BLUF domains exist in various proteins from bacteria and lower eukaryotes. the BLUF domain (sensors of blue-light using FAD) is a FAD-binding protein domain. They are present in various proteins, primarily from bacteria. The BLUF domain is involved in sensing blue-light (and possibly redox) using FAD and is similar to the flavin-binding PAS domains and cryptochromes. The predicted secondary structure reveals that the BLUF domain has a novel FAD-binding fold. They are completely modular and can transmit signals to output units with different structures and functions, most of which are related to nucleotide metabolism.

BLUF Domain is one of the optogenetics switches available at Creative BioMart. We provide plenty of services and related solutions based on the euPAC, PixD/ PixE, BlrP1, EB1, NgPAC, bPAC (BlaC) switch system.

euPAC Switch System

Overview

Photoactivated adenylate cyclase is a blue light receptor, which is composed of four flavin protein subunits-two PACSα and two PACSβ. Each subunit consists of two BLUF (blue light sensor using FAD) domains that bind fad for photoreceptor and two cyclase domains to catalyze the conversion of ATP to cAMP. The catalytic function of PAC α and PAC β is independent, and their ability to form cAMP can be strongly and repeatedly increased by blue light.

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