Difference between revisions of "Pgk"

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(Database entries)
(Extended information on the protein)
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=== Extended information on the protein ===
 
=== Extended information on the protein ===
  
* '''Kinetic information:'''
+
* '''Kinetic information:''' Two Substrate Reversible Michaelis-Menten (in ''G. stearothermophillus'') [http://www.ncbi.nlm.nih.gov/pubmed/7154941 PubMed]
  
 
* '''Domains:'''  
 
* '''Domains:'''  
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* '''Modification:''' phosphorylation on Ser-183 AND Thr-299 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
 
* '''Modification:''' phosphorylation on Ser-183 AND Thr-299 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
  
* '''Cofactor(s):'''
+
* '''Cofactor(s):''' Mg2+ or Mn2+ [http://www.ncbi.nlm.nih.gov/pubmed/7154941 PubMed]
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
 +
** Inhibited by NDP and NMP [http://www.ncbi.nlm.nih.gov/pubmed/7154941 PubMed]
  
 
* '''Interactions:'''  
 
* '''Interactions:'''  

Revision as of 12:48, 10 June 2009

  • Description: phosphoglycerate kinase, glycolytic/ gluconeogenic enzyme

Gene name pgk
Synonyms
Essential yes
Product phosphoglycerate kinase
Function enzyme in glycolysis/ gluconeogenesis
MW, pI 42,0 kDa, 4.77
Gene length, protein length 1182 bp, 394 amino acids
Immediate neighbours gapA, tpi
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Pgk context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU33930

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 + 1,3-bisphosphoglycerate (according to Swiss-Prot)
  • Protein family: phosphoglycerate kinase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Two Substrate Reversible Michaelis-Menten (in G. stearothermophillus) PubMed
  • Domains:
    • nucleotide binding domain (ATP) (350–353)
    • 2x substrate binding domain (21–23), (59–62)
  • Modification: phosphorylation on Ser-183 AND Thr-299 PubMed, PubMed
  • Cofactor(s): Mg2+ or Mn2+ PubMed
  • Effectors of protein activity:
    • Inhibited by NDP and NMP PubMed
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot), Cytoplasm (Homogeneous) PubMed

Database entries

  • Structure: 1PHP (Geobacillus stearothermophilus), Geobacillus stearothermophilus NCBI
  • KEGG entry: [3]

Additional information

Expression and regulation

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

Biological materials

  • Mutant:
  • Expression vector: pGP1102 (N-terminal His-tag, in pWH844), pGP95 (N-terminal Strep-tag, in pGP172), pGP91 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
  • lacZ fusion: pGP514 (in pAC6), a series of promoter deletion variants is also available 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

Your additional remarks

References

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Laurent Jannière, Danielle Canceill, Catherine Suski, Sophie Kanga, Bérengère Dalmais, Roxane Lestini, Anne-Françoise Monnier, Jérôme Chapuis, Alexander Bolotin, Marina Titok, Emmanuelle Le Chatelier, S Dusko Ehrlich
Genetic evidence for a link between glycolysis and DNA replication.
PLoS One: 2007, 2(5);e447
[PubMed:17505547] [WorldCat.org] [DOI] (I e)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] [DOI] (P p)