Difference between revisions of "Pgm"

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* '''Operon:'''  
 
* '''Operon:'''  
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** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]''
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** ''[[cggR]]-[[gapA]]-[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' {{PubMed|11489127}}
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** ''[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]''
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** ''[[pgk]]-[[tpiA]]-[[pgm]]-[[eno]]'' {{PubMed|11489127}}
  
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* '''Sigma factor:''' [[SigA]]
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* '''Sigma factor:''' [[SigA]] {{PubMed|11489127}}
  
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* '''Regulation:''' expression activated by glucose (7.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]   
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* '''Regulation:'''  
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''[[cggR]]'': neg. regulated by [[CggR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed], induced by sugar
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** expression activated by glucose (3.3 fold) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]   
 +
** ''[[cggR]]'': induced by glycolytic substrates [[CggR]] {{PubMed|11489127}}
 +
** ''[[pgk]]'': constitutive {{PubMed|11489127}}
  
−
''[[pgk]]'': constitutive [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed]
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* '''Regulatory mechanism:''' transcription repression by [[CggR]] {{PubMed|11489127}}
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−
* '''Regulatory mechanism:''' transcription repression by [[CggR]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11489127 PubMed]
 
  
 
* '''Additional information:'''
 
* '''Additional information:'''

Revision as of 19:52, 4 October 2009

  • 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
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 tpi, eno
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Pgm context.gif
This image was kindly provided by SubtiList








The gene

Basic information

  • Locus tag: BSU33910

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:
  • 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
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism: transcription repression by CggR PubMed
  • Additional information:

Biological materials

  • Mutant: GP698 (cat), available in Stülke lab
  • Expression vector:
    • 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
    • pGP1500 (expression in B. subtilis, in pBQ200), 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

Your additional remarks

References

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)

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