Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. Overexpression of wild-type or mutant proteins confers resistance to pyrazinoic acid (POA), the active form of the anti-tuberculosis prodrug pyrazinamide (PZA), when grown on agar plates. H(+) + L-aspartate = beta-alanine + CO2 Binds 1 pyruvoyl group covalently per subunit. Partially inhibited by POA but not by PZA or nicotinamide, probably also inhibited by calcium pantothenate. Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. Heterooctamer of four alpha and four beta subunits. Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus. 30 POA or PZA-resistant mutants were identified in this gene by selection at pH 5.7 - 6.8. The antituberculosis activity of POA is antagonized by beta-alanine and pantothenate, the immediate and final reaction products of this enzyme (PubMed:26038753). Experiments in strain H37Rv suggest however that the PZA target may not be PanD (By similarity). Belongs to the PanD family.