Analysis of Domain Architecture and Phylogenetics of Family 2 Glycoside Hydrolases (GH2)

作者：Talens Perales David; Gorska Anna; Huson Daniel H; Polaina Julio; Marin Navarro Julia^*

来源：PLos One, 2016, 11(12): e0168035.

DOI：10.1371/journal.pone.0168035

In this work we report a detailed analysis of the topology and phylogenetics of family 2 glycoside hydrolases (GH2). We distinguish five topologies or domain architectures based on the presence and distribution of protein domains defined in Pfam and Interpro databases. All of them share a central TIM barrel (catalytic module) with two beta-sandwich domains (non-catalytic) at the N-terminal end, but differ in the occurrence and nature of additional non-catalytic modules at the C-terminal region. Phylogenetic analysis was based on the sequence of the Pfam Glyco_hydro_2_C catalytic module present in most GH2 proteins. Our results led us to propose a model in which evolutionary diversity of GH2 enzymes is driven by the addition of different non-catalytic domains at the C-terminal region. This model accounts for the divergence of beta-galactosidases from beta-glucuronidases, the diversification of beta-galactosidases with different transglycosylation specificities, and the emergence of bicistronic beta-galactosidases. This study also allows the identification of groups of functionally uncharacterized protein sequences with potential biotechnological interest.

• 出版日期2016-12-8
• 单位上海生物信息技术研究中心