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PRU00700


General rule information [?]

Accession PRU00700
Dates 27-MAR-2008 (Created)
19-NOV-2022 (Last updated, Version 21)
Data class Domain
Predictors PROSITE; PS51368; UREASE_3
Name Urease domain
Function Urease (EC 3.5.1.5) is a nickel-binding enzyme that catalyzes the hydrolysis of urea to carbon dioxide and ammonia. The urease domain forms an (alpha beta)(8) barrel structure that binds two nickel ions and with a histidine that is catalytically involved.

Propagated annotation [?]


Description [?]

case <FT:2> and <FTGroup:1> and <FTGroup:2> and not <OC:Bacteria> and not <OC:Archaea>
+ AltName: Full=Urease; EC 3.5.1.5; AltName: Full=Urea amidohydrolase;
end case


Comments [?]

case <FT:2> and <FTGroup:1> and <FTGroup:2>
Catalytic activity RHEA:20557: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
EC 3.5.1.5
end case

case <FTGroup:1> or <FTGroup:2>
Cofactor Ni(2+)
Note: Binds #(Ni(2+),ion) per subunit.
end case

case <OC:Bacteria>
Subcellular location Cytoplasm.
end case

case <OC:Eukaryota> and <AnyFeature:Nter~350,~PS51368>
Similarity In the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
else
Similarity Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
end case


Cross-references [?]

case <FT:3> and <FT:4>
PROSITE PS01120; UREASE_1; 1;
end case

case <FT:2>
PROSITE PS00145; UREASE_2; 1;
end case


Gene Ontology [?]

case <FT:2>
GO:0016787; Molecular function: hydrolase activity.
end case

case <FTGroup:1> or <FTGroup:2>
GO:0046872; Molecular function: metal ion binding.
GO:0016151; Molecular function: nickel cation binding.
end case

case <OC:Bacteria>
GO:0005737; Cellular component: cytoplasm.
end case


Keywords [?]

case <OC:Bacteria>
Cytoplasm
end case

case <FT:2>
Hydrolase
end case

case <FTGroup:1> or <FTGroup:2>
Metal-binding
Nickel
end case


Features [?]

From: PS51368
Key     From     To       Description   Tag   Condition   FTGroup
DOMAIN     from     to       Urease #        
ACT_SITE     192     192       Proton donor     H  
BINDING     6     6       /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="#1     H   1
BINDING     8     8       /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="#1     H   1
BINDING     89     89       /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="#1" /note="via carbamate group     K   1
BINDING     89     89       /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="#2" /note="via carbamate group     K   1
BINDING     118     118       /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="#2     H   2
BINDING     144     144       /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="#2     H   2
BINDING     232     232       /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="#1     D   2
BINDING     91     91       /ligand="substrate     H  

Additional information [?]

Size range 420-470 amino acids
Related rules None
Repeats 1
Topology Undefined
Example Q5KCQ6 (UREA_CRYNE)
Scope
Eukaryota
Bacteria
Archaea

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


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UniProtKB rule member sequences [?]