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. 2017 Feb 14;15(2):37. doi: 10.3390/md15020037

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© 2017 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Multiple alignment for amino acid sequences of FlAld and other KDPG aldolases. Gray box and closed triangles indicate catalytic and substrate-recognition residues of KDPG aldolase from E. coli [44,45], respectively. FlAld, KDPG aldolase from Flavobacterium sp. strain UMI-01 (GenBank accession number, BAQ25539); Lacin, KDPG aldolase-like protein from Lacinutrix sp. 5H-3-7-4 (GenBank accession number, AEH01606); Dokdo, KDPG aldolase-like protein from Dokdonia sp. MED134 (GenBank accession number, WP_013749799); Grame, KDPG aldolase-like protein from G. forsetii KT0803 (GenBank accession number, CAL66136); Sacch, KDPG aldolase from S. degradans 2-40^T (GenBank accession number, ABD80644) [25]; Esche, KDPG aldolase from E. coli (GenBank accession number, WP_000800517) [44,45]; Zymom, KDPG aldolase from Zymomonas mobilis (GenBank accession number, S18559) [44]; Pseud, KDPG aldolase from Pseudomonas putida (GenBank accession number, WP_016501275) [44,46].