<jats:title>Summary</jats:title><jats:p>The gene encoding the multifunctional enzyme enniatin synthetase from <jats:italic>Fusarium scirpi (esyn1)</jats:italic> was isolated and characterized by transcriptional mapping and expression studies in <jats:italic>Escherichia coli.</jats:italic> This is the first example of a gene encoding an <jats:italic>N</jats:italic>‐methyl peptide synthetase. The nucleotide sequence revealed an open reading frame of 9393 bp encoding a protein of 3131 amino acids (M<jats:sub>r</jats:sub> 346 900). Two domains designated EA and EB within the protein were identified which share similarity to each other and to microbial peptide synthetase domains. In contrast to the <jats:italic>N</jats:italic>‐terminal domain EA, the carboxyl terminal domain EB is interrupted by a 434‐amino‐acid portion which shows local similarity to a motif apparently conserved within adenine and cytosine RNA and DNA methyltransferases and therefore seems to harbour the <jats:italic>N</jats:italic>‐methyl‐transferase function of the multienzyme.