BLUF Domain

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

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.

euPAC PixD/PixE BlrP1 EB1 NgPAC bPAC (BlaC)
Photoreceptor euPACα, euPACβ PixD BlrP1 EB1 NgPAC bPAC (BlaC)
Binding partner / PixE / / /
Cofactor FAD or FMN FAD or FMN FAD or FMN  FAD FAD FAD or FMN
Source organism Euglena gracilis Synechocystis sp. PCC 6803 Klebsiella pneumoniae Magnetococcus marinus Naegleria gruberi Beggiatoa sp.
Mode of action cAMP production Heterooligomerization, dissociation c-di-GMP hydrolysis c-di-GMP hydrolysis cAMP production cAMP production
Excitation wavelength 450 nm 450 nm 450 nm 450 nm 450 nm 450 nm
Reversion wavelength Dark Dark Dark Dark Dark Dark
Excitation time Seconds Seconds Seconds
Reversion time Seconds Minutes Tens of seconds

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