Urease alpha-subunit, N-terminal domain (IPR011612)

Short name: Urease_alpha_N_dom

Overlapping homologous superfamilies

Domain relationships



Urease (urea amidohydrolase, EC: catalyses the hydrolysis of urea to form ammonia and carbamate. The subunit composition of urease from different sources varies [PMID: 7565414], but each holoenzyme consists of four structural domains [PMID: 7754395]: three structural domains and a nickel-binding catalytic domain common to amidohydrolases [PMID: 9144792]. 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 [PMID: 7754395].

Contributing signatures

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