Figure 3

Correctly mapped remote homolog: N-terminal domain of mannitol 2-dehydrogenase. a) Ribbon diagram of mannitol 2-dehydrogenase from Pseudomonas fluorescens (PDB: 1lj8 [19]). The N-terminal domain is shown in color. Regions in red are positions among the top 25% of most conserved positions in both the query (1lj8_A, N-terminal domain) and library representative (1i36_A, N-terminal domain). Regions in orange are positions among the top 25% of most conserved positions in either the query or the library representative domain, but not both. Positions in this domain that are not among the most highly conserved are blue (α-helices), yellow (β-strands), and green (coils). The C-terminal domain is shown in grey, and the bound nucleotide in shown in ball-and-stick format and is colored magenta. This and all other structure figures were prepared using MOLSCRIPT[48]. b) Ribbon diagram of conserved hypothetical protein MTH1747 from Methanobacterium thermoautotrophicum (PDB: 1i36). The N-terminal domain, shown in color, is a representative of the NAD(P)-binding Rossmann-fold superfamily. The colors have equivalent meaning to those in figure 3a. The C-terminal domain is shown in grey, and nucleotide in shown in ball-and-stick format and is colored magenta. Dashed lines indicate breaks in the chain. c) Pairwise alignment of the query (1lj8_A) and library representative (1i36_A) from DaliLite results. Residues in red bold text are among the top 25% of most conserved positions in at least one of the domains. Residues indicated with an asterisk are among the top 25% of most conserved positions in both the query and library domains. Secondary structure is indicated above the alignment, with E signifying β-strand residues and H signifying α-helix residues. In this and other alignments, the numbers flanking the alignment indicate the residue number in the sequence of the first (or last) aligned residue on that line. Numbers in brackets specify the number of residues in an insert that are not shown. In all alignments produced based on DaliLite results, capital letters are aligned residues and lower-case letters are unaligned residues.