Difference between revisions of "Pgk"
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=== Extended information on the protein === | === Extended information on the protein === | ||
| − | * '''Kinetic information:''' | + | * '''Kinetic information:''' Two Substrate Reversible Michaelis-Menten (in ''G. stearothermophillus'') [http://www.ncbi.nlm.nih.gov/pubmed/7154941 PubMed] |
* '''Domains:''' | * '''Domains:''' | ||
| Line 68: | Line 68: | ||
* '''Modification:''' phosphorylation on Ser-183 AND Thr-299 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | * '''Modification:''' phosphorylation on Ser-183 AND Thr-299 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | ||
| − | * '''Cofactor(s):''' | + | * '''Cofactor(s):''' Mg2+ or Mn2+ [http://www.ncbi.nlm.nih.gov/pubmed/7154941 PubMed] |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| + | ** Inhibited by NDP and NMP [http://www.ncbi.nlm.nih.gov/pubmed/7154941 PubMed] | ||
* '''Interactions:''' | * '''Interactions:''' | ||
Revision as of 12:48, 10 June 2009
- Description: phosphoglycerate kinase, glycolytic/ gluconeogenic enzyme
| Gene name | pgk |
| Synonyms | |
| Essential | yes |
| Product | phosphoglycerate kinase |
| Function | enzyme in glycolysis/ gluconeogenesis |
| MW, pI | 42,0 kDa, 4.77 |
| Gene length, protein length | 1182 bp, 394 amino acids |
| Immediate neighbours | gapA, tpi |
| 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: BSU33930
Phenotypes of a mutant
- Essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + 3-phospho-D-glycerate = ADP + 1,3-bisphosphoglycerate (according to Swiss-Prot)
- Protein family: phosphoglycerate kinase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Two Substrate Reversible Michaelis-Menten (in G. stearothermophillus) PubMed
- Domains:
- nucleotide binding domain (ATP) (350–353)
- 2x substrate binding domain (21–23), (59–62)
- Cofactor(s): Mg2+ or Mn2+ PubMed
- Effectors of protein activity:
- Inhibited by NDP and NMP PubMed
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot), Cytoplasm (Homogeneous) PubMed
Database entries
- Swiss prot entry: P40924
- KEGG entry: [3]
- E.C. number: 2.7.2.3
Additional information
Expression and regulation
- Sigma factor: SigA
- Regulation: expression activated by glucose (2.8 fold) PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector: pGP1102 (N-terminal His-tag, in pWH844), pGP95 (N-terminal Strep-tag, in pGP172), pGP91 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab
- lacZ fusion: pGP514 (in pAC6), a series of promoter deletion variants is also available in pAC6, available in Stülke lab
- 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
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P 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)
Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537]
[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)
