Covalently binds beta-alanine in an ATP-dependent manner to form a thioester bond with its phosphopantetheine group and transfers it to an as yet unknown acceptor via an amide bond. May be required for a post-translational protein modification or for post-transcriptional modification of an RNA. Has been shown to be up-regulated by a lysine-rich diet (PubMed:12712191). However, levels of expression have also been shown not to be significantly changed even when diets differ markedly in PQQ and lysine content (PubMed:17029795). Belongs to the ATP-dependent AMP-binding enzyme family. Was suggested to bind pyrroloquinoline quinone (PQQ) based on prediction tools and indirect results (PubMed:12712191). However, this has not been confirmed in other publications (PubMed:15689995, PubMed:15689994). In invertebrates, the aminoadipate-semialdehyde dehydrogenase reaction is a key step of the L-lysine biosynthesis pathway which is not fully conserved in vertebrates and it has been suggested that this protein participates in the reverse reaction i.e. in lysine catabolism (PubMed:12712191). However, this is unlikely to be the case as no dehydrogenase activity has been detected and the authentic mammalian 2-aminoadipate semialdehyde dehydrogenase has been identified as ALDH7A1 (PubMed:24467666).