Figure 2.

A multiple sequence alignment of BioHx and other known bacterial BioH proteins. The numbering of sequences is indicated above the alignments. The starting and ending residue numbers of each protein sequence used in this study are indicated before and after each sequence. Identical amino acid residues as well as the conserved ones (>50% of the sequences) are highlighted in black and in grey, respectively, with the consensus sequence shown below each alignment. The pentapeptide motif and catalytic triad are shown in boxes. The BioH sequences chosen for the analysis are from the GenBank database, except 1M33 from the PDB database: ABY81653, Serratia sp. SES-01; BAB39459, Kurthia sp. 538-KA26; Q8GHL1, Serratia marcescens Sr41; P13001, Escherichia coli K-12; 1M33, Escherichia coli DH5α; BioHx, obtained in this study.

Shi et al. BMC Biotechnology 2013 13:13   doi:10.1186/1472-6750-13-13
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