Figure 6

Structure-guided sequence analysis of the ABSs suggests a functional classification for gut bacterial GUSs. Relative occurrence of residues in loop 3 (or in the α2-helix loop) and loop 5 of the bacterial GUSs. Each of the five enzymes studied for this report was used as a query for an NCBI BLASTp search. After downloading the sequences sharing 55 to 95% identity, proteins derived from environmental or industrial sample were manually removed. The remaining enzymes were aligned in the T-Coffee-Expresso server, and a sequence logo for each group was created using WebLogo. The residues forming the ABS of each groups of GUSs are highlighted in black rectangles. The physicochemical properties of the side chains of the residues are shown in black (nonpolar, aliphatic residues), orange (aromatic), blue (polar, uncharged), and purple (polar, charged).