Difference between revisions of "Tpi"

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(Expression and regulation)
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 759 bp, 253 amino acids
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 759 bp, 253 amino acids
 
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[pgk]]'', ''[[pgm]]''
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[pgm]]'', ''[[pgk]]''
 
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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:CAB15397&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
 
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15397&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''

Revision as of 11:12, 7 December 2009

  • Description: triose phosphate isomerase, glycolytic/ gluconeogenic enzyme

Gene name tpi
Synonyms tpiA
Essential yes
Product triosephosphate isomerase
Function enzyme in glycolysis/ gluconeogenesis
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism, Sugar catabolism
MW, pI 26,9 kDa, 4.79
Gene length, protein length 759 bp, 253 amino acids
Immediate neighbours pgm, pgk
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Tpi context.gif
This image was kindly provided by SubtiList








The gene

Basic information

  • Locus tag: BSU33920

Phenotypes of a mutant

Database entries

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

Additional information

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:
  • Domains:
  • Modification: phosphorylation on Ser-213 PubMed
  • Cofactor(s):
  • Effectors of protein activity: inhibited by 2-phosphoglycolate (in B. stearothermophilus) PubMed
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot), cytoplasm 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

Expression and regulation

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

Biological materials

  • Mutant: GP700 (cat), available in Stülke lab
  • Expression vector:
    • pGP394 (N-terminal His-tag, in pWH844), available in Stülke lab
    • pGP89 (N-terminal Strep-tag, for SPINE, expression in B. subtilis), available in Stülke lab
    • pGP1511 (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

Your additional remarks

References

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)

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] (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)