Nonribosomal peptide synthetase that synthesizes cyclooctadepsipeptides (CODPs) PF 1022 that show powerful broad-spectrum anthelmintic activity with low toxicity in animals (PubMed:10751395, PubMed:19072825). Couples 4 N-methyl-L-leucines and a varying content of alpha-D-hydroxy acids (D-lactates or D-phenyllactates) in an alternative fashion (PubMed:10751395, PubMed:19072825). The enzyme is capable of synthesizing all known natural cyclooctadepsipeptides of the PF1022 type differing in the content of D-lactate and D-phenyllactate, using from 4 D-lactates (PF 1022F) to 4 D-phenyllactates (PF 1022B), respectively (PubMed:10751395). The formation of different PF-related compounds is mainly controlled by the molar ratio of the hydroxy acids (PubMed:10751395). N-methylation of the substrate L-leucine takes place after covalent binding prior to peptide bond formation (PubMed:10751395). 2 (R)-3-phenyllactate + 2 (R)-lactate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022A + 4 S-adenosyl-L-homocysteine 4 (R)-3-phenyllactate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022B + 4 S-adenosyl-L-homocysteine 3 (R)-3-phenyllactate + (R)-lactate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022C + 4 S-adenosyl-L-homocysteine (R)-3-phenyllactate + 3 (R)-lactate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022D + 4 S-adenosyl-L-homocysteine 4 (R)-lactate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-methionine = 8 AMP + 8 diphosphate + 8 H(+) + PF1022F + 4 S-adenosyl-L-homocysteine 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. 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, additional domains required for further modifications are also present (By similarity). PF 1022 synthetase has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (By similarity). The precursors D-hydroxycarboxylic acids and L-Leucine become activated at the A1 and the A2 domains (By similarity). N-methylation of the amino acid takes place at the MT-domain. The building blocks are transferred from one module to another by means of T-domains and are ultimately stored at the waiting position T2b (By similarity). Condensation of the building blocks and final cyclization and release from the enzyme is catalyzed by the C-domains (By similarity). The cyclooctadepsipeptides (CODP) of the PF 1022 type such as PF 1022A are described as powerful broad-spectrum anthelmintic neurotoxins that have low toxicity in animals (PubMed:7592027). PF 1022A has been shown to bind to the aminoterminus of a the latrophilin-like transmembrane receptor (HC-110R) from Haemonchus contortus (Rudolphi) and thereby induces an influx of external Ca(2+) into cells (PubMed:11344131). Both PF 1022A and PF 1022E can serve as valuable starting materials for the synthesis of semi-synthetic CODP derivatives with improved intrinsic anthelmintic potency and broad-spectrum activity (PubMed:16228266). Belongs to the NRP synthetase family.