<jats:p>The biosynthetic gene cluster of the myxochelin‐type iron chelator was cloned from <jats:italic>Stigmatella aurantiaca</jats:italic> Sg a15 and characterized. This catecholate siderophore was only known from two other myxobacteria. The biosynthetic genes of 2,3‐dihydroxybenzoic acid are located in the cluster (<jats:italic>mxcC</jats:italic>–<jats:italic>mxcF</jats:italic>). Two molecules of 2,3‐dihydroxybenzoic acid are activated and condensed with lysine in a unique way by a protein homologous to nonribosomal peptide synthetases (MxcG). Inactivation of <jats:italic>mxcG,</jats:italic> which encodes an adenylation domain for lysine, results in a myxochelin negative mutant unable to grow under iron‐limiting conditions. Growth could be restored by adding Fe<jats:sup>3+</jats:sup>, myxochelin A or B to the medium. Inactivation of <jats:italic>mxcD</jats:italic> leads to the same phenotype. A new type of reductive release from nonribosomal peptide synthetases of the 2,3‐dihydroxybenzoic acid bis‐amide of lysine from MxcG, catalyzed by a protein domain with homology to NAD(P) binding sites, is discussed. The product of a gene, encoding a protein similar to glutamate‐1‐semialdehyde 2,1‐aminomutases (<jats:italic>mxcL</jats:italic>), is assumed to transaminate the aldehyde that is proposed as an intermediate. Further genes encoding proteins homologous to typical iron utilization and iron uptake polypeptides are reported.