Difference between revisions of "Pgi"

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Revision as of 08:07, 23 April 2012

  • 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
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
Get the DNA and protein sequences
(Barbe et al., 2009)
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

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

Biological materials

  • Mutant: GP508 (spc), available in Stülke lab
  • Expression vector:
    • pGP398 (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

PubMed

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)