Structure of the photoactivated adenylyl cyclase OaPAC forming a homodimer. FMN: flavin mononucleotide, the light-absorbing pigment. [1]
Photoactivated adenylyl cyclase (PAC) is a protein consisting of an adenylyl cyclaseenzyme domain directly linked to a BLUF (blue light receptor using FAD) type light sensor domain. When illuminated with blue light, the enzyme domain becomes active and converts ATP to cAMP, an important second messenger in many cells. In the unicellular flagellate Euglena gracilis, PACα and PACβ (euPACs) serve as a photoreceptor complex that senses light for photophobic responses and phototaxis.[2] Small but potent PACs were identified in the genome of the bacteria Beggiatoa (bPAC) and Oscillatoria acuminata (OaPAC).[3][1] While natural bPAC has some enzymatic activity in the absence of light, variants with no dark activity have been engineered (PACmn).[4]