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The evolution of putative starch‐binding domains
Author(s) -
Machovič Martin,
Janeček Štefan
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.041
Subject(s) - biochemistry , isoamylase , pullulanase , biology , glycogen debranching enzyme , conserved sequence , starch , enzyme , glycogen branching enzyme , glycogen synthase , amylase , peptide sequence , gene
The present bioinformatics analysis was focused on the starch‐binding domains (SBDs) and SBD‐like motifs sequentially related to carbohydrate‐binding module (CBM) families CBM20 and CBM21. Originally, these SBDs were known from microbial amylases only. At present homologous starch‐ and glycogen‐binding domains (or putative SBD sequences) have been recognised in various plant and animal proteins. The sequence comparison clearly showed that the SBD‐like sequences in genethonin‐1, starch synthase III and glucan branching enzyme should possess the real SBD function since the two tryptophans (or at least two aromatics) of the typical starch‐binding site 1 are conserved in their sequences. The same should apply also for the sequences corresponding with the so‐called KIS‐domain of plant AKINβγ protein that is a homologue of the animal AMP‐activated protein kinase (AMPK). The evolutionary tree classified the compared SBDs into three distinct groups: (i) the family CBM20 (the motifs from genethonins, laforins, starch excess 4 protein, β‐subunits of the animal AMPK and all plant and yeast homologues, and eventually from amylopullulanases); (ii) the family CBM21 (the motifs from regulatory subunits of protein phosphatase 1 together with those from starch synthase III); and (iii) the (CBM20 + CBM21)‐related group (the motifs from the pullulanase subfamily consisting of pullulanase, branching enzyme, isoamylase and maltooligosyl trehalohydrolase).