Pgm

• Description: phosphoglycerate mutase, glycolytic/ gluconeogenic enzyme
  
  

Gene name	pgm
Synonyms	gpmI
Essential	yes
Product	2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Function	enzyme in glycolysis/ gluconeogenesis
MW, pI	56,1 kDa, 5.21
Gene length, protein length	1533 bp, 511 amino acids
Immediate neighbours	tpi, eno
Gene sequence (+200bp)	Protein sequence
Genetic context

The gene

Basic information

• Coordinates: 3476911 - 3478443

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2-phospho-D-glycerate = 3-phospho-D-glycerate

• Protein family: BPG-independent phosphoglycerate mutase family

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylation PubMed

• Cofactor(s): 2 manganese ions per subunit

• Effectors of protein activity:

• Interactions: Pgm-PfkA

• Localization: cytoplasm PubMed

Database entries

• Structure: Geobacillus stearothermophilus, complex with 2-phosphoglycerate NCBI, Geobacillus stearothermophilus, complex with 3-phosphoglycerate NCBI

• Swiss prot entry: [3]

• KEGG entry: [4]

• E.C. number: [5]

Additional information

is pH sensitive

Expression and regulation

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

• Sigma factor: SigA

• Regulation: neg. regulated by CggR PubMed, induced by sugar

• Regulatory mechanism: repressor CggR PubMed

• Additional information:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

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