Difference between revisions of "Pgk"

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(The gene)
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=== Basic information ===
 
=== Basic information ===
  
* '''Coordinates:'''
+
* '''Coordinates:''' 3479231 - 3480412
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
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=== Additional information===
 
=== Additional information===
 
  
 
=The protein=
 
=The protein=

Revision as of 12:00, 13 January 2009

  • Description: catalyzes the reaktion of 1,3-phosphoglycerate to 3-Phosphoglycerate by phosphorylation of ADP and the reverse reaktion

Gene name pgk
Synonyms
Essential yes
Product Phosphoglycerate kinase
Function phosphorylation
MW, pI 42,0 kDa, 4.77
Gene length, protein length 1182 bp, 394 amino acids
Immediate neighbours gapA, tpi
Gene sequence (+200bp) Protein sequence
Genetic context
Pgk context.gif












The gene

Basic information

  • Coordinates: 3479231 - 3480412

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
  • Protein family: phosphoglycerate kinase family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • nucleotide binding domain (ATP) (350–353)
    • 2x substrate binding domain (21–23), (59–62)
  • Modification: phosphorylation PubMed,
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions: Pgk-GapA
  • Localization: Cytoplasm PubMed

Database entries

  • Structure: Geobacillus stearothermophilus NCBI
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

Expression and regulation

  • Regulation: neg. regulated by CggR PubMed, induced by sugar
  • Additional information:

Biological materials

Labs working on this gene/protein

Your additional remarks

References

  1. 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