IPR011612
Urease alpha-subunit, N-terminal domain
InterPro entry
Short name | Urease_alpha_N_dom |
Overlapping homologous superfamilies |
Description
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
[3]: three structural domains and a nickel-binding catalytic domain common to amidohydrolases
[2]. 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
[3].
References
1.Molecular biology of microbial ureases. Mobley HL, Island MD, Hausinger RP. Microbiol. Rev. 59, 451-80, (1995). View articlePMID: 7565414
2.An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Holm L, Sander C. Proteins 28, 72-82, (1997). View articlePMID: 9144792
3.The crystal structure of urease from Klebsiella aerogenes. Jabri E, Carr MB, Hausinger RP, Karplus PA. Science 268, 998-1004, (1995). View articlePMID: 7754395
Cross References
ENZYME
Genome Properties
Contributing Member Database Entry
- Pfam:PF00449