Pgm

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• Description: phosphoglycerate mutase, glycolytic / gluconeogenic enzyme<br/><br/>

Gene name	pgm
Synonyms	gpmI
Essential	yes
Product	2,3-bisphosphoglycerate-independent <br/>phosphoglycerate mutase
Function	enzyme in glycolysis / gluconeogenesis
Metabolic function and regulation of this protein in SubtiPathways: <br/>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 <br/> (Barbe et al., 2009)
Genetic context <br/> <div align="right"> <small>This image was kindly provided by SubtiList</small></div>

<br/><br/><br/><br/><br/><br/>

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]

Expression and regulation

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

References

<pubmed>11514674,17085493,10764795,8215434,10747010,11712498,9830105,10388626,8636019,11827481,16479537, 12850135,17726680,17505547, 8021172,11489127, 10388626,10747010, 10764795, 11712498, 12729763, 17085493, 17218307 33963 </pubmed>