Active Site

Urease active site (IPR017950)

Short name: Urease_AS

Description

Urease (urea amidohydrolase, EC:3.5.1.5) is a nickel-binding enzyme that catalyses the hydrolysis of urea to carbon dioxide and ammonia [PMID: 3402446]. 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 [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 and phosphotriesterase.

This entry represents a conserved region that contains the active site histidine.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0009039 urease activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns