Summary: Urease, gamma subunit
Urease, gamma subunit Provide feedback
Urease is a nickel-binding enzyme that catalyses the hydrolysis of urea to carbon dioxide and ammonia.
Internal database links
|SCOOP:||Apyrase Rib Svf1 DUF5073|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002026
Urease (urea amidohydrolase, EC) catalyses the hydrolysis of urea to form ammonia and carbamate. The subunit composition of urease from different sources varies [PUBMED:7565414], but each holoenzyme consists of four domains [PUBMED:7754395]: three structural domains and a nickel-binding catalytic domain common to amidohydrolases [PUBMED:9144792].
In Klebsiella aerogenes, urease exists as an alpha, beta and gamma subunit, with the alpha subunit possessing the catalytic domain. In Helicobacter pylori, the gamma and beta subunits are fused and called the alpha subunit, while the catalytic subunit is called the beta subunit. In Canavalia ensiformis, urease has a fused gamma-beta-alpha organisation.
This entry represents the urease gamma subunit. It also identifies gamma subunits fused with other urease subunits, as found in Helicobacter and other species.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||nickel cation binding (GO:0016151)|
|Biological process||urea catabolic process (GO:0043419)|
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Curation and family details
|Number in seed:||179|
|Number in full:||10905|
|Average length of the domain:||98.40 aa|
|Average identity of full alignment:||69 %|
|Average coverage of the sequence by the domain:||75.51 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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There are 5 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Urease_gamma domain has been found. There are 69 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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