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Cyanuric acid is a common environmental contaminant and a metabolic intermediate in the catabolism of  s- triazine compounds, including atrazine and other herbicides. Cyanuric acid is catabolized  via  a number of bacterial pathways, including one first identified in  Pseudomonas  sp. strain ADP, which is encoded by a single, five-gene operon ( atzDGEHF ) found on a self-transmissible plasmid. The discovery of two of the five genes ( atzG  and  atzH ) was reported in 2018 and although the function of  atzG  was determined, the role of  atzH  was unclear. Here, we present the first  in vitro  reconstruction of the complete, five-protein cyanuric acid catabolism pathway, which indicates that AtzH may be an amidase responsible for converting 1,3-dicarboxyurea (the AtzE product) to allophanate (the AtzF substrate). We have solved the AtzH structure (a DUF3225 protein from the NTF2 superfamily) and used it to predict the substrate-binding pocket. Site-directed mutagenesis experiments suggest that two residues (Tyr22 and Arg46) are needed for catalysis. We also show that  atzH  homologs are commonly found in Proteobacteria associated with homologs of the  atzG  and  atzE  genes. The genetic context of these  atzG-atzE-atzH  clusters imply that they have a role in the catabolism of nitrogenous compounds. Moreover, their presence in many genomes in the absence of homologs of  atzD  and  atzF  suggests that the  atzG-atzE-atzH  cluster may pre-date the evolution of the cyanuric acid catabolism operon.

A novel decarboxylating amidohydrolase involved in avoiding metabolic dead ends during cyanuric acid catabolism in Pseudomonas sp. strain ADP