{PDOC00133}
{PS01120; UREASE_1}
{PS00145; UREASE_2}
{PS51368; UREASE_3}
{BEGIN}
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* Urease domain signatures and profile *
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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
(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 [3]. The urease domain forms an (alpha
beta)(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.

-Consensus pattern: T-[AY]-[GA]-[GATR]-[LIVMF]-D-x-H-[LIVM]-H-x(3)-[PA]
                    [The 2 H's bind nickel]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [LIVM](2)-[CT]-H-[HNG]-L-x(3)-[LIVM]-x(2)-D-[LIVM]-x-F-
                    [AS]
                    [H is the active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: April 2008 / Text revised; profile added.

[ 1] Takishima K., Suga T., Mamiya G.
     "The structure of jack bean urease. The complete amino acid sequence,
     limited proteolysis and reactive cysteine residues."
     Eur. J. Biochem. 175:151-165(1988).
     PubMed=3402446
[ 2] Mobley H.L.T., Hausinger R.P.
     "Microbial ureases: significance, regulation, and molecular
     characterization."
     Microbiol. Rev. 53:85-108(1989).
     PubMed=2651866
[ 3] Jabri E., Carr M.B., Hausinger R.P., Karplus P.A.
     "The crystal structure of urease from Klebsiella aerogenes."
     Science 268:998-1004(1995).
     PubMed=7754395

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