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"  
 
{| 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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|-
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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"| '''Product''' ||  2,3-bisphosphoglycerate-independent &lt;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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|-
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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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|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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|-
 
|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+&#91;EMBLCDS:CAB15396&#93;+-newId sequences] <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+&amp;#91;EMBLCDS:CAB15396&amp;#93;+-newId sequences] &lt;br/> (Barbe ''et al.'', 2009)'''
 
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|-
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|colspan="2" | '''Genetic context''' <br/> [[Image:pgm_context.gif]]
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|colspan="2" | '''Genetic context''' &lt;br/> [[Image:pgm_context.gif]]
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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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  &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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|-
 
|}
 
|}
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__TOC__
 
__TOC__
  
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<br/><br/><br/><br/><br/><br/>
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&lt;br/>&lt;br/>&lt;br/>&lt;br/>&lt;br/>&lt;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&uid=16359 NCBI], ''Geobacillus stearothermophilus'', complex with 3-phosphoglycerate [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&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&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]
  
 
* '''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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<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>
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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>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 07:16, 24 November 2010

UNDER COSTRUCTION, PLEASE SEE THIS POST IN RESERVE COPY

CLICK HERE

  • 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/> Pgm context.gif 
<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

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

<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>

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