Difference between revisions of "Pgm"

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* '''Description:''' phosphoglycerate mutase, glycolytic / gluconeogenic enzyme<br/><br/>
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=[http://yjucofi.co.cc UNDER COSTRUCTION, PLEASE SEE THIS POST IN RESERVE COPY]=
 
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=[http://yjucofi.co.cc CLICK HERE]=
 
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* '''Description:''' phosphoglycerate mutase, glycolytic / gluconeogenic enzyme&lt;br/>&lt;br/>
 
  
 
{| align="right" border="1" cellpadding="2"  
 
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|style="background:#ABCDEF;" align="center"| '''Essential''' || yes
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || yes
 
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|style="background:#ABCDEF;" align="center"| '''Product''' ||  2,3-bisphosphoglycerate-independent &lt;br/>phosphoglycerate mutase
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|style="background:#ABCDEF;" align="center"| '''Product''' ||  2,3-bisphosphoglycerate-independent <br/>phosphoglycerate mutase
 
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|style="background:#ABCDEF;" align="center"|'''Function''' || enzyme in glycolysis / gluconeogenesis
 
|style="background:#ABCDEF;" align="center"|'''Function''' || enzyme in glycolysis / gluconeogenesis
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: &lt;br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 56,1 kDa, 5.21
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 56,1 kDa, 5.21
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[eno]]'', ''[[tpi]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[eno]]'', ''[[tpi]]''
 
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&amp;#91;EMBLCDS:CAB15396&amp;#93;+-newId sequences] &lt;br/> (Barbe ''et al.'', 2009)'''
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15396&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
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|colspan="2" | '''Genetic context''' &lt;br/> [[Image:pgm_context.gif]]
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|colspan="2" | '''Genetic context''' <br/> [[Image:pgm_context.gif]]
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  &lt;div align="right"> &lt;small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]&lt;/small>&lt;/div>
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  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
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__TOC__
 
__TOC__
  
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&lt;br/>&lt;br/>&lt;br/>&lt;br/>&lt;br/>&lt;br/>
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<br/><br/><br/><br/><br/><br/>
  
  
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=== Database entries ===
 
=== Database entries ===
  
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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1EJJ 1EJJ] (Geobacillus stearothermophilus, complex with 3-phosphoglycerate),  [http://www.rcsb.org/pdb/explore.do?structureId=1EQJ 1EQJ] (Geobacillus stearothermophilus, complex with 2-phosphoglycerate),  ''Geobacillus stearothermophilus'', complex with 2-phosphoglycerate [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&amp;uid=16359 NCBI], ''Geobacillus stearothermophilus'', complex with 3-phosphoglycerate [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&amp;uid=15578 NCBI]
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* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1EJJ 1EJJ] (Geobacillus stearothermophilus, complex with 3-phosphoglycerate),  [http://www.rcsb.org/pdb/explore.do?structureId=1EQJ 1EQJ] (Geobacillus stearothermophilus, complex with 2-phosphoglycerate),  ''Geobacillus stearothermophilus'', complex with 2-phosphoglycerate [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=16359 NCBI], ''Geobacillus stearothermophilus'', complex with 3-phosphoglycerate [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=15578 NCBI]
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39773 P39773]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39773 P39773]
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=References=
 
=References=
  
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&lt;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  &lt;/pubmed>
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<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>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:38, 24 November 2010

  • 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 eno, tpi
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:
    • 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

Your additional remarks

References

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