Figure 1

Amino acid sequence alignment of ManB from B. licheniformis and other mannan endo-1,4-β-mannosidases belonging to glycosyl hydrolase family 26 (GH26). α-Helices are displayed as squiggles; β-strands are rendered as arrows. The eight β-strands forming the core of the TIM-barrel are referred as S1 to S8, whereas the eight α-helices connecting these β-strands are referred to as H1 to H8. A white character in a box indicates strict identity, while a black character in a frame indicates similarity across a group. The catalytic glutamate residues are located at position 167 and 266 of β-mannanase from B. subtilis Z-2 [16]. Multiple sequence alignment was done by CLUSTAL W [36] followed by ESPript [37] to display the secondary structure of the β-mannanase from B. subtilis Z-2, 2QHA. The similarity of different enzymes is shown as % identity, based on the sequence of B. licheniformis DSM13 (100%); B. subtilis Z-2 (81.90%); B. subtilis 168 (81.90%); P. cellulosa (19.90%); C. acetobutylicum (15.27%); A. tumefaciens (13.82%) and M. loti (11.08%). Key: B. subtilis Z-2 (Bacillus subtilis Z-2, PDB code; 2QHA); B. licheniformis DSM 13 (Bacillus licheniformis DSM 13, NCBI accession number NC006322); B. subtilis 168 (Bacillus subtilis subsp. subtilis str. 168, NCBI accession number NC000964); P. cellulosa (Pseudomonas cellulose, NC010995); C. acetobutylicum (Clostridium acetobutylicum str. ATCC 824, NC003030); A. tumefaciens (Agrobacterium tumefaciens str. C58, NCBI accession number NC003063) and M. loti (Mesorhizobium loti MAFF303099, NCBI accession number, NC002678).