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
Gene expression levels in SubtiExpress: pgi
Metabolic function and regulation of this protein in SubtiPathways: pgi
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, phosphoproteins, most abundant proteins

The gene

Basic information

• Locus tag: BSU31350

Database entries

• BsubCyc: BSU31350

• 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:
  • Reversible Michaelis-Menten PubMed
  • specific activity: 2.1 µmol min^-1 (mg protein)^-1 PubMed

• Domains:

• Modification: phosphorylation on Thr-39 PubMed

• Cofactors:

• Effectors of protein activity: competitively inhibited by 6-phosphogluconate (in B.caldotenax, B.stearothermophilus) PubMed

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot), cytoplasm

Database entries

• BsubCyc: BSU31350

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

• UniProt: P80860

• KEGG entry: [3]

• E.C. number: 5.3.1.9

Additional information

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

Expression and regulation

• Operon: pgi-yugM-yugN PubMed

• Expression browser: pgi PubMed

• Sigma factor:

• Regulation: constitutively expressed PubMed

• Additional information:
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant: GP508 (spc), available in Jörg Stülke's lab, PubMed

• Expression vector:
  • pGP398 (N-terminal His-tag, in pWH844), available in Jörg Stülke's lab

• lacZ fusion: pGP510 (in pAC6), available in Jörg Stülke's lab

• 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

References

Michael Kohlstedt, Praveen K Sappa, Hanna Meyer, Sandra Maaß, Adrienne Zaprasis, Tamara Hoffmann, Judith Becker, Leif Steil, Michael Hecker, Jan Maarten van Dijl, Michael Lalk, Ulrike Mäder, Jörg Stülke, Erhard Bremer, Uwe Völker, Christoph Wittmann
Adaptation of Bacillus subtilis carbon core metabolism to simultaneous nutrient limitation and osmotic challenge: a multi-omics perspective.
Environ Microbiol: 2014, 16(6);1898-917
[PubMed:24571712] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)