The gene encoding an acid endo-1,4-β-glucanase from sp. KSM-330 was cloned into the III site of pBR322 and expressed in HB101. The recombinant plasmid contained a 3.1 kb III insert, 1.8 kb of which was sufficient for the expression of endoglucanase activity in HB101. Nucleotide sequencing of this region (1816 bp) revealed an open reading frame of 1389 bp. The protein deduced from this sequence was composed of 463 amino acids with an of 51882. The deduced amino acid sequence from amino acids 56 through 75 coincided with the amino-terminal sequence of the endoglucanase, Endo-K, purified from culture of sp. KSM-330. The deduced amino acid sequence of Endo-K had 30% homology with that of the enzyme from NCIB 10682 and 25% homology with that of the enzyme from CB4. However, the Endo-K protein exhibited no homology with respect to either the nucleotide or the amino acid sequences of other endoglucanases from that had been previously characterized. These results indicate that the gene for Endo-K in sp. KSM-330 has evolved from an ancestral gene distinct from that of other endoglucanases.


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