Figure 7.

Multiple sequence alignments of the amino acid sequences of Arabidopsis β-UP with β-UPs from rat and C. elegans, and with two amidohydrolases and a nitrilase. Arabidopsis β-UP (b-UP At) was aligned with the rat and C. elegans β-UPs (b-UP Rat and b-UP Cel; GenBank accession nos. Q03248 and AAC46683, respectively) using the MegAlign program of Lasergene (DNAstar, Madison, WI). The alignment of the N-carbamyl-d-amino acid amidohydrolase from Agrobacterium sp. (DAAH Atu; GenBank accession no. JW0082), Pseudomonas aeruginosa aliphatic amidase (Amid Pae; GenBank accession no. P11436), and Arabidopsis nitrilase I (Nitr Ath; GenBank accession no. CAA45041) sequences was based on that in Nakai et al. (2000). Residues conserved with Arabidopsis β-UP are shaded gray and residues that are completely conserved in all six sequences are shaded black. The Cys, Glu, and Lys residues that comprise the catalytic triad (Nakai et al., 2000) are marked by +. The underlined residues at the beginning of the Arabidopsis β-UP are derived from the genomic sequence (GenBank accession no. BAB09868). The M above residue 16 denotes the N terminus of the truncated polypeptide that was functionally overexpressed in E. coli.