Abstract
The analysis of the 6.8-Mbp draft genome sequence of the phenylmalonate-assimilating bacterium Bordetella bronchiseptica KU1201 identified 6,358 protein-coding sequences. This will give us an insight into the catabolic variability of this strain for aromatic compounds, along with the roles of arylmalonate decarboxylases in nature.
Highlights
The analysis of the 6.8-Mbp draft genome sequence of the phenylmalonate-assimilating bacterium Bordetella bronchiseptica KU1201 identified 6,358 protein-coding sequences
The whole-genome shotgun sequence of Bordetella bronchiseptica KU1201 was obtained by an Illumina GAIIx run
A total number of 55 RNA genes were detected by RAST analysis
Summary
The analysis of the 6.8-Mbp draft genome sequence of the phenylmalonate-assimilating bacterium Bordetella bronchiseptica KU1201 identified 6,358 protein-coding sequences. Bordetella bronchiseptica KU1201 (formerly, Alcaligenes bronchisepticus KU1201) was isolated from soil sample through enrichment culture on phenylmalonate as a sole carbon source [1]. We determined that this strain harbors a novel unique enzyme that shows decarboxylation activities to arylmalonates, materials unfound in the natural environment. The enzyme AMDase catalyzes an asymmetric decarboxylation of prochiral arylmalonates to produce optically pure (R)-arylcarboxylates without any cofactor [2].
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