Difference between revisions of "Pgm"

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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:''' Reversible Michaelis-Menten [http://www.ncbi.nlm.nih.gov/pubmed/33963 PubMed]
  
 
* '''Domains:'''  
 
* '''Domains:'''  
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* '''Modification:''' phosphorylation on Ser-62 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
 
* '''Modification:''' phosphorylation on Ser-62 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed]
  
* '''Cofactor(s):''' 2 manganese ions per subunit
+
* '''Cofactor(s):''' Mn2+
  
* '''Effectors of protein activity:''' inhibited by heavy-metal ions, 2,3-butanedione and sulfhydryl agents [http://www.ncbi.nlm.nih.gov/sites/entrez/33963 PubMed]
+
* '''Effectors of protein activity:'''  
 +
** Inhibited by diverse divalent heavy-metal ions and 2,3-butanedione [http://www.ncbi.nlm.nih.gov/sites/entrez/33963 PubMed]
 +
** 2,3-Diphosphoglycerate has NO role on this enzyme regulation [http://www.ncbi.nlm.nih.gov/sites/entrez/33963 PubMed]
  
 
* '''Interactions:''' Pgm-[[PfkA]]
 
* '''Interactions:''' Pgm-[[PfkA]]

Revision as of 13:01, 10 June 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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Pgm context.gif
This image was kindly provided by SubtiList





The gene

Basic information

  • Locus tag: BSU33910

Phenotypes of a mutant

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 (according to Swiss-Prot)
  • Protein family: BPG-independent phosphoglycerate mutase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Reversible Michaelis-Menten PubMed
  • Domains:
  • Cofactor(s): Mn2+
  • Effectors of protein activity:
    • Inhibited by diverse divalent heavy-metal ions and 2,3-butanedione PubMed
    • 2,3-Diphosphoglycerate has NO role on this enzyme regulation PubMed
  • Interactions: Pgm-PfkA
  • Localization: Cytoplasm (Homogeneous) PubMed

Database entries

  • Structure: 1EJJ (Geobacillus stearothermophilus, complex with 3-phosphoglycerate), 1EQJ (Geobacillus stearothermophilus, complex with 2-phosphoglycerate), Geobacillus stearothermophilus, complex with 2-phosphoglycerate NCBI, Geobacillus stearothermophilus, complex with 3-phosphoglycerate NCBI
  • Swiss prot entry: [3]
  • KEGG entry: [4]

Additional information

is pH sensitive

Expression and regulation

  • Regulation: expression activated by glucose (7.3 fold) PubMed

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