Literature summary for 3.5.2.1 extracted from

Seffernick, J.L.; Wackett, L.P.
Ancient evolution and recent evolution converge for the biodegradation of cyanuric acid and related triazines (2016), Appl. Environ. Microbiol., 82, 1638-1645 .

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
barbiturate + H2O	Actinobacteria	-	3-oxo-3-ureidopropanoate	-	?

Organism

Organism	UniProt	Comment	Textmining
Actinobacteria	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
barbiturate + H2O	-	Actinobacteria	3-oxo-3-ureidopropanoate	-	?

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to a protein family that consists of only cyanuric acid hydrolase (CAH) and barbiturase. CAH and barbiturase enzymes act on structurally analogous 6-membered ring substrates, yet each enzyme is specific and does not react with the other's substrate. While most organisms utilize a reductive pyrimidine degradation pathway, some actinobacteria use barbiturase in an oxidative catabolic pathway. Unlike barbiturase, cyanuric acid hydrolases are more broadly distributed throughout bacteria and fungi. The CAH/barbiturase family includes 169 different sequences of Actinobacteria, phylogenetic analysis and tree, overview	Actinobacteria
metabolism	barbiturase participating in pyrimidine catabolism by some actinobacterial species. Barbiturase catalyzes the second step in the oxidative pyrimidine degradation pathway	Actinobacteria

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Release 2023.1 (January 2023)