Photoreceptor proteins control vital cellular responses to light. The photocycle of the Slr1694 blue light using flavin photoreceptor is initiated by photoexcitation to a locally excited state within the flavin, followed by electron transfer from Tyr8 to the flavin and a proton relay from Tyr8 to the flavin via an intervening glutamine. Herein, the two-dimensional excited state potential energy surfaces associated with this double proton-transfer reaction are computed using the complete active space self-consistent-field method and multiconfigurational perturbation theory, including the protein and solvent environment with electrostatic embedding. The double proton-transfer reaction was found to be energetically unfavorable in the ground state and locally excited state but energetically favorable in the charge-transfer state corresponding to electron transfer from Tyr8 to the flavin. These results indicate that the proton-coupled electron transfer process is sequential, with electron transfer preceding double proton transfer, and that the double proton-transfer reaction is also sequential, with proton transfer from Tyr8 to Gln50 followed by proton transfer from Gln50 to the flavin. The barrier is lower for the first proton-transfer reaction, and both barriers are significantly influenced by geometrical changes within the active site, particularly the proton donor-acceptor distance as well as the protein environment. These calculations provide insight into the impact of protein reorganization and electrostatics on the excited electronic states prior to and during the double proton-transfer reaction. This interplay between excited states and the environment has implications for other photoreceptor proteins.