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. Author manuscript; available in PMC: 2012 Jul 1.
Published in final edited form as: Arch Biochem Biophys. 2011 Apr 13;511(1-2):48–55. doi: 10.1016/j.abb.2011.04.004

Figure 2.

Figure 2

Sequence alignment of diverse eukaryotic and prokaryotic HMG-CoA lyase proteins. Residues flanking cysteine residues in the animal proteins are depicted. Alignment was generated using ClustalW. Residue numbering corresponds to human HMGCL (uncleaved mitochondrial isoform). Sequences from the following organisms are included: Homo sapiens, Gallus gallus, Drosophila melanogaster, Pseudomonas mevalonii, Rhodospirillum rubrum, and Bacillus subtilis. Amino acid sequences were obtained from the UniProt database using the following accession numbers: P35914, P35915, Q9VM58, P13703, Q2RT05, and O34873 respectively. A more extensive alignment would indicate infrequent substitutions for C174 (e.g. aspartate in Streptomyces coelicolor HMGCL).