Prokaryotic riboflavin biosynthesis protein: In molecular biology, the prokaryotic riboflavin biosynthesis protein is a bifunctional enzyme found in bacteria.Riboflavin synthaseRossmann foldFlavin groupOxidoreductase FAD-binding domain: B:7-104 B:7-104 B:7-104Bulbar palsyThiamine transporter: Members of this protein family have been assigned as thiamine transporters by a phylogenomic analysis of families of genes regulated by the THI element, a broadly conserved RNA secondary structure element through which thiamine pyrophosphate (TPP) levels can regulate transcription of many genes related to thiamine transport, salvage, and de novo biosynthesis. Species with this protein always lack the ThiBPQ ABC transporter.PteridineUltraviolet light therapyPheophorbidase: Pheophorbidase (, phedase, PPD) is an enzyme with system name pheophorbide-a hydrolase. This enzyme catalyses the following chemical reactionEgg white: Egg white is the common name for the clear liquid (also called the albumen or the glair/glaire) contained within an egg. In chickens it is formed from the layers of secretions of the anterior section of the hen's oviduct during the passage of the egg.MultivitaminPyridoxineTripartite ATP-independent periplasmic transporter: Tripartite ATP-independent periplasmic transporters (TRAP transporters) are a large family of solute transporters found in bacteria and archaea, but not in eukaryotes, that appear to be specific for the uptake of organic acids. They are unique in that they utilize a substrate binding protein (SBP) in combination with a secondary transporter.Pyridoxine 5'-phosphate oxidase: Pyridoxine 5’-phosphate oxidase is an enzyme that catalyzes several reactions in the vitamin B6 metabolism pathway. Pyridoxine-5-P oxidase catalyzes the terminal step (also the rate-limiting step) in vitamin B6 metabolism, the biosynthesis of pyridoxal-5’-phosphate, the biologically active form of vitamin B6 which acts as an essential cofactor.