Difference between revisions of "Pgm"

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(Biological materials)
(Biological materials)
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** pGP396 (Pgm-S62A, N-terminal His-tag, in [[pWH844]]), available in [[Stülke]] lab  
 
** pGP396 (Pgm-S62A, N-terminal His-tag, in [[pWH844]]), available in [[Stülke]] lab  
 
** pGP92 (N-terminal Strep-tag, for [[SPINE]], expression in B. subtilis, in [[pGP380]]), available in [[Stülke]] lab  
 
** pGP92 (N-terminal Strep-tag, for [[SPINE]], expression in B. subtilis, in [[pGP380]]), available in [[Stülke]] lab  
** pGP1500 (expression in ''B. subtilis'', in [[pBQ200]]), expression in B. subtilis, in [[pKT25]]), available in [[Stülke]] lab
+
** pGP1500 (expression in ''B. subtilis'', in [[pBQ200]]), expression in B. subtilis), available in [[Stülke]] lab
 
 
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''

Revision as of 10:40, 7 July 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
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
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, EDTA 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

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: GP698 (cat), available in Stülke lab
  • Expression vector:
    • pGP1101 (N-terminal His-tag, in pWH844), available in Stülke lab
    • pGP396 (Pgm-S62A, N-terminal His-tag, in pWH844), available in Stülke lab
    • pGP92 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
    • pGP1500 (expression in B. subtilis, in pBQ200), expression in B. subtilis), 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