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The evolution of starch‐binding domain
Author(s) -
Janeček Štefan,
Ševčı́k Jozef
Publication year - 1999
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/s0014-5793(99)00919-9
Subject(s) - taxonomy (biology) , rhizopus oryzae , phylogenetic tree , amylase , biology , multiple sequence alignment , phylogenetics , rhizopus , enzyme , computational biology , evolutionary biology , domain (mathematical analysis) , starch , biochemistry , sequence alignment , genetics , peptide sequence , botany , gene , mathematical analysis , mathematics , fermentation
Amylolytic enzymes belonging to three distinct families of glycosidases (13, 14, 15) contain the starch‐binding domain (SBD) positioned almost exclusively at the C‐terminus. Detailed analysis of all available SBD sequences from 43 different amylases revealed its independent evolutionary behaviour with regard to the catalytic domains. In the evolutionary tree based on sequence alignment of the SBDs, taxonomy is respected so that fungi and actinomycetes form their own separate parts surrounded by bacteria that are also clustered according to taxonomy. The only known N‐terminal SBD from Rhizopus oryzae glucoamylase is on the longest branch separated from all C‐terminal SBDs. The 3‐dimensional (3‐D) structures of fungal glucoamylase and bacterial CGTase SBDs are compared and used to discuss the interesting SBD evolution.