Identification of two vicinal operons for the degradation of 2-aminobenzenesulfonate encoded on plasmid pSAH in Alcaligenes sp. strain O-1

SummaryAlcaligenes sp. strain O-1 inducibly deaminates 2-aminobenzenesulfonate (ABS) via dioxygenation to 3-sulfocatechol, which is desulfonated during meta ring-cleavage to yield 2-hydroxymuconate. This intermediate is transformed through the oxalocrotonate-branch of the sulfocatechol meta-pathway (Scm). The complete pathway is encoded on the 180-kb plasmid pSAH, 20 kb of which was sequenced. Twenty open reading frames (ORFs) were detected. Two clusters (abs and scm) with degradative genes were surrounded by several transposon-related ORFs. The six genes of the abs cluster were shown to be co-transcribed, and contained the genes for two characterised subunits of the oxygenase component of the ABS-dioxygenase system, and genes putatively encoding ABS-transport functions with similarities to (a) an ABC-type transporter system and (b) a putative major facilitator superfamily transporter. No gene encoding the reductase for the oxygenase system was present in the abs gene cluster, but a candidate gene was found in the scm cluster. The seven-gene scm cluster was also transcribed as single polycistronic message. Functions could be attributed to the gene products, but one enzyme, which was shown to be present, 2-hydroxymuconate isomerase, was not encoded in the scm cluster. No transcriptional regulator was found. This genetic information on the degradation of ABS in strain O-1 provides another example of both split operons and dispersed pathway genes.