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. 2019 Aug 1;9:11195. doi: 10.1038/s41598-019-47637-z

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© The Author(s) 2019

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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Alignment of the predicted amino acid sequence of XynA3 and its closest relatives from the GenBank databases. The closest sequences shown are: 1,4-beta-xylanase from Paenibacillaceae bacterium JTherm derived from compost metagenome (PDO11710); Paenibacillus ihumii (WP_055108594); Paenibacillus kribbensis (WP_094156067); Bacillus pseudalcaliphilus (KMK76771); Paenibacillus campinasensis (WP_095266106 and AEI54132) and synthetic construct (ACJ67896). Gaps are indicated by dashes. Asterisks indicate identical amino acids. The black boxes indicate conserved regions and the secondary structure elements are selected by black lines. Asparagine (N) present in alkaline xylanases is shown in bold. The glutamic acid residues corresponding to Glu 122 and 212 of XynA3, essential for the catalytic activity, are highlighted in green.

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