A putative novel starch-binding domain revealed by in silico analysis of the N-terminal domain in bacterial amylomaltases from the family GH77

Filip Mareček, Marie Sofie Møller, Birte Svensson, Štefan Janeček*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The family GH77 contains 4-α-glucanotransferase acting on α-1,4-glucans, known as amylomaltase in prokaryotes and disproportionating enzyme in plants. A group of bacterial GH77 members, represented by amylomaltases from Escherichia coli and Corynebacterium glutamicum, possesses an N-terminal extension that forms a distinct immunoglobulin-like fold domain, of which no function has been identified. Here, in silico analysis of 100 selected sequences of N-terminal domain homologues disclosed several well-conserved residues, among which Tyr108 (E. coli amylomaltase numbering) may be involved in α-glucan binding. These N-terminal domains, therefore, may represent a new type of starch-binding domain and define a new CBM family. This hypothesis is supported by docking of maltooligosaccharides to the N-terminal domain in amylomaltases, representing the four clusters of the phylogenetic tree. The online version contains supplementary material available at 10.1007/s13205-021-02787-8.
Original languageEnglish
Article number229
Journal3 Biotech
Volume11
Issue number5
Number of pages14
ISSN2190-572X
DOIs
Publication statusPublished - 2021

Keywords

  • Amylomaltase
  • Family GH77
  • N-termial domain
  • Starch-binding domain
  • CBM families
  • Conserved sequence regions
  • Evolutionary relatedness

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