Chanoclavine-I dehydrogenase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:22403186). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:22403186). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (PubMed:22403186). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:22403186). Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such as fumiclavine in Trichocomaceae (PubMed:22403186). However, the metabolites downstream of chanoclavine-I aldehyde in Arthrodermataceae have not been identified yet (PubMed:22403186). chanoclavine-I + NAD(+) = chanoclavine-I aldehyde + H(+) + NADH Alkaloid biosynthesis; ergot alkaloid biosynthesis. Homotetramer. Belongs to the short-chain dehydrogenases/reductases (SDR) family.