Difference between revisions of "Pgm"

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=Biological materials =
 
=Biological materials =
 
* '''Mutant:'''
 
* '''Mutant:'''
−
** GP593 (''pgm''::''cat''), available in [[Stülke]] lab
+
** GP593 (''pgm''::''cat''), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}}
−
** GP598 (''pgm''::''erm''), available in [[Stülke]] lab
+
** GP598 (''pgm''::''erm''), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}}
−
** GP698 (''pgm''-''eno''::cat), available in [[Stülke]] lab
+
** GP698 (''pgm''-''eno''::cat), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}}
  
 
* '''Expression vector:'''  
 
* '''Expression vector:'''  
−
** pGP1425 (expression of ''pgm'' in ''B. subtilis'', in [[pBQ200]]), available in [[Stülke]] lab
+
** 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 [[Stülke]] 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 [[Stülke]] 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 [[Stülke]] 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 [[Stülke]] lab  
+
** pGP92 (N-terminal Strep-tag, for [[SPINE]], expression in B. subtilis, in [[pGP380]]), available in [[Jörg Stülke]]'s lab
 
 
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
Line 148: Line 148:
 
* '''GFP fusion:'''
 
* '''GFP fusion:'''
  
−
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab
+
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Jörg Stülke]]'s lab
  
 
* '''Antibody:'''
 
* '''Antibody:'''
Line 161: Line 161:
  
 
=References=
 
=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  23420519 </pubmed>
 
<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  23420519 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:37, 13 July 2013

  • 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 DNA_with_flanks
Genetic context
Pgm context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Pgm expression.png
















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

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

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

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

Expression and regulation

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

Biological materials

  • 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

Your additional remarks

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)

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