Pgi

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  • 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 yugM, yugK
Gene sequence (+200bp) corrected Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context
Pgi context.gif
This image was kindly provided by SubtiList



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 on Thr-39 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. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
  2. Lee et al. (2008) Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis. Acta Cryst. Sect. F 64:1181-1183. PubMed
  3. 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
  4. 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
  5. Prasad and Freese (1974) Cell lysis of Bacillus subtilis caused by intracellular accumulation of glucose-1-phosphate. J. Bacteriol. 118:1111-1122. PubMed
  6. 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
  7. Macek et al. (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics 6(4): 697-707. PubMed