Cloning and characterization of the gene encoding endo-beta-1,3-glucanase from Arthrobacter sp. NHB-10.
The gluA gene, encoding an endo-beta-1,3-glucanase from Arthrobacter sp. (strain NHB-10), was cloned and analyzed. The deduced endo-beta-1,3-glucanase amino acid sequence was 750 amino acids long and contained a 42 amino acid signal peptide with a mature protein of 708 amino acids. There was no similarity to known endo-beta-1,3-glucanases, but GluA was partially similar to two fungal exo-beta-1,3-glucanases in glycoside hydrolase (GH) family 55. Of five possible residues for catalysis and two motifs in two beta-helix heads of GH family 55, three residues and one motif were conserved in GluA, suggesting that GluA is the first bacterial endo-beta-1,3-glucanase in GH family 55. Significant similarity was also found to two proteins of unknown function from Streptomyces coelicolor A3(2) and S. avermitilis.
Okazaki
Katsuichiro
K
Department of Applied Biological Science, Faculty of Agriculture, Kagawa University Japan. okazaki@ag.kagawa-u.ac.jp
Nishimura
Naohito
N
Matsuoka
Fumiyoshi
F
Hayakawa
Shigeru
S
D000595:Amino Acid Sequence; D001173:Arthrobacter / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D020134:Catalytic Domain; D003001:Cloning, Molecular; D017124:Conserved Sequence; D040461:Gene Components; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000235:genetics*; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D004693:Glucan Endo-1,3-beta-D-Glucosidase