Tpi

• 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	pgk, pgm
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU33920

Phenotypes of a mutant

• Essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Swiss prot entry: P27876

• KEGG entry: [3]

• E.C. number: 5.3.1.1 5.3.1.1]

Expression and regulation

• Operon:
  • cggR-gapA-pgk-tpiA-pgm-eno
  • pgk-tpiA-pgm-eno

• Sigma factor: SigA

• Regulation: expression activated by glucose (2.8 fold) PubMed
  • cggR: neg. regulated by CggR PubMed, induced by sugar
  • pgk: constitutive PubMed

• 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), pGP89 (N-terminal Strep-tag, for SPINE, expression in B. subtilis), 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:

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] [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)