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ProRule PRU00700


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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

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UniProtKB rule member sequences [?]