Pgi

• 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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU31350

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• 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 (according to Swiss-Prot), cytoplasm

Database entries

• Structure: 1B0Z (Geobacillus stearothermophilus), 2PGI (Geobacillus stearothermophilus)

• Swiss prot entry: P80860

• KEGG entry: [3]

• E.C. number: 5.3.1.9

Expression and regulation

• Operon: pgi PubMed

• 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

References

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)

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