Formation of phosphoenolpyruvate. ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate Activated by light-induced dephosphorylation. Inhibited by dark-induced phosphorylation. Both reactions are catalyzed by PDRP1. Homotetramer. The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site. Phosphorylation of Thr-536 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme. The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain (By similarity). A short cytoplasmic isoform may be produced by alternative promoter usage. Belongs to the PEP-utilizing enzyme family.