Catalyzes the production of firefly sulfoluciferin from luciferin using the sulfo-donor 3'-phosphoadenylyl sulfate (PAPS). Is also able to catalyze the reverse reaction, i.e. the adenosine 3',5'-bisphosphate-dependent desulfonation of sulfoluciferin. Can use either D- or L-luciferin stereoisomer as substrate. Sulfoluciferin, which is not a substrate of P.pyralis luciferase, likely serves as a luciferin storage form in fireflies. 3'-phosphoadenylyl sulfate + firefly D-luciferin = adenosine 3',5'-bisphosphate + firefly D-sulfoluciferin + H(+) 3'-phosphoadenylyl sulfate + firefly L-luciferin = adenosine 3',5'-bisphosphate + firefly L-sulfoluciferin + H(+) Sulfoluciferin formation is inhibited by the product adenosine 3',5'-bisphosphate. kcat is at least 3 sec(-1) with D-luciferin as substrate. LST may find use as a new tool to modulate existing biotechnological applications of the firefly bioluminescent system. Both D- and L-luciferin stereoisomers are found within the firefly. L-luciferin is the likely biosynthetic precursor to D-luciferin, though D-luciferin is the major stereoisomer by static abundance. Belongs to the sulfotransferase 1 family.