In Silico Exploration of the Fructose-6- Phosphate Phosphorylation
Step in Glycolysis: Genomic Evidence of the Coexistence of an Atypical
ATP-Dependent Along with a PPi-Dependent Phosphofructokinase in
Propionibacterium freudenreichii subsp. shermanii
Affiliations: INRA-STLO, 65 rue de Saint-Brieuc, 35042 Rennes cedex,
France | Institut Pasteur, Génopole, Intégration
et Analyse Génomiques, 25/28 rue du Dr E. Roux, 75015 Paris cedex,
France | UMR PBV, INRA - Universités Bordeaux 1 - Victor
Ségalen Bordeaux 2, BP 81, 33883 Villenave d'Ornon cedex, France | Centre Bioinformatique de Bordeaux, 146 rue Léo
Saignat, 33076 Bordeaux cedex, France | Danisco, BP 10, 86220 Dangé Saint Romain,
France | Genome Express, 11 chemin des Prés, 38944
Meylan, France
Abstract: We performed a detailed bioinformatic study of the catalytic step of
fructose-6-phosphate phosphorylation in glycolysis based on the raw genomic
draft of Propionibacterium freudenreichii subsp. shermanii (P. shermanii)
ATCC9614 [Meurice et al., 2004]. Our results provide the first in silico
evidence of the coexistence of genes coding for an ATP-dependent
phosphofructokinase (ATP-PFK) and a PPi-dependent phosphofructokinase
(PPi-PFK), whereas the fructose-1,6-bisphosphatase (FBP) and ADP-dependent
phosphofructokinase (ADP-PFK) are absent. The deduced amino acid sequence
corresponding to the PPi-PFK (AJ508922) shares 100% similarity with the already
characterised propionibacterial protein (P29495; Ladror et al., 1991]. The
unexpected ATP-PFK gene (AJ509827) encodes a protein of 373 aa which is highly
similar (50% positive residues) along at least 95% of its sequence length to
different well-characterised ATP-PFKs. The characteristic PROSITE pattern
important for the enzyme function of ATP-PFKs (PS00433) was conserved in the
putative ATP-PFK sequence: 8 outof.
