The low enoyl-acyl carrier protein reductase activity of FabI2 is responsible for the high unsaturated fatty acid composition in Sinorhizobium meliloti.

Background: Sinorhizobium meliloti is noted for its exceptional capacity to produce unsaturated fatty acids (UFAs). Earlier studies have indicated that S. meliloti primarily employs the FabA-FabB pathway for UFA synthesis, however, the mechanisms remain elusive.

A Nonessential Sfp-Type Phosphopantetheinyl Transferase Contributes Significantly to the Pathogenicity of .

4'-Phosphopantetheinyl transferases (PPTases) play important roles in the posttranslational modifications of bacterial carrier proteins, which are involved in various metabolic pathways. Here, we found that and encoded a functional AcpS-type and Sfp-type PPTase, respectively, in GMI1000, and both are capable of modifying AcpP1, AcpP2, AcpP3, and AcpP5 proteins. is located on the megaplasmid, which does not affect strain growth and fatty acid synthesis but significantly contributes to the virulence of and preferentially participates in secondary metabolism.

An atypical 3-ketoacyl ACP synthase III required for acyl homoserine lactone synthesis in pv. B728a.

The last step of the initiation phase of fatty acid biosynthesis in most bacteria is catalyzed by the 3-ketoacyl-acyl carrier protein (ACP) synthase III (FabH). pv. strain B728a encodes two FabH homologs, Psyr_3467 and Psyr_3830, which we designated PssFabH1 and PssFabH2, respectively.