Urease, alpha subunit (IPR005848)

Short name: Urease_asu

Overlapping homologous superfamilies

Family relationships



Urease (urea amidohydrolase, EC: is a nickel-binding enzyme that catalyses the hydrolysis of urea to form ammonia and carbamate [PMID: 3402446]. It is mainly found in plant seeds, microorganisms and invertebrates. In plants, urease is a hexamer of identical chains, but the subunit composition of urease from different sources varies [PMID: 7565414], in bacteria [PMID: 2651866] it consists of either two or three different subunits (alpha, beta and gamma).

Urease binds two nickel ions per subunit; four histidine, an aspartate and a carbamated-lysine serve as ligands to these metals; an additional histidine is involved in the catalytic mechanism [PMID: 7754395]. The urease domain forms an (alpha beta)(8) barrel structure with structural similarity to other metal-dependent hydrolases, such as adenosine and AMP deaminase and phosphotriesterase. Urease is unique among nickel metalloenzymes in that it catalyses a hydrolysis rather than a redox reaction.

The orthologous protein is known as the alpha subunit (ureC) in most other bacteria.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). This entry describes the urease alpha subunit UreC (designated beta or B chain, UreB in Helicobacter species).

GO terms

Biological Process

GO:0006807 nitrogen compound metabolic process

Molecular Function

GO:0016151 nickel cation binding
GO:0009039 urease activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.