ArticleApplied microbiology and biotechnology2024
Two newly established and mutually related subfamilies GH13_48 and GH13_49 of the α-amylase family GH13.
Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- Comparative Analysis of Carbohydrate-Active Enzyme (CAZyme) Diversity Across Diverse Algal Lineages.Marine biotechnology (New York, N.Y.) · 2026Article
- Structure and Function of Honeybee α-Amylase of Glycoside Hydrolase Family 13 Subfamily 15.Molecules (Basel, Switzerland) · 2026Article
- Genome description of a potentially novel species of Rossellomorea sp. strain H39_3 isolated from the Hindon River, India.Access microbiology · 2026Article
- The role of N185D substitution in enhancing activity of BaqA∆C α-amylase.Scientific reports · 2025Article
- ez-CAZy a reference annotation database for linking glycoside hydrolase sequence to enzymatic activity.Scientific reports · 2025Article
- Exploring the Microbiome and Functional Metabolism of Fermented Camel Milk (Shubat) Using Metagenomics.Foods (Basel, Switzerland) · 2025Article
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Abstract
Currently, the main α-amylase family GH13 has been divided into 47 subfamilies in CAZy, with new subfamilies regularly emerging. The present in silico study was performed to highlight the groups, represented by the maltogenic amylase from Thermotoga neapolitana and the α-amylase from Haloarcula japonica, which are worth of creating their own new GH13 subfamilies. This enlarges functional annotation and thus allows more precise prediction of the function of putative proteins. Interestingly, those two share certain sequence features, e.g. the highly conserved cysteine in the second conserved sequence region (CSR-II) directly preceding the catalytic nucleophile, or the well-preserved GQ character of the end of CSR-VII. On the other hand, the two groups bear also specific and highly conserved positions that distinguish them not only from each other but also from representatives of remaining GH13 subfamilies established so far. For the T. neapolitana maltogenic amylase group, it is the stretch of residues at the end of CSR-V highly conserved as L-[DN]. The H. japonica α-amylase group can be characterized by a highly conserved [WY]-[GA] sequence at the end of CSR-II. Other specific sequence features include an almost fully conserved aspartic acid located directly preceding the general acid/base in CSR-III or well-preserved glutamic acid in CSR-IV. The assumption that these two groups represent two mutually related, but simultaneously independent GH13 subfamilies has been supported by phylogenetic analysis as well as by comparison of tertiary structures. The main α-amylase family GH13 has thus been expanded by two novel subfamilies GH13_48 and GH13_49. KEY POINTS: • In silico analysis of two groups of family GH13 members with characterized representatives • Identification of certain common, but also some specific sequence features in seven CSRs • Creation of two novel subfamilies-GH13_48 and GH13_49 within the CAZy database.
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