InterPro domain: IPR011612

Urease (urea amidohydrolase, 3.5.1.5 ) catalyses the hydrolysis of urea to form ammonia and carbamate. The subunit composition of urease from different sources varies [ 1 ], but each holoenzyme consists of four structural domains [ 2 ]: three structural domains and a nickel-binding catalytic domain common to amidohydrolases [ 3 ]. Urease is unique among nickel metalloenzymes in that it catalyses a hydrolysis rather than a redox reaction. In Helicobacter pylori, the gamma and beta domains are fused and called the alpha subunit ( IPR008223 ). The catalytic subunit (called beta or B) has the same organisation as the Klebsiella alpha subunit. Jack bean (Canavalia ensiformis) urease has a fused gamma-beta-alpha organisation ( IPR008221 ).

The N-terminal domain is a composite domain and plays a major trimer stabilising role by contacting the catalytic domain of the symmetry related alpha-subunit [ 4 ].

1. Molecular biology of microbial ureases. Microbiol. Rev. 59, 451-80
2. The crystal structure of urease from Klebsiella aerogenes. Science 268, 998-1004
3. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins 28, 72-82