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: pgm
MW, pI	56,1 kDa, 5.21
Gene length, protein length	1533 bp, 511 amino acids
Immediate neighbours	eno, tpi
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, 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

• BsubCyc: BSU33910

• 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

• BsubCyc: BSU33910

• 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:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2946 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2005 PubMed

Biological materials

• Mutant:
  • GP593 (pgm::cat), available in Jörg Stülke's lab, PubMed
  • GP598 (pgm::erm), available in Jörg Stülke's lab, PubMed
  • GP698 (pgm-eno::cat), available in Jörg Stülke's lab, PubMed

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

• lacZ fusion:

• 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

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