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


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

SUBMITTER: Talens-Perales D 

PROVIDER: S-EPMC5145203 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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

Talens-Perales David D   Górska Anna A   Huson Daniel H DH   Polaina Julio J   Marín-Navarro Julia J  

PloS one 20161208 12


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. Phy  ...[more]

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