pfam02887: PK_C (This model is not part of the current CDD release)
Pyruvate kinase, alpha/beta domain
Pyruvate kinase catalyzes the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP. The structure of several pyruvate kinases from various organisms have been determined. The protein comprises three-four domains: a small N-terminal helical domain (absent in bacterial PK), a beta/alpha barrel domain, a beta-barrel domain (inserted within the beta/alpha-barrel domain), and a 3-layer alpha/beta/alpha sandwich domain (represented in this entry). This domain is at the C-terminal of pyruvate kinases and contains the FBP (fructose 1,6-bisphosphate) binding site.
Jiyao W et al.(2023). "The conserved domain database in 2023.",