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
Sequences	Protein DNA Advanced_DNA
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

References

Fabian M Commichau, Nico Pietack, Jörg Stülke
Essential genes in Bacillus subtilis: a re-evaluation after ten years.
Mol Biosyst: 2013, 9(6);1068-75
[PubMed:23420519] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Laurent Jannière, Danielle Canceill, Catherine Suski, Sophie Kanga, Bérengère Dalmais, Roxane Lestini, Anne-Françoise Monnier, Jérôme Chapuis, Alexander Bolotin, Marina Titok, Emmanuelle Le Chatelier, S Dusko Ehrlich
Genetic evidence for a link between glycolysis and DNA replication.
PLoS One: 2007, 2(5);e447
[PubMed:17505547] [WorldCat.org] [DOI] (I e)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Masatoshi Nukui, Luciane V Mello, James E Littlejohn, Barbara Setlow, Peter Setlow, Kijeong Kim, Terrance Leighton, Mark J Jedrzejas
Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species.
Biophys J: 2007, 92(3);977-88
[PubMed:17085493] [WorldCat.org] [DOI] (P p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Daniel J Rigden, Ejvis Lamani, Luciane V Mello, James E Littlejohn, Mark J Jedrzejas
Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling.
J Mol Biol: 2003, 328(4);909-20
[PubMed:12729763] [WorldCat.org] [DOI] (P p)

Daniel J Rigden, Luciane V Mello, Peter Setlow, Mark J Jedrzejas
Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity.
J Mol Biol: 2002, 315(5);1129-43
[PubMed:11827481] [WorldCat.org] [DOI] (P p)

M J Jedrzejas, P Setlow
Comparison of the binuclear metalloenzymes diphosphoglycerate-independent phosphoglycerate mutase and alkaline phosphatase: their mechanism of catalysis via a phosphoserine intermediate.
Chem Rev: 2001, 101(3);607-18
[PubMed:11712498] [WorldCat.org] [DOI] (P p)

D J Rigden, I Bagyan, E Lamani, P Setlow, M J Jedrzejas
A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase.
Protein Sci: 2001, 10(9);1835-46
[PubMed:11514674] [WorldCat.org] [DOI] (P p)

H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127] [WorldCat.org] [DOI] (P p)

M J Jedrzejas, M Chander, P Setlow, G Krishnasamy
Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate.
J Biol Chem: 2000, 275(30);23146-53
[PubMed:10764795] [WorldCat.org] [DOI] (P p)

M J Jedrzejas, M Chander, P Setlow, G Krishnasamy
Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus.
EMBO J: 2000, 19(7);1419-31
[PubMed:10747010] [WorldCat.org] [DOI] (P p)

M Chander, P Setlow, E Lamani, M J Jedrzejas
Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus.
J Struct Biol: 1999, 126(2);156-65
[PubMed:10388626] [WorldCat.org] [DOI] (P p)

M Chander, B Setlow, P Setlow
The enzymatic activity of phosphoglycerate mutase from gram-positive endospore-forming bacteria requires Mn2+ and is pH sensitive.
Can J Microbiol: 1998, 44(8);759-67
[PubMed:9830105] [WorldCat.org] [DOI] (P p)

N G Magill, A E Cowan, M A Leyva-Vazquez, M Brown, D E Koppel, P Setlow
Analysis of the relationship between the decrease in pH and accumulation of 3-phosphoglyceric acid in developing forespores of Bacillus species.
J Bacteriol: 1996, 178(8);2204-10
[PubMed:8636019] [WorldCat.org] [DOI] (P p)

M A Leyva-Vazquez, P Setlow
Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis.
J Bacteriol: 1994, 176(13);3903-10
[PubMed:8021172] [WorldCat.org] [DOI] (P p)

N J Kuhn, B Setlow, P Setlow
Manganese(II) activation of 3-phosphoglycerate mutase of Bacillus megaterium: pH-sensitive interconversion of active and inactive forms.
Arch Biochem Biophys: 1993, 306(2);342-9
[PubMed:8215434] [WorldCat.org] [DOI] (P p)

K Watabe, E Freese
Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis.
J Bacteriol: 1979, 137(2);773-8
[PubMed:33963] [WorldCat.org] [DOI] (P p)