D-lysergyl-peptide-synthetase subunit 1; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid ergovaline, the predominant ergopeptine product in E.festucae var. lolii (PubMed:17308187). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). 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 (By similarity). 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 (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). The presence of easA is not required to complete this reaction (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (By similarity). Paspalic acid is then further converted to D-lysergic acid (By similarity). Ergovaline is assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a trimodular (lpsA) nonribosomal peptide synthetase subunit (PubMed:17308187, PubMed:11592979). Alkaloid biosynthesis; ergot alkaloid biosynthesis. NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module (By similarity). Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product (By similarity). Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) or reductase domain (R) that releases the newly synthesized peptide from the enzyme (By similarity). LpsA1 has a domain arrangement (A-T-C-A-T-C-A-T-Cyc) with 3 A and 3 peptidyl carrier (PCP/T) domains, 2 C-domains, and a terminal domain called the Cyc domain (By similarity). The Cyc domain has limited similarity to both C and Cy domains of NRPS but is most different in the so-called C3 and Cy3 motif of the latter domains, suggesting a special mechanism in acyl diketopiperazine formation, which is the final step of D-lysergyl peptide lactam synthesis (By similarity). LpsA misses an N-terminal C domain in the first module, leading to the conclusion that this C domain is located on the other subunit (lpsB) containing the D-lysergic acid module (By similarity). Abolishes the production of ergovaline (PubMed:11592979). Belongs to the NRP synthetase family.