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. 2022 Sep 6;8:71. doi: 10.1038/s41522-022-00333-9

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© The Author(s) 2022

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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Fig. 4 — UGL D-4,5-unsaturated β-glucuronyl hydrolase, Endochit endochitinase, MCP methyl-accepting chemotaxis protein, Ni-SOD nickel-containing superoxide dismutase, LBD ligand-binding domain, SD signaling domain, TM transmembrane, HAMP histidine kinase, adenyl cyclase, methyl-accepting chemotaxis protein and phosphatase. Representative substrates of glycoside hydrolases (GHs) encoded by AMGs and the associated simplest products are shown. The cleavage points of the substrates are indicated by red arrows. The computational protein models of GHs, MCPs and Ni-SOD are displayed. Representative ligands of MCPs and the active site of Ni-SOD are shown. *, if the products of GHs or representative ligands of MCPs can be utilized directly by SRMs to reduce sulfate, their names are in blue. Additional details are presented in Supplementary Tables 10 and 11.