PROSITE documentation PDOC00133Urease domain signatures and profile
Urease (EC 3.5.1.5) is a nickel-binding enzyme that catalyzes the hydrolysis of urea to carbon dioxide and ammonia [1]. Historically, it was the first enzyme to be crystallized (in 1926). It is mainly found in plant seeds, microorganisms and invertebrates. In plants, urease is a hexamer of identical chains. In bacteria [2], it consists of either two or three different subunits (α, β and γ).
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 [3]. The urease domain forms an (α β)(8) barrel structure (see <PDB:2KAU>) with structural similarity to other metal-dependent hydrolases, such as adenosine and AMP deaminase (see <PDOC00419>) and phosphotriesterase (see <PDOC01026>).
As signatures for this enzyme, we selected a region that contains two histidines that bind one of the nickel ions and the region of the active site histidine. We also developed a profile that covers the whole urease domain.
Last update:April 2008 / Text revised; profile added.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Takishima K. Suga T. Mamiya G. |
| Title | The structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues. | |
| Source | Eur. J. Biochem. 175:151-165(1988). | |
| PubMed ID | 3402446 |
| 2 | Authors | Mobley H.L.T. Hausinger R.P. |
| Title | Microbial ureases: significance, regulation, and molecular characterization. | |
| Source | Microbiol. Rev. 53:85-108(1989). | |
| PubMed ID | 2651866 |
| 3 | Authors | Jabri E. Carr M.B. Hausinger R.P. Karplus P.A. |
| Title | The crystal structure of urease from Klebsiella aerogenes. | |
| Source | Science 268:998-1004(1995). | |
| PubMed ID | 7754395 |
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