Difference between revisions of "PfkA"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' ''Geobacillus stearothermophilus'' [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=58449 NCBI], | + | * '''Structure:''' ''Geobacillus stearothermophilus'' [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=58449 NCBI], Mutant form, complex with fructose-6-phosphate ''Geobacillus stearothermophilus'' [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=21480 NCBI] |
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34529] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34529] |
Revision as of 18:22, 13 January 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 |
Gene sequence (+200bp) | Protein sequence |
Genetic context |
Contents
The gene
Basic information
- Coordinates: 2985630 - 2986586
Phenotypes of a mutant
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
- Protein family: 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:
- Interactions: Pyk-PfkA
- Localization: cytoplasm PubMed
Database entries
- Structure: Geobacillus stearothermophilus NCBI, Mutant form, complex with fructose-6-phosphate Geobacillus stearothermophilus NCBI
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: [5]
Additional information
Expression and regulation
- Operon: pfkA pyk
- Sigma factor:
- Regulation: twofold induced by glucose
- Regulatory mechanism:
- Additional information:
Biological materials
Labs working on this gene/protein
Your additional remarks
References
- Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. subm.
- 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