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PLoS One. 2016 Dec 8;11(12):e0168035. doi: 10.1371/journal.pone.0168035. eCollection 2016.

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

Author information

1
Instituto de Agroquímica y Tecnología de Alimentos, CSIC, Paterna, Valencia, Spain.
2
Center for Bioinformatics, University of Tübingen, Tübingen, Germany.

Abstract

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 β-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 β-galactosidases from β-glucuronidases, the diversification of β-galactosidases with different transglycosylation specificities, and the emergence of bicistronic β-galactosidases. This study also allows the identification of groups of functionally uncharacterized protein sequences with potential biotechnological interest.

PMID:
27930742
PMCID:
PMC5145203
DOI:
10.1371/journal.pone.0168035
[Indexed for MEDLINE]
Free PMC Article

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