Urease alpha subunit, C-terminal (IPR017951)
Short name: Urease_asu_c
Overlapping homologous superfamilies
- Metal-dependent hydrolase (IPR032466)
Urease (urea amidohydrolase, EC:126.96.36.199) 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 (see PDOC00419) and phosphotriesterase see PDOC01026). 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).
This entry describes the C-terminal domain of urease alpha subunit UreC (designated beta or UreB in Helicobacter species).
Urease (EC:188.8.131.52) belongs to MEROPS peptidase family M38 (clan MJ).
- PS51368 (UREASE_3)