Difference between revisions of "Tpi"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[carbon core metabolism]]}},
 
{{SubtiWiki category|[[carbon core metabolism]]}},
−
{{SubtiWiki category|[[phosphoproteins]]}}
+
{{SubtiWiki category|[[phosphoproteins]]}},
 +
[[most abundant proteins]]
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
−
* '''Domains:'''  
+
* '''[[Domains]]:'''  
  
 
* '''Modification:''' phosphorylation on Ser-213 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
 
* '''Modification:''' phosphorylation on Ser-213 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed]
  
−
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:''' inhibited by 2-phosphoglycolate (in ''B. stearothermophilus'') [http://www.ncbi.nlm.nih.gov/sites/entrez/8580851 PubMed]
 
* '''Effectors of protein activity:''' inhibited by 2-phosphoglycolate (in ''B. stearothermophilus'') [http://www.ncbi.nlm.nih.gov/sites/entrez/8580851 PubMed]
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* '''Additional information:'''
 
* '''Additional information:'''
 +
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
  
−
<pubmed>12850135 11489127 17505547 8021172 17218307 8580851 19193632 21821766 23420519</pubmed>
+
<pubmed>12850135 11489127 17505547 8021172 17218307 8580851 19193632 21821766 23420519 15378759</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:37, 5 March 2014

  • Description: triose phosphate isomerase, glycolytic/ gluconeogenic enzyme

Gene name tpi
Synonyms tpiA
Essential no
Product triosephosphate isomerase
Function enzyme in glycolysis/ gluconeogenesis
Gene expression levels in SubtiExpress: tpi
Interactions involving this protein in SubtInteract: Tpi
Metabolic function and regulation of this protein in SubtiPathways:
tpi
MW, pI 26,9 kDa, 4.79
Gene length, protein length 759 bp, 253 amino acids
Immediate neighbours pgm, pgk
Sequences Protein DNA DNA_with_flanks
Genetic context
Tpi context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Tpi expression.png
















Categories containing this gene/protein

carbon core metabolism, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

CggR regulon

The gene

Basic information

  • Locus tag: BSU33920

Phenotypes of a mutant

Database entries

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

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate (according to Swiss-Prot)
  • Protein family: triosephosphate isomerase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification: phosphorylation on Ser-213 PubMed
  • Effectors of protein activity: inhibited by 2-phosphoglycolate (in B. stearothermophilus) PubMed

Database entries

  • Structure: 1BTM (complex with 2-phosphoglycolic acid, Geobacillus stearothermophilus), complex with 2-phosphpoglycolic acid, Geobacillus stearothermophilus NCBI
  • KEGG entry: [3]

Additional information

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

Expression and regulation

  • Regulatory mechanism: transcription repression by CggR PubMed

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

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)

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632] [WorldCat.org] [DOI] (I 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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)

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)

L F Delboni, S C Mande, F Rentier-Delrue, V Mainfroid, S Turley, F M Vellieux, J A Martial, W G Hol
Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.
Protein Sci: 1995, 4(12);2594-604
[PubMed:8580851] [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)

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