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: 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, phosphoproteins

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: 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

• Interactions:

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

Database entries

• 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:

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

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)