Homologous Superfamily

Urease, beta subunit superfamily (IPR036461)

Short name: Urease_betasu_sf

Overlapping entries


Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, archaea, fungi and plants. Their primary role is to allow the use of external and internally-generated urea as a nitrogen source. The enzyme consists of three subunits, alpha, beta and gamma, which can exist as separate proteins or can be fused on a single protein chain. The alpha-beta-gamma heterotrimer forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel centre complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers [PMID: 11996109, PMID: 10865198, PMID: 16173497, PMID: 11373617, PMID: 7565414].

This entry represents the urease beta subunit superfamily. In Helicobacter pylori, the gamma and beta subunits are fused and known (confusingly) as the alpha subunit.

The urease beta subunit structure is composed of double-stranded ribbon sharply bent in two places where the ribbon ends form incomplete barrel and has a jelly-roll.

Contributing signatures

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