Multiple sequence alignment of MPT-adenylyl-transferases from different organisms.

<p>Corresponding MPT-adenylyl-transferases are abbreviated as follows: PfuMoaB, <i>Pyrococcus furious</i>; StoMoaB, <i>Sulfolobus tokodaii</i>; BceMoaB, <i>Bacillus cereus;</i> EcoMogA and EcoMoaB, <i>Escherichia coli</i>; TthMogA, <i>Thermus thermophilus</i>; AaeMogA, <i>Aquifex aeolicus</i>; <i>Arabidopsis thaliana</i>; HsaGephG, <i>Homo sapiens</i>. Secondary structure elements of PfuMoaB are shown. The conserved MPT-binding motif GGTG is highlighted with a red box, the conserved aspartate residue coordinating Mg²⁺- ion with a green box <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0086030#pone.0086030-Kuper1" target="_blank">[6]</a>, residues of PfuMoaB α3-helix with a blue box. Highly conserved residues are depicted in white letters and black background; semi-conserved residues are shadowed in grey. Consensus threshold was set to 0.8. Sequences were aligned with Clustal Omega <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0086030#pone.0086030-Sievers1" target="_blank">[62]</a>,and modified with BoxShade server (Swiss Institute of Bioinformatics).