The selected horse ALDH7A1 A0A9L0RRL6 is521 aa versus canonical human 539 aa. Alignment identifies an internal deletion of human 65–82; the human structure has a beta strand at 65–70, so this should not be dismissed as a variable terminal peptide. Catalytic Glu296/Cys330 and the annotated nucleotide/substrate-binding positions are preserved; the N-terminal mitochondrial precursor segment is present. Broad ALDH chemistry and mitochondrial targeting remain reasonable inferences, but exact substrate kinetics and effects of the deletion are unresolved.
PMID:20207735(https://pubmed.ncbi.nlm.nih.gov/20207735/), DOI 10.1074/jbc.M109.077925, reports purified recombinant human enzyme metabolizing betaine aldehyde, lipid-peroxidation aldehydes and alpha-aminoadipic semialdehyde. PMID:16491085(https://pubmed.ncbi.nlm.nih.gov/16491085/) establishes pathogenic ALDH7A1 loss of alpha-AASA dehydrogenase activity. Neither inspected source provides a negative glyceraldehyde-3-phosphate assay. Broad ALDH substrate promiscuity cannot validate the ProtNLM substrate prediction, but it also makes a confident rejection based only on the canonical substrate unsafe.
The selected horse protein is not assumed to represent all human-like cytosolic isoforms. The horse GOA localization rows beyond mitochondria require isoform-specific evidence. A completed human Falcon report has been inspected; horse-specific Edison was not indicated by genome-only source references.
Conservation of the catalytic residues does not establish an intact active fold after the internal deletion. Broad aldehyde-dehydrogenase and oxidoreductase activity therefore remain UNDECIDED for this exact model as well as the substrate-specific terms; the ALDH7A1 family assignment itself remains well supported.