Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes the O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide (PubMed:27390873). This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL (PubMed:27390873). The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification (PubMed:18272357). Phomamide is converted into phomalizarine via oxidation, probably by sirT (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357). Mycotoxin biosynthesis. Expressed during canola infection (PubMed:20507539). Expression is co-regulated with the other genes from the sirodesmin cluster and corresponds with sirodesmin production (PubMed:15387811). 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) that releases the newly synthesized peptide from the enzyme (By similarity). Occasionally, epimerase (E) domains (responsible for L- to D-amino acid conversion) are present within the NRP synthetase (By similarity). NRPS10 has the foolowing architecture: A-T-C-A-T-C (PubMed:15387811). Impairs the production of sirodesmin PL (PubMed:15387811, PubMed:20507539). Decreases the number of lesions and the efficiency in colonizing stems during infection of canola (PubMed:20507539). Belongs to the NRP synthetase family.