PROSITE documentation PDOC00133 [for PROSITE entry PS00145]

Urease domain signatures and profile





Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

UREASE_2, PS00145; Urease active site  (PATTERN)

UREASE_3, PS51368; Urease domain profile  (MATRIX)

UREASE_1, PS01120; Urease nickel ligands signature  (PATTERN)


References

1AuthorsTakishima K., Suga T., Mamiya G.
TitleThe structure of jack bean urease. The complete amino acid sequence, limited proteolysis and reactive cysteine residues.
SourceEur. J. Biochem. 175:151-165(1988).
PubMed ID3402446

2AuthorsMobley H.L.T., Hausinger R.P.
TitleMicrobial ureases: significance, regulation, and molecular characterization.
SourceMicrobiol. Rev. 53:85-108(1989).
PubMed ID2651866

3AuthorsJabri E., Carr M.B., Hausinger R.P., Karplus P.A.
TitleThe crystal structure of urease from Klebsiella aerogenes.
SourceScience 268:998-1004(1995).
PubMed ID7754395



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