Difference between revisions of "PfkA"
| Line 35: | Line 35: | ||
=== Basic information === | === Basic information === | ||
| − | * '''Locus tag:''' | + | * '''Locus tag:''' BSU29190 |
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| Line 82: | Line 82: | ||
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34529 O34529] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34529 O34529] | ||
| − | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+ | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU29190] |
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.1.11 2.7.1.11] 1 2.7.1.11] | * '''E.C. number:''' [http://www.expasy.org/enzyme/2.7.1.11 2.7.1.11] 1 2.7.1.11] | ||
Revision as of 11:55, 3 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:
- Domains:
- 3 x nucleotide binding domain (ATP) (21–25), (154–158), (171–187)
- Modification:
- Cofactor(s): ATP
- Effectors of protein activity: inhibited by citrate, ATP, PEP, Ca2+, and others (in B. licheniformes) 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)
