Figure 3

Sequence alignment between a representative sequence of each family of type I domains and the most similar structural template. Sequences are labeled by their databank code. Aminotran_3 (a): [UniProt: Q2T5Z2] indicates polyketide synthase from Burkholderia thailandensis; [PDB:2E7U] is the glutamate-1-semialdehyde 2,1-aminomutase from Thermus thermophilus HB8. Aminotran_1_2 (b): [UniProt:B1XHP8] indicates AMP-binding enzyme from Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6); [PDB:3A2B] denotes serine palmitoyltransferase from Sphingobacterium multivorum. Beta_elim_lyase (c): [UniProt:F8TUA6] corresponds to keto-hydroxyglutarate-aldolase/polyketide synthase from Lysobacter sp.; [PDB:1C7G] labels the tyrosine phenol-lyase from Erwinia herbicola. Pyridoxal_deC (d): [UniProt:B6IZA3] is the non-ribosomal peptide synthetase module from Coxiella burnetii; [PDB:2JIS] stands for the cysteine sulfinic acid decarboxylase from Homo sapiens. Secondary structures are charted below the template sequence. Helices (alpha and 3₁₀ helices are designated by α or η respectively) are displayed as squiggles and beta strands (β) are rendered as arrows. Beta turns are denoted as “TT” and strict α turns as “TTT”. Dots indicate gaps. Identically conserved residues are displayed on a red background; red letters indicate conservative substitutions. Triangles mark residues known to be functionally important in the template enzyme. Black circles tag important residues from the other subunit. Stars label the Asp and the Lys residue involved in interaction with pyridine nitrogen and in Schiff-base forming, respectively. The black square in the panel (c) indicates the Arg381 of the template missing in the homologous PLP domain.