Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of Asp-melanin, a pigment that confers resistance against UV light and hampers phagocytosis by soil amoeba (PubMed:23841722, PubMed:27133313, PubMed:29270299). The nonribosomal peptide synthase melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (PubMed:27133313, PubMed:29270299). The tyrosinase tyrP then performs hydroxylations of both aromatic moieties of aspulvinone E (PubMed:27133313). The product of tyrP is highly unstable, and, due to the high reactivity of methides and ortho-diquinones, the polymeric Asp-melanin forms spontaneously (PubMed:27133313). Expression is induced during conidiation. MelA has a A-T-TE domain architecture. The adenylation (A) domain recognizes and activates the aryl acid substrates, and loads them onto the thiolation (T) domain. The thioesterase (TE) domain shares the missing condensation (C) domain function, and is responsible for condensation and final product release. Results in white conidia. Belongs to the ATP-dependent AMP-binding enzyme family.