PfkA

• 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

The gene

Basic information

• Coordinates: 2985630 - 2986586

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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: inhibited by citrate, ATP, PEP, Ca2+, and others (in B. licheniformes) PubMed

• 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]

Expression and regulation

• Operon: pfkA pyk

• Sigma factor:

• Regulation: twofold induced by glucose

• 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

• lacZ fusion: pGP511 (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

Jörg Stülke, University of Göttingen, Germany Homepage

References

1. 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.
2. 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