The nucleotide sequence of the gene coding for the thermostable exo-1,4-β-glucanase Avicelase II of was determined. The gene consists of an ORF of 2742 bp which encodes a preprotein of 914 amino acids with a molecular mass of 103 kDa. The signal-peptide cleavage site was identified by comparison with the N-terminal amino acid sequence of Avicelase II purified from . The gene is located in close vicinity to the gene coding for the endo-1,4-β-glucanase Avicelase I. The CelY-encoding sequence was isolated from genomic DNA of with the PCR technique. The recombinant enzyme produced in as a LacZ'-CelY fusion protein could be purified using a simple two-step procedure. The properties of CelY proved to be consistent with those of Avicelase II purified from . Sequence comparison revealed that CelY consists of an N-terminal catalytic domain flanked by a domain of 95 amino acids with unknown function joined to a type III cellulose-binding domain. The catalytic domain belongs to the recently proposed family L of cellulases (family 48 of glycosyl hydrolases).


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