Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of the aspergillicins A and F, 2 cryptic cyclic hexa-depsipeptides (PubMed:31117395). The hexamodular NRPS agiA catalyzes the condensation of the six amino acid residues including N-Me-L-O-Me-tyrosine, L-proline 1, L-proline 2, D-isoleucine, O-acetyl-threonine, and L-isoleucine (PubMed:31117395). The starting condensation domain (C1) of agiA probably loads acetyl-CoA which is condensed on the N-terminus of threonine by the first module to yield O-acetyl-threonine (PubMed:26273902). The second module then loads L-isoleucine. The epimerase (E) domain on module 2 is probably involved in the formation of the D-isoleucine moiety (PubMed:26273902). Modules 3 and 4 further load 2 successive L-prolines (PubMed:26273902). Module 5 is then involved in the condensation of O-Me-L-tyrosine produced by the O-methyltransferase agiB and the N-methyl transferase (NMeT) domain on module 5 probably catalyzes the N-methylation to yield the N-Me-L-O-Me-tyrosine moiety (PubMed:26273902). The A domain of module 5 loads preferentially O-Me-L-tyrosine, but it can also accept L-phenylalanine, which leads to the production of aspergillicin G (PubMed:26273902). Module 6 then loads the last residue, L-isoleucine (PubMed:26273902). The C-terminal thiolesterase (TE) domain probably cyclizes the peptide using the hydroxy group from threonine to form the cyclic depsipeptide (PubMed:26273902). 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. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, additional domains such as epimerase (E) or methyltransferase (MeT) required for further modifications are also present. Aspergillicins synthetase has the C1-A1-T1-C2-A2-T2-E-C3-A3-T3-C4-A4-T4-C5-A5-T5-NMeT-C6-A6-T6-TE domain organization. The epimerase (E) domain on module 2 is probably involved in the formation of the D-isoleucine moiety and the N-methyl transferase (NMeT) domain on module 5 catalyzes the N-methylation of phenylalanine/tyrosine. The C-terminal thiolesterase (TE) domain probably cyclizes the peptide when releasing the final product from the enzyme. Impairs the production of aspergillicins A and F. Aspergillicins show innate immunity-modulating activity. Innate immunity is a good pharmaceutical target for the development of immune regulators to suppress unwanted immune responses, such as septic shock, inflammatory diseases, and autoimmune diseases. The innate immune system also provides targets for the development of agents that stimulate protective immune responses toward some diseases, such as infections with pathogenic organisms and cancer. Belongs to the NRP synthetase family.