Pgk

• Description: phosphoglycerate kinase, glycolytic/ gluconeogenic enzyme
  
  

Gene name	pgk
Synonyms
Essential	yes
Product	phosphoglycerate kinase
Function	enzyme in glycolysis/ gluconeogenesis
MW, pI	42,0 kDa, 4.77
Gene length, protein length	1182 bp, 394 amino acids
Immediate neighbours	gapA, tpi
Gene sequence (+200bp)	Protein sequence
Genetic context

The gene

Basic information

• Coordinates: 3479231 - 3480412

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + 3-phospho-D-glycerate = ADP + 1,3-bisphosphoglycerate

• Protein family: phosphoglycerate kinase family

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

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

• Modification: phosphorylation PubMed,

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: Cytoplasm PubMed

Database entries

• Structure: Geobacillus stearothermophilus NCBI

• Swiss prot entry: [3]

• KEGG entry: [4]

• E.C. number: [5]

Expression and regulation

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

• Sigma factor: SigA

• Regulation:

cggR: neg. regulated by CggR PubMed, induced by sugar

pgk: constitutive PubMed

• Regulatory mechanism: transcription repression by CggR PubMed

• Additional information:

Biological materials

• Mutant:

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

1. 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
2. Jannière, L., Canceill, D., Suski, C., Kanga, S., Dalmais, B., Lestini, R., Monnier, A. F., Chapuis, J., Bolotin, A., Titok, M., Le Chatelier, E., and Ehrlich, S. D. (2007) Genetic evidence for a link between glycolysis and DNA replication. PLoS ONE 2, e447. PubMed
3. Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed