NCBI
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Operon: pfkA pyk
  • Sigma factor:
  • Regulation: twofold induced by glucose
  • Regulatory mechanism:
  • Additional information:

Biological materials

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

  1. Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. subm.
  2. 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