Difference between revisions of "Pyk"
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=== Basic information === | === Basic information === | ||
− | * '''Locus tag:''' | + | * '''Locus tag:''' BSU29180 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P80885] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P80885] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU29180] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.1.40 2.7.1.40] | * '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.1.40 2.7.1.40] |
Revision as of 09:55, 3 June 2009
- Description: pyruvate kinase, glycolytic enzyme
Gene name | pyk |
Synonyms | pykA |
Essential | no |
Product | pyruvate kinase |
Function | catabolic enzyme in glycolysis |
MW, pI | 61,9 kDa, 4.88 |
Gene length, protein length | 1755 bp, 585 amino acids |
Immediate neighbours | pfkA, ytzA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU29180
Phenotypes of a mutant
Unable to grow with non-PTS carbohydrates (such as glucitol or glycerol) as single carbon source.
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ADP + phosphoenolpyruvate --> ATP + pyruvate, the reaction is irreversible under physiological conditions
- Protein family: PEP-utilizing enzyme family (according to Swiss-Prot) pyruvate kinase family, (C-terminal section: PEP-utilizing enzyme family)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s): magnesium ion, potassium
- Effectors of protein activity: activated by PEP PubMed
- Interactions:
- Localization: cytoplasm PubMed
Database entries
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: 2.7.1.40
Additional information
Expression and regulation
- Sigma factor:
- Regulation: twofold induced by glucose PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP590 (cat), available in Stülke lab
- Expression vector:
Expression in E. coli, N-terminal His-tag: pGP1100 (in pWH844), available in Stülke lab
Expression in B. subtilis, native protein: pGP1411 (in pBQ200), available in Stülke lab
Expression in B. subtilis, N-terminal Strep-tag: pGP1409 (in pGP380), available in Stülke lab
Expression in B. subtilis, C-terminal Strep-tag: pGP1410 (in pGP382), available in Stülke lab
- lacZ fusion: see pfkA
- 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
Your additional remarks
References
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Lévine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6: 2157-2173 PubMed
- Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol Microbiol 41, 409-422.PubMed
- Jannière, L., Canceill, D., Suski, C., Kanga, S., Dalmais, B., Lestini, R., Monnier, A. F., Chapuis, J., Bolotin, A., Titok, M., Le Chatelier, E., and Ehrlich, S. D. (2007) Genetic evidence for a link between glycolysis and DNA replication. PLoS ONE 2, e447. PubMed
- Fry, B., Zhu, T., Domach, M. M., Koepsel, R. R., Phalakornkule, C., and Ataai, M. M. (2000) Characterization of growth and acid formation in a Bacillus subtilis pyruvate kinase mutant. Appl Env Microbiol 66: 4045-4049. PubMed
- Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed