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molecular biology Molecular biology is the branch of biology that seeks to understand the molecular basis of biological activity in and between cells, including biomolecular synthesis, modification, mechanisms, and interactions. The study of chemical and physi ...
, the BLUF domain (sensors of blue-light using FAD) is a
FAD A fad or trend is any form of collective behavior that develops within a culture, a generation or social group in which a group of people enthusiastically follow an impulse for a short period. Fads are objects or behaviors that achieve short- ...
-binding
protein domain In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of ...
. They are present in various proteins, primarily from
bacteria Bacteria (; singular: bacterium) are ubiquitous, mostly free-living organisms often consisting of one Cell (biology), biological cell. They constitute a large domain (biology), domain of prokaryotic microorganisms. Typically a few micrometr ...
, for example a BLUF domain is found at the N-terminus of the AppA protein from ''
Rhodobacter sphaeroides ''Rhodobacter sphaeroides'' is a kind of purple bacterium; a group of bacteria that can obtain energy through photosynthesis. Its best growth conditions are anaerobic phototrophy ( photoheterotrophic and photoautotrophic) and aerobic chemoheter ...
''. The BLUF domain is involved in sensing blue-light (and possibly
redox Redox (reduction–oxidation, , ) is a type of chemical reaction in which the oxidation states of substrate change. Oxidation is the loss of electrons or an increase in the oxidation state, while reduction is the gain of electrons or a ...
) using FAD and is similar to the flavin-binding
PAS domain A Per-Arnt-Sim (PAS) domain is a protein domain found in all kingdoms of life. Generally, the PAS domain acts as a molecular sensor, whereby small molecules and other proteins associate via binding of the PAS domain. Due to this sensing capabilit ...
s and cryptochromes. The predicted secondary structure reveals that the BLUF domain has a novel FAD-binding fold.


References

{{InterPro content, IPR007024 Protein domains