Catalyzes the reversible phosphorylation of pyruvate and phosphate. ATP + phosphate + pyruvate = AMP + diphosphate + H(+) + phosphoenolpyruvate Activated by light-induced dephosphorylation. Inhibited by dark-induced phosphorylation. Both reactions are catalyzed by PDRP1 (By similarity). Homodimer. The N-terminal domain contains the ATP/Pi active site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate active site. Phosphorylation of Thr-466 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme (By similarity). The reaction takes place in three steps, each mediated by a carrier 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. Belongs to the PEP-utilizing enzyme family.