Difference between revisions of "PfkA"
(→Biological materials) |
|||
Line 78: | Line 78: | ||
** Activated by NH4+ [http://www.ncbi.nlm.nih.gov/pubmed/7873536 PubMed] | ** Activated by NH4+ [http://www.ncbi.nlm.nih.gov/pubmed/7873536 PubMed] | ||
− | * '''Interactions:''' [[PfkA]]-[[Pgm]], [[PfkA]]-[[Eno]], [[PfkA]]-[[Rny]], [[PfkA]]-[[PnpA]], [[PfkA]]-[[RnjA]] | + | * '''Interactions:''' [[PfkA]]-[[Pgm]] {{PubMed|19193632}}, [[PfkA]]-[[Eno]] {{PubMed|19193632}}, [[PfkA]]-[[Rny]] {{PubMed|19193632}}, [[PfkA]]-[[PnpA]], [[PfkA]]-[[RnjA]] {{PubMed|19193632}}, [[Eno]]-[[CshA]] {{PubMed|20572937}} |
* '''Localization:''' cytoplasm (Homogeneous) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] | * '''Localization:''' cytoplasm (Homogeneous) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed] | ||
Line 136: | Line 136: | ||
=References= | =References= | ||
− | <pubmed> 16479537,19193632, 11489127, 8136379, 7873536 4269800 20473954 </pubmed> | + | <pubmed> 16479537,19193632, 11489127, 8136379, 7873536 4269800 20473954 20572937</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 09:29, 25 June 2010
- Description: phosphofructokinase, glycolytic enzyme
Gene name | pfkA |
Synonyms | pfk |
Essential | no |
Product | 6-phosphofructokinase |
Function | catabolic enzyme in glycolysis |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism, Sugar catabolism | |
MW, pI | 34,1 kDa, 6.14 |
Gene length, protein length | 957 bp, 319 amino acids |
Immediate neighbours | pyk, accA |
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 according to Kobayashi et al., dispensable according to Munoz-Marquez and Ponce-Rivas
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)
- 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): Mg2+
- 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 G. stearothermophillus PubMed
- Activated by GDP and ADP in lower concentrations (1mM); above that inhibition, competing with the ATP for the binding site (in G. stearothermophillus) PubMed
- Activated by NH4+ PubMed
- Interactions: PfkA-Pgm PubMed, PfkA-Eno PubMed, PfkA-Rny PubMed, PfkA-PnpA, PfkA-RnjA PubMed, Eno-CshA PubMed
- Localization: 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
- UniProt: O34529
- KEGG entry: [3]
- E.C. number: 2.7.1.11
Additional information
PfkA is a moonlighting protein. PubMed
Expression and regulation
- Sigma factor:
- Regulation:
- twofold induced by glucose PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Expression vector:
- for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP87, available in Stülke lab
- for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP393, available in Stülke lab
- for expression in B. subtilis, in pBQ200: pGP1422, 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