Carboxylic acid reductase that shows a broad range of substrate specificity towards aromatic acids, especially to phenyl carboxylic and phenyl acrylic acids, to convert them into their respective aldehydes (PubMed:4389863, PubMed:11946054, PubMed:27917101, PubMed:29515539). Also able to use aliphatic acids as substrates (PubMed:29515539). AMP + an aromatic aldehyde + diphosphate + NADP(+) = an aromatic carboxylate + ATP + H(+) + NADPH a carboxylate + ATP + H(+) + NADPH = AMP + an aldehyde + diphosphate + NADP(+) ATP + benzoate + H(+) + NADPH = AMP + benzaldehyde + diphosphate + NADP(+) (E)-cinnamate + ATP + H(+) + NADPH = (E)-cinnamaldehyde + AMP + diphosphate + NADP(+) ATP + H(+) + NADPH + piperonylate = AMP + diphosphate + NADP(+) + piperonal ATP + H(+) + NADPH + salicylate = AMP + diphosphate + NADP(+) + salicylaldehyde 3-hydroxybenzoate + ATP + H(+) + NADPH = 3-hydroxybenzaldehyde + AMP + diphosphate + NADP(+) 2-methoxybenzoate + ATP + H(+) + NADPH = 2-methoxybenzaldehyde + AMP + diphosphate + NADP(+) 3-methoxybenzoate + ATP + H(+) + NADPH = 3-methoxybenzaldehyde + AMP + diphosphate + NADP(+) 4-hydroxybenzoate + ATP + H(+) + NADPH = 4-hydroxybenzaldehyde + AMP + diphosphate + NADP(+) 4-methoxybenzoate + ATP + H(+) + NADPH = 4-methoxybenzaldehyde + AMP + diphosphate + NADP(+) 3-phenylpropanoate + ATP + H(+) + NADPH = 3-phenylpropanal + AMP + diphosphate + NADP(+) ATP + H(+) + NADPH + picolinate = AMP + diphosphate + NADP(+) + picolinal ATP + H(+) + NADPH + propanoate = AMP + diphosphate + NADP(+) + propanal ATP + butanoate + H(+) + NADPH = AMP + butanal + diphosphate + NADP(+) ATP + H(+) + NADPH + pentanoate = AMP + diphosphate + NADP(+) + pentanal ATP + H(+) + hexanoate + NADPH = AMP + diphosphate + hexanal + NADP(+) ATP + H(+) + heptanoate + NADPH = AMP + diphosphate + heptanal + NADP(+) ATP + H(+) + NADPH + octanoate = AMP + diphosphate + NADP(+) + octanal ATP + H(+) + NADPH + nonanoate = AMP + diphosphate + NADP(+) + nonanal Optimum pH is 8.0. Optimum temperature is 35 degrees Celsius. The NRPS-like carboxylic acid reductase (CAR) has an unusual domain architecture (A-T-R), with the adenylation domain A activating and thioesterifying the carboxylic acid which is then channeled through the phosphopantetheine arm of the T domain, the thioester reductase domain R reducing the carboxylic acid to the corresponding aldehyde. Belongs to the adenylate-forming reductase family.