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Vol 50(2016) N 1 p. 132-140; DOI 10.1134/S0026893315060205  D.G. Naumoff* GH10 Family of Glycoside Hydrolases: Structure and Evolutionary Connections Winogradsky Institute of Microbiology, Russian Academy of Sciences, Moscow, 117312 Russia*daniil_naumoff@yahoo.com Received - 2015-04-08; Accepted - 2015-05-05 Evolutionary connections were analyzed for endo-β-xylanases, which possess the GH10 family catalytic domains. A homology search yielded thrice as many proteins as are available from the Carbohydrate-Active Enzymes (CAZy) database. Lateral gene transfer was shown to play an important role in evolution of bacterial proteins of the family, especially in the phyla Acidobacteria, Cyanobacteria, Planctomycetes, Spirochaetes, and Verrucomicrobia. In the case of Verrucomicrobia, 23 lateral transfers from organisms of other phyla were detected. Evolutionary relationships were observed between the GH10 family domains and domains with the TIM-barrel tertiary structure from several other glycosidase families. The GH39 family of glycoside hydrolases showed the closest relationship. Unclassified homologs were grouped into 12 novel families of putative glycoside hydrolases (GHL51-GHL62). glycoside hydrolase, endoglycosidase, β-xylanase, GH10 family, GH-A clan, PSI-BLAST, PSI Protein Classifier, protein evolution, search for homologs, gene annotation, lateral transfer, carbohydrate metabolism, xylan utilization, new protein families, GHL families, protein superfamily, PF00331 family, Verrucomicrobia |
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