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Fig. 1 | Biotechnology for Biofuels

Fig. 1

From: A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity

Fig. 1

Amino acid sequence alignment of Ac-Abf51A from Alicyclobacillus sp. A4 with CelA4 from Alicyclobacillus sp. A4 (ADI82825.1) and other GH51 Abfs from Bifidobacterium longum B667 (PDB: 2Y2 W), Geobacillus stearothermophilus T6 (PDB: 1PZ3), Clostridium thermocellum ATCC 27405 (PDB: 2C7F), Thermobacillus xylanilyticus D3 (PDB: 2VRK), Thermotoga maritima MSB8 (PDB: 3UG3), and Thermotoga petrophila RKU-1 (PDB: 3S2C), using the ClustalW program. Identical and similar amino acids are indicated by black and gray shades, respectively. The catalytic glutamate residues are indicated by asterisk, and the conserved residues are indicated by hash

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