Difference between revisions of "Pgi"

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(References)
(Extended information on the protein)
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* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
* '''Effectors of protein activity:'''
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* '''Effectors of protein activity:''' Inhibited by 6-phosphogluconate (in ''B.caldotenax, B.stearothermophilus'') [http://www.ncbi.nlm.nih.gov/pubmed/7400125 PubMed]
  
 
* '''Interactions:'''
 
* '''Interactions:'''

Revision as of 10:42, 2 February 2009

  • Description: glucose 6-phosphate isomerase, glycolytic/ gluconeogenic enzyme

Gene name pgi
Synonyms yugL
Essential no
Product glucose-6-phosphate isomerase
Function enzyme in glycolysis/ gluconeogenesis
MW, pI 50.4 kDa, 4.85
Gene length, protein length 1353 bp, 451 amino acids
Immediate neighbours yugK, yugM
Gene sequence (+200bp) Protein sequence
Genetic context
Pgi context.gif



The gene

Basic information

  • Coordinates: 3219772 - 3221124

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: D-glucose 6-phosphate = D-fructose 6-phosphate
  • Protein family: GPI family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation (STY) PubMed
  • Cofactor(s):
  • Effectors of protein activity: Inhibited by 6-phosphogluconate (in B.caldotenax, B.stearothermophilus) PubMed
  • Interactions:
  • Localization: cytoplasm

Database entries

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

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation: constitutively expressed PubMed
  • Additional information:

Biological materials

  • Mutant: GP508 (spc), available in Stülke lab
  • Expression vector: pGP762 (N-terminal His-tag, in pWH844), available in Stülke lab
  • lacZ fusion: pGP510 (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

Jörg Stülke, University of Göttingen, Germany homepage

Your additional remarks

References

  1. Lee et al. (2008) Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis. Acta Cryst. Sect. F 64:1181-1183. PubMed
  2. Lin and Prasad (1975) Selection of a mutant of Bacillus subtilis deficient in glucose-6-phosphate dehydrogenase and phosphoglucoisomerase. J. Gen. Microbiol. 83:419-421. PubMed
  3. 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
  4. Prasad and Freese (1974) Cell lysis of Bacillus subtilis caused by intracellular accumulation of glucose-1-phosphate. J. Bacteriol. 118:1111-1122. PubMed
  5. Stülke, J., Martin-Verstraete, I., Glaser, P. & Rapoport, G. (2001) Characterization of glucose repression resistant mutants of Bacillus subtilis: identification of the glcR gene. Arch. Microbiol. 175: 441-449. PubMed
  6. Macek et al. (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics 6(4): 697-707. PubMed