Abstract
BackgroundGlycoside hydrolase family 32 (GH32) enzymes cleave the glycosidic bond between two monosaccharides or between a carbohydrate and an aglycone moiety. GH32 enzymes have been studied in prokaryotes and in eukaryotes but not in viruses.FindingsThis is the first analysis of GH32 enzymes in Bacillus subtilis phage SP10, ϕNIT1 and SPG24. Phylogenetic analysis, molecular docking and secretability predictions suggest that phage GH32 enzymes function as levan (fructose homopolysaccharide) fructotransferase.ConclusionsWe showed that viruses also contain GH32 enzymes and that our analyses in silico strongly suggest that these enzymes function as levan fructotransferase.Electronic supplementary materialThe online version of this article (doi:10.1186/s12985-015-0373-6) contains supplementary material, which is available to authorized users.
Highlights
Glycoside hydrolase family 32 (GH32) enzymes cleave the glycosidic bond between two monosaccharides or between a carbohydrate and an aglycone moiety
They play a major role in the lateral gene transfer (LGT) [2]
The genomes of some phages have been shown to contain host-like genes known as auxiliary metabolic genes (AMGs) [3]
Summary
Glycoside hydrolase family 32 (GH32) enzymes cleave the glycosidic bond between two monosaccharides or between a carbohydrate and an aglycone moiety. The present report focuses on an AMG, a glycoside hydrolase 32 (GH32) family protein, observed for the first time in a viral genome and shown to have been acquired by LGT from the bacterial host of a phage. * Correspondence: halim.maaroufi@ibis.ulaval.ca 1Institut de biologie intégrative et des systèmes (IBIS), Plate-Forme de Bio-Informatique, Université Laval, Pavillon Charles-Eugène Marchand, 1030 Avenue de la médecine, Québec, Québec G1V 0A6, Canada Full list of author information is available at the end of the article nucleophile and the EC motif as the acid/base catalyst [7].
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