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. 2006 Jan;74(1):537–548. doi: 10.1128/IAI.74.1.537-548.2006

FIG. 9.

FIG. 9.

Alignment of A. hydrophila Gne, its bacterial homologs, and other characterized bacterial epimerases. The A. hydrophila Gne (AH3) was aligned with its homologs in B. subtilis (BS), Haemophilus influenzae (HI), and Y. enterocolitica (YE), as well as the UDP-GlcNAc epimerase WbpP from P. aeruginosa (PA). Identical amino acids are shown on a black background, and similar residues are shown on a gray background. Residues that are involved in nucleotide binding (underlined) and amino acids that have been shown to be important for catalysis (asterisk) are indicated. Amino acids that are underlined twice are thought to be involved in substrate binding. Multiple-sequence alignments were performed with ClustalW available at the ExPASy molecular biology server (au.expasy.org).