Fig. 1
From: Cloning, expression and characterization of a novel esterase from Bacillus pumilus
Alignment of the amino acid sequence of B. pumilus ARA CE1 with the amino acid sequences of other bacterial esterases. Alignment was maximized by introducing gaps, which are indicated by dashes. Identical (*), highly similar (:) and similar (.) amino acids are indicated. The consensus active site sequence of serine esterases and the putative catalytic triad components (93Ser, 192Asp and 222His) are indicated in bold. CE1-Bp esterase from B. pumilus ARA (this study), Est-Bs esterase from B. subtilis 168 (CAB15367), Est-Gt esterase from G. thermoleovorans (AAG53982), Est-Gs esterase from G. stearothermophilus IFO 12550 (Q06174), Est-Bh esterase from B. halodurans C-125 (NP_244421)