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Ylr456w and Ypr172w annotations are inferred from only one domain involved in pyridoxamine 5’-phosphate function.

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posted on 2015-09-01, 03:06 authored by Tatiana Domitrovic, Diana P. Raymundo, Tiago Fernandes da Silva, Fernando L. Palhano

(A) Pfam protein family database profile of the proteins Ylr456w, Ypr172w and Pdx3. PF01243 Pyridox_oxidase domain and PF10590 Pyridox_oxidase C-terminal dimerization domain are located on the N-terminal and C-terminal, respectively. (B) Vitamin B6 biosynthesis. (C) Crystal structure of the P(N/M)P oxidase Pdx3 (pdb 1CI0) from S. cerevisiae. The P(N/M)P oxidase protein is a homodimer (monomers colored in cyan and magenta) that binds two FMN molecules. The side chain of the conserved residues that contact FMN and their ligands are shown in black (residues R73, L76, K96, Q153, S154, E197, W199, R205, H207, R209 and P228 are indicated by red asterisks in Fig 4). The second structure (bottom) was colored to show the tridimensional position of the amino-acid residues within PF01243 in green and PF10590 in red.