Difference between revisions of "Pgi"

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=References=
 
[http://www.ncbi.nlm.nih.gov/pubmed/PubMed]
 
 
 
<pubmed>17218307 19052382 4214896 23420519 11489127 4275311 11491085 17218307, </pubmed>
 
<pubmed>17218307 19052382 4214896 23420519 11489127 4275311 11491085 17218307, </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:01, 13 July 2013

  • 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
Gene expression levels in SubtiExpress: pgi
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism, Sugar catabolism
MW, pI 50.4 kDa, 4.85
Gene length, protein length 1353 bp, 451 amino acids
Immediate neighbours yugM, yugK
Sequences Protein DNA DNA_with_flanks
Genetic context
Pgi context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Pgi expression.png















Categories containing this gene/protein

carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU31350

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 (according to Swiss-Prot) D-glucose 6-phosphate = D-fructose 6-phosphate
  • Protein family: GPI family (according to Swiss-Prot) GPI family
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Reversible Michaelis-Menten PubMed
  • Domains:
  • Modification: phosphorylation on Thr-39 PubMed
  • Cofactor(s):
  • Effectors of protein activity: competitively inhibited by 6-phosphogluconate (in B.caldotenax, B.stearothermophilus) PubMed
  • Localization:
    • cytoplasm (according to Swiss-Prot), cytoplasm

Database entries

  • Structure: 1B0Z (Geobacillus stearothermophilus), 2PGI (Geobacillus stearothermophilus)
  • KEGG entry: [3]

Additional information

  • extensive information on the structure and enzymatic properties of Pgi can be found at Proteopedia

Expression and regulation

  • Regulation: constitutively expressed PubMed
  • Additional information:

Biological materials

  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
  • Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany homepage

Your additional remarks

References

Fabian M Commichau, Nico Pietack, Jörg Stülke
Essential genes in Bacillus subtilis: a re-evaluation after ten years.
Mol Biosyst: 2013, 9(6);1068-75
[PubMed:23420519] [WorldCat.org] [DOI] (I p)

Yian Liang Lee, TienHsiung Thomas Li
Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2008, 64(Pt 12);1181-3
[PubMed:19052382] [WorldCat.org] [DOI] (I p)

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)

J Stülke, I Martin-Verstraete, P Glaser, G Rapoport
Characterization of glucose-repression-resistant mutants of Bacillus subtilis: identification of the glcR gene.
Arch Microbiol: 2001, 175(6);441-9
[PubMed:11491085] [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)

J Y Lin, C Prasad
Selection of a mutant of Bacillus subtilis deficient in glucose-6-phosphate dehydrogenase and phosphoglucoisomerase.
J Gen Microbiol: 1974, 83(2);419-21
[PubMed:4214896] [WorldCat.org] [DOI] (P p)

C Prasad, E Freese
Cell lysis of Bacillus subtilis caused by intracellular accumulation of glucose-1-phosphate.
J Bacteriol: 1974, 118(3);1111-22
[PubMed:4275311] [WorldCat.org] [DOI] (P p)