PRU00700
General rule information
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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
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Description
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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
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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
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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
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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.
GO:0016151; Molecular function: nickel cation binding.
end case
case <OC:Bacteria>
GO:0005737; Cellular component: cytoplasm.
end case
Keywords
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case <OC:Bacteria>
end case
case <FT:2>
end case
case <FTGroup:1> or <FTGroup:2>
end case
Features
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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
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Size range | 420-470 amino acids |
Related rules | None |
Repeats | 1 |
Topology | Undefined |
Example | Q5KCQ6 (UREA_CRYNE) |
Scope | Eukaryota
Bacteria
Archaea |
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
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UniProtKB/Swiss-Prot sets
Archaea [4] Bacteria [261] Eukaryota [11] All [ 276 ]
- Retrieve set of proteins with 3D structure for this domain