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Urea carboxylase (UC) is conserved in many bacteria, algae, and fungi and catalyzes the conversion of urea to allophanate, an essential step in the utilization of urea as a nitrogen source in these organisms.UC belongs to the biotin-dependent carboxylase superfamily and shares the biotin carboxylase (BC) and biotin carboxyl carrier protein (BCCP) domains with these other enzymes, but its carboxyltransferase (CT) domain is distinct.
In most living organisms, urea is generated in the degradation of nitrogen-containing molecules.
The BC and BCCP domains of biotin-dependent carboxylases are highly homologous, but their CT domains are distinct.
Recently, high resolution crystal structures of the PC (18, 19) and PCC (20) holoenzymes have been reported, which greatly advanced the understanding of biotin-dependent carboxylases.
However, the molecular mechanism for how UC recognizes the urea substrate and catalyzes its carboxylation is currently not known.
We report here the crystal structure at 2.6 Å resolution of the urea amidolyase UC domain (Kl UC).
It is an essential component of a pyrimidine nucleic acid precursor degradation pathway (12).