The myxochelin iron transport regulon of the myxobacterium Stigmatella aurantiaca Sg a15.

摘要: The biosynthetic gene cluster of the myxochelin-type iron chelator was cloned from Stigmatella aurantiaca Sg a15 and characterized. This catecholate siderophore only known two other myxobacteria. genes 2,3-dihydroxybenzoic acid are located in (mxcC–mxcF). Two molecules activated condensed with lysine a unique way by protein homologous to nonribosomal peptide synthetases (MxcG). Inactivation mxcG, which encodes an adenylation domain for lysine, results myxochelin negative mutant unable grow under iron-limiting conditions. Growth could be restored adding Fe3+, myxochelin A or B medium. mxcD leads same phenotype. A new type reductive release bis-amide MxcG, catalyzed homology NAD(P) binding sites, is discussed. product gene, encoding similar glutamate-1-semialdehyde 2,1-aminomutases (mxcL), assumed transaminate aldehyde that proposed as intermediate. Further proteins typical utilization uptake polypeptides reported.