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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: A novel thermostable chitinolytic machinery of Streptomyces sp. F-3 consisting of chitinases with different action modes

Fig. 1

Sequence analysis of the chitin degradation-related enzymes from Streptomyces sp. F-3. a Phylogenetic tree analysis of SsChi18A, SsChi18B, and SsChi18C. The putative catalytic domain was compared with those of S. coelicolor, C. japonicus, and S. marcescens. b The architecture of the secreted chitin degradation-related proteins of Streptomyces sp. F-3. The indicated domains are shown as follows: GH18, GH19, GH20, AA10, catalytic domains; CBM2 and CBM4, chitin-binding domain; FN3, fibronectin domain; SP, signal peptide. There are three domains in SsChi18A, including CBM2, FN3, and GH18 from the N-terminus to the C-terminus, respectively. SsChi18B contains CBM4, FN3, and GH18; SsChi18C contains CBM2 and GH18. SsChi19A and SsLPMO10A have only one catalytic domain from the GH19 and AA10 family, respectively. For SsGH20A, there are three domains, a bacterial type N-terminal β-hexosaminidase (GH20b) and two catalytic domains from glycoside hydrolase family 20

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