Difference between revisions of "PfkA"
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Revision as of 11:16, 10 June 2009
- Description: phosphofructokinase, glycolytic enzyme
| Gene name | pfkA |
| Synonyms | pfk |
| Essential | yes |
| Product | 6-phosphofructokinase |
| Function | catabolic enzyme in glycolysis |
| MW, pI | 34,1 kDa, 6.14 |
| Gene length, protein length | 957 bp, 319 amino acids |
| Immediate neighbours | accA, pyk |
| 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: BSU29190
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 + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate (according to Swiss-Prot) ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
- Protein family: phosphofructokinase family (according to Swiss-Prot) phosphofructokinase family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Allosteric Regulation (Reversible) PubMed
- Domains:
- 3 x nucleotide binding domain (ATP) (21–25), (154–158), (171–187)
- Modification:
- Cofactor(s): ATP
- Effectors of protein activity:
- Inhibited by citrate, PEP (Hill Coefficient 3) and Ca2+ (competes with Mg2+) in B. licheniformes PubMed.
- Inhibited by ATP (competitively) and f6p (non-competitively) in B. stearothermophillus PubMed
- Activated by GDP and ADP in lower concentrations (1mM); above that inhibition, competing with the ATP for the binding site (in B. stearothermophillus) PubMed
- Localization: cytoplasm (according to Swiss-Prot), Cytoplasm (Homogeneous) PubMed
Database entries
- Structure: 1MTO (mutant, complex with fructose-6-phosphate, Geobacillus stearothermophilus), 4PFK (Geobacillus stearothermophilus), Geobacillus stearothermophilus NCBI, Mutant form, complex with fructose-6-phosphate Geobacillus stearothermophilus NCBI
- Swiss prot entry: O34529
- KEGG entry: [3]
- E.C. number: 2.7.1.11 1 2.7.1.11]
Additional information
Expression and regulation
- Sigma factor:
- Regulation: twofold induced by glucose PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector: pGP393 (N-terminal His-tag, in pWH844), pGP87 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), 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
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
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)
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)
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)
X Zhu, M Byrnes, J W Nelson, S H Chang
Role of glycine 212 in the allosteric behavior of phosphofructokinase from Bacillus stearothermophilus.
Biochemistry: 1995, 34(8);2560-5
[PubMed:7873536]
[WorldCat.org]
[DOI]
(P p)
M Byrnes, X Zhu, E S Younathan, S H Chang
Kinetic characteristics of phosphofructokinase from Bacillus stearothermophilus: MgATP nonallosterically inhibits the enzyme.
Biochemistry: 1994, 33(11);3424-31
[PubMed:8136379]
[WorldCat.org]
[DOI]
(P p)
