Difference between revisions of "Pgm"

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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]
 
[[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
  
[Jedrzejas|Mark J. Jedrzejas]], Research Center Oakland, CA, USA  [http://www.chori.org/Principal_Investigators/Jedrzejas_Mark_J/jedrzejas_research.html Homepage]
+
[[Jedrzejas|Mark J. Jedrzejas]], Research Center Oakland, CA, USA  [http://www.chori.org/Principal_Investigators/Jedrzejas_Mark_J/jedrzejas_research.html Homepage]
  
 
=Your additional remarks=
 
=Your additional remarks=

Revision as of 15:18, 18 January 2009

  • Description: phosphoglycerate mutase, glycolytic/ gluconeogenic enzyme

Gene name pgm
Synonyms gpmI
Essential yes
Product 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Function enzyme in glycolysis/ gluconeogenesis
MW, pI 56,1 kDa, 5.21
Gene length, protein length 1533 bp, 511 amino acids
Immediate neighbours tpi, eno
Gene sequence (+200bp) Protein sequence
Genetic context
Pgm context.gif




The gene

Basic information

  • Coordinates: 3476911 - 3478443

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: 2-phospho-D-glycerate = 3-phospho-D-glycerate
  • Protein family: BPG-independent phosphoglycerate mutase family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation PubMed
  • Cofactor(s): 2 manganese ions per subunit
  • Effectors of protein activity:
  • Interactions: Pgm-PfkA
  • Localization: cytoplasm PubMed

Database entries

  • Structure: Geobacillus stearothermophilus, complex with 2-phosphoglycerate NCBI, Geobacillus stearothermophilus, complex with 3-phosphoglycerate NCBI
  • Swiss prot entry: [3]
  • KEGG entry: [4]
  • E.C. number: [5]

Additional information

is pH sensitive

Expression and regulation

  • Regulation:

cggR: neg. regulated by CggR PubMed, induced by sugar

pgk: constitutive PubMed

  • Regulatory mechanism: transcription repression by CggR PubMed
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector: pGP1101 (N-terminal His-tag, in pWH844), pGP396 (Pgm-S62A, N-terminal His-tag, in pWH844), pGP92 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
  • lacZ fusion:
  • 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

Mark J. Jedrzejas, Research Center Oakland, CA, USA Homepage

Your additional remarks

References

  1. Jannière, L., Canceill, D., Suski, C., Kanga, S., Dalmais, B., Lestini, R., Monnier, A. F., Chapuis, J., Bolotin, A., Titok, M., Le Chatelier, E., and Ehrlich, S. D. (2007) Genetic evidence for a link between glycolysis and DNA replication. PLoS ONE 2, e447. PubMed
  2. Leyva-Vazquez, M. A., and Setlow, P. (1994) Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis. J Bacteriol 176: 3903-3910. PubMed
  3. Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M. & 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