Additional file 18.

Ni-CODH catalytic subunit alignment. Genes in this alignment are the Ni-CODH catalytic subunits from R. rubrum (CooS, PDB:1JQK), M. thermoacetica (AcsA, PDB:1MJG) and Fer2 (fer2_31_0047). fer2_31_0047’s secondary structure was predicted by YASPIN [118]. β-strands are shown in green and α-helices are highlighted in cyan. Residues belonging to the D-cluster are boxed in yellow (Cys41 and Cys49). Ligands of the B-cluster are boxed in black (Cys50, Cys53, Cys58 and Cys72). Catalytic residues binding the Ni-Fe-S cluster from C-cluster are boxed in purple (His265, Cys300, Cys338, Cys451, Cys481, and Cys531) and catalyze the oxidation of carbon. His95 and Lys568 (boxed in dark red) are non-coordinating residues conserved in Ni-CODHs and have been suggested to be involved in facilitating the reaction [119]. Residue numbering is from the R. rubrum Ni-CODH.

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Yelton et al. BMC Genomics 2013 14:485   doi:10.1186/1471-2164-14-485