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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU00700


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00700
General rule information [?]

Accession PRU00700
Dates 27-MAR-2008 (Created)
03-SEP-2024 (Last updated, Version 24)
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.
Scope(s) Eukaryota
Bacteria
Archaea
Example(s) Q5KCQ6;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FT:2> and <FTGroup:1> and <FTGroup:2> and not <OC:Bacteria> and not <OC:Archaea>
Protein name + 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 Reaction=urea + 2 H2O + H(+) = hydrogencarbonate + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938; EC=3.5.1.5;
end case
case <FTGroup:1> or <FTGroup:2>
COFACTOR Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Note=Binds #(Ni(2+),ion) per subunit.;
end case
case <OC:Bacteria>
SUBCELLULAR LOCATIONCytoplasm.
end case
case <OC:Eukaryota> and <AnyFeature:Nter~350,~PS51368>
SIMILARITYIn the C-terminal section; belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
else
SIMILARITYBelongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.
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

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

Cross-references [?]

PROSITE PS01120; UREASE_1; 1;
PROSITE PS00145; UREASE_2; 1;

Features [?]

From: PS51368
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Urease #"
ACT_SITE 192 192 /note="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
Fusion None
Repeats 1
Topology Undefined

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.

UniProtKB rule member sequences [?]