InterPro domain: IPR012004

Phosphofructokinase (PFK) catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate, which then enters the Embden-Meyerhof pathway. PFK is a key regulatory enzyme in glycolysis [ 1 ].

This family consists of a group of plant and bacterial pyrophosphate-dependent phosphofructokinases related to TP0108 from Treponema [ 2 ]. The bacterial versions are non-allosteric dimers, while the plant versions are allosteric heterotetramers [ 3 ]. They belong to the PFK domain superfamily of proteins, which also includes prokaryotic ( IPR012003 ) and eukaryotic ATP-dependent PFKs ( IPR009161 ). The membership of this group largely resembles group B1 PFKs [ 4 ].

1. The biochemical properties and phylogenies of phosphofructokinases from extremophiles. Extremophiles 5, 357-73
2. Different physiological roles of ATP- and PP(i)-dependent phosphofructokinase isoenzymes in the methylotrophic actinomycete Amycolatopsis methanolica. J. Bacteriol. 183, 7231-40
3. The structure of a pyrophosphate-dependent phosphofructokinase from the Lyme disease spirochete Borrelia burgdorferi. Structure 10, 659-71
4. Rampant horizontal gene transfer and phospho-donor change in the evolution of the phosphofructokinase. Gene 318, 185-91