Pgm

• Description: phosphoglycerate mutase, glycolytic / gluconeogenic enzyme
  
  

Gene name	pgm
Synonyms	gpmI
Essential	Yes (PubMed)
Product	2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Function	enzyme in glycolysis / gluconeogenesis
Gene expression levels in SubtiExpress: pgm
Interactions involving this protein in SubtInteract: Pgm
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	56,1 kDa, 5.21
Gene length, protein length	1533 bp, 511 amino acids
Immediate neighbours	eno, tpi
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, essential genes, phosphoproteins

This gene is a member of the following regulons

CggR regulon

The gene

Basic information

• Locus tag: BSU33910

Phenotypes of a mutant

• Essential PubMed

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 (according to Swiss-Prot)

• Protein family: BPG-independent phosphoglycerate mutase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information: Reversible Michaelis-Menten PubMed

• Domains:

• Modification: phosphorylation on Ser-62 PubMed, PubMed

• Cofactor(s): Mn2+

• Effectors of protein activity:
  • Inhibited by diverse divalent heavy-metal ions, EDTA and 2,3-butanedione PubMed
  • 2,3-Diphosphoglycerate has NO role on this enzyme regulation PubMed

• Interactions:
  • Pgm-PfkA

• Localization: Cytoplasm (Homogeneous) PubMed

Database entries

• Structure: 1EJJ (Geobacillus stearothermophilus, complex with 3-phosphoglycerate), 1EQJ (Geobacillus stearothermophilus, complex with 2-phosphoglycerate), Geobacillus stearothermophilus, complex with 2-phosphoglycerate NCBI, Geobacillus stearothermophilus, complex with 3-phosphoglycerate NCBI

• UniProt: P39773

• KEGG entry: [3]

• E.C. number: 5.4.2.1]

Additional information

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

Expression and regulation

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

• Expression browser: pgm PubMed

• Sigma factor: 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:
  • GP593 (pgm::cat), available in Stülke lab
  • GP598 (pgm::erm), available in Stülke lab
  • GP698 (pgm-eno::cat), available in Stülke lab

• Expression vector:
  • pGP1425 (expression of pgm in B. subtilis, in pBQ200), available in Stülke lab
  • pGP1500 (expression of pgm and eno in B. subtilis, in pBQ200), available in Stülke lab
  • pGP1101 (N-terminal His-tag, in pWH844), available in Stülke lab
  • pGP396 (Pgm-S62A, N-terminal His-tag, in pWH844), available in Stülke lab
  • pGP92 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody:

Labs working on this gene/protein

Jörg Stülke, University of Göttingen, Germany Homepage

Mark J. Jedrzejas, Research Center Oakland, CA, USA Homepage