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. 2020 Jun 10;10:9390. doi: 10.1038/s41598-020-66293-2

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Modelling of AlyA1 and Alg2A based on A1-II’ (2CWS) crystal structure. (A,B) Models of protein structures of AlyA1 and Alg2A, respectively. Loops involved in the interaction with the substrate are labeled in light blue. In dark blue we show the conserved residues in the cavity close to the putative active site. In red, non-conserved residues of the cavity. (C) ClustalW alignment of AlyA1 (WP_013992548.1), A1-II’ and Alg2A (AEB69783.1) protein sequences. Shadowed in dark blue are the residues that form the conserved substrate cavity and in red the important but non-conserved residues of this cavity. Loops important for substrate binding are labelled in light blue. Highly conserved regions described for PL7 family are marked with an asterisk. In bright pink, we show the unique aa sequences present in Alg2A or AlyA1 sequences.