InterPro domain: IPR002026

Urease (urea amidohydrolase, 3.5.1.5 ) is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. The enzyme consists of three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer forms multimers, mainly trimers. The subunit composition of urease from different sources varies [ 1 ], but each holoenzyme consists of four domains [ 2 ]: three structural domains and a nickel-binding catalytic domain common to amidohydrolases [ 3 ].

In Klebsiella aerogenes, urease exists as an alpha, beta and gamma subunit, with the alpha subunit possessing the catalytic domain. In Helicobacter pylori, the gamma and beta subunits are fused and called the alpha subunit, while the catalytic subunit is called the beta subunit. In Canavalia ensiformis, urease has a fused gamma-beta-alpha organisation.

This entry represents the urease gamma subunit. It also identifies gamma subunits fused with other urease subunits, as found in Helicobacter and other species.

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