Pgk

• Description: phosphoglycerate kinase, glycolytic/ gluconeogenic enzyme, universally conserved protein
  
  

Gene name	pgk
Synonyms
Essential	No
Product	phosphoglycerate kinase
Function	enzyme in glycolysis/ gluconeogenesis
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	42,0 kDa, 4.77
Gene length, protein length	1182 bp, 394 amino acids
Immediate neighbours	tpi, gapA
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: BSU33930

Phenotypes of a mutant

• no growth on LB medium, the mutant requires glucise and malate for growth
• essential acoording to Kobayashi et al. PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins, universally conserved proteins

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + 3-phospho-D-glycerate = ADP + 1,3-bisphosphoglycerate (according to Swiss-Prot)

• Protein family: phosphoglycerate kinase family (according to Swiss-Prot)
• Paralogous protein(s):

Extended information on the protein

• Kinetic information: Two Substrate Reversible Michaelis-Menten PubMed

• Domains:
  • nucleotide binding domain (ATP) (350–353)
  • 2x substrate binding domain (21–23), (59–62)

• Modification: phosphorylation on Ser-183 AND Thr-299 PubMed, PubMed

• Cofactor(s): Mg2+ or Mn2+ PubMed

• Effectors of protein activity:
  • Inhibited by Co2+, NDP and NMP PubMed

• Interactions:

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

Database entries

• Structure: 1PHP (Geobacillus stearothermophilus), Geobacillus stearothermophilus NCBI

• UniProt: P40924

• KEGG entry: [3]

• E.C. number: 2.7.2.3

Expression and regulation

• Operon:
  • cggR-gapA-pgk-tpiA-pgm-eno PubMed
  • pgk-tpiA-pgm-eno PubMed

• Sigma factor:
  • cggR: SigA PubMed
  • pgk: SigA PubMed

• Regulation:
  • expression activated by glucose (3.3 fold) PubMed
  • cggR: induced by glycolytic substrates CggR PubMed
  • pgk: constitutive PubMed

• Regulatory mechanism: transcription repression by CggR PubMed

• Additional information:

Biological materials

• Mutant:
  • GP699 (pgk::cat), available in Stülke lab
  • GP707 (pgk::erm), available in Stülke lab

• Expression vector:
  • pGP1102 (N-terminal His-tag, in pWH844), available in Stülke lab
  • pGP95 (N-terminal Strep-tag, in pGP172), available in Stülke lab
  • pGP91 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
  • pGP1513 (expression in B. subtilis, in pBQ200), available in Stülke lab

• lacZ fusion: pGP514 (in pAC6), a series of promoter deletion variants is also available 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:

References

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Laurent Jannière, Danielle Canceill, Catherine Suski, Sophie Kanga, Bérengère Dalmais, Roxane Lestini, Anne-Françoise Monnier, Jérôme Chapuis, Alexander Bolotin, Marina Titok, Emmanuelle Le Chatelier, S Dusko Ehrlich
Genetic evidence for a link between glycolysis and DNA replication.
PLoS One: 2007, 2(5);e447
[PubMed:17505547] [WorldCat.org] [DOI] (I e)

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)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

K Kobayashi, S D Ehrlich, A Albertini, G Amati, K K Andersen, M Arnaud, K Asai, S Ashikaga, S Aymerich, P Bessieres, F Boland, S C Brignell, S Bron, K Bunai, J Chapuis, L C Christiansen, A Danchin, M Débarbouille, E Dervyn, E Deuerling, K Devine, S K Devine, O Dreesen, J Errington, S Fillinger, S J Foster, Y Fujita, A Galizzi, R Gardan, C Eschevins, T Fukushima, K Haga, C R Harwood, M Hecker, D Hosoya, M F Hullo, H Kakeshita, D Karamata, Y Kasahara, F Kawamura, K Koga, P Koski, R Kuwana, D Imamura, M Ishimaru, S Ishikawa, I Ishio, D Le Coq, A Masson, C Mauël, R Meima, R P Mellado, A Moir, S Moriya, E Nagakawa, H Nanamiya, S Nakai, P Nygaard, M Ogura, T Ohanan, M O'Reilly, M O'Rourke, Z Pragai, H M Pooley, G Rapoport, J P Rawlins, L A Rivas, C Rivolta, A Sadaie, Y Sadaie, M Sarvas, T Sato, H H Saxild, E Scanlan, W Schumann, J F M L Seegers, J Sekiguchi, A Sekowska, S J Séror, M Simon, P Stragier, R Studer, H Takamatsu, T Tanaka, M Takeuchi, H B Thomaides, V Vagner, J M van Dijl, K Watabe, A Wipat, H Yamamoto, M Yamamoto, Y Yamamoto, K Yamane, K Yata, K Yoshida, H Yoshikawa, U Zuber, N Ogasawara
Essential Bacillus subtilis genes.
Proc Natl Acad Sci U S A: 2003, 100(8);4678-83
[PubMed:12682299] [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)

K Suzuki, K Imahori
Phosphoglycerate kinase from Bacillus stearothermophilus.
Methods Enzymol: 1982, 90 Pt E;126-30
[PubMed:7154941] [WorldCat.org] [DOI] (P p)