HAMAP rule MF_01953
General rule information
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Accession | MF_01953 |
Dates | 10-APR-2006 (Created) 1-JUN-2023 (Last updated, Version 36) |
Name | Urease_alpha |
Scope | Bacteria
Archaea; Sulfolobales
Archaea; Halobacteria |
Templates | P18314 (URE1_KLEAE); P77837 (URE1_BACSU); P69996 (URE1_HELPY): [Recover all] |
Triggered by |
Propagated annotation
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Identifier, protein and gene names
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Identifier |
|
case not <OC:Campylobacterales>
Protein name |
|
Gene name |
|
else case <OC:Campylobacterales>
Protein name |
|
Gene name |
|
end case
Comments
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Catalytic activity | RHEA:20557: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
EC 3.5.1.5 |
case <FTGroup:1> and <FTGroup:2>
Cofactor | Ni cation Note: Binds 2 nickel ions per subunit. |
end case
Pathway | Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. |
case <OC:Campylobacterales>
Subunit | Heterohexamer of 3 UreA (alpha) and 3 UreB (beta) subunits. |
else case <OC:Deinococcus> or <OC:Sulfolobus>
Subunit | Heterohexamer of 3 UreC (alpha) and 3 UreAB (gamma/beta) subunits. |
else case <OS:Pseudomonas syringae> or <OC:Streptomyces>
Subunit | May form a heterohexamer of 3 UreC (alpha) and 3 UreAB (gamma/beta) subunits. May also form a heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme. |
else
Subunit | Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme. |
end case
Subcellular location | Cytoplasm. |
case <FT:4>
Ptm | Carboxylation allows a single lysine to coordinate two nickel ions. |
end case
Similarity | Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family. |
case <OC:Campylobacterales>
Caution | The orthologous protein is known as the alpha subunit (UreC) in most other bacteria. |
end case
Keywords
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case <FTGroup:1> or <FTGroup:2>
end case
Gene Ontology
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GO:0009039; Molecular function: urease activity.
case <FTGroup:1> or <FTGroup:2>
GO:0016151; Molecular function: nickel cation binding.
end case
Cross-references
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PROSITE | PS01120; UREASE_1; 1; |
PS00145; UREASE_2; 1; | |
PS51368; UREASE_3; 1; trigger=PRU00700; | |
Pfam | PF01979; Amidohydro_1; 1; |
PF00449; Urease_alpha; 1; | |
PRINTS | PR01752; UREASE; 1; |
NCBIfam | TIGR01792; Urease_alph; 1; |
Features
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From: URE1_KLEAE (P18314) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 320 | 320 | Proton donor | H | ||||||||
BINDING | 134 | 134 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="1 | H | 2 | |||||||
BINDING | 136 | 136 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="1 | H | 2 | |||||||
BINDING | 217 | 217 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="1" /note="via carbamate group | K | 1 | |||||||
BINDING | 217 | 217 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="2" /note="via carbamate group | K | 2 | |||||||
BINDING | 246 | 246 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="2 | H | 1 | |||||||
BINDING | 272 | 272 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="2 | H | 1 | |||||||
BINDING | 360 | 360 | /ligand="Ni(2+)" /ligand_id="ChEBI:CHEBI:49786" /ligand_label="1 | D | 2 | |||||||
BINDING | 219 | 219 | /ligand="substrate | H | ||||||||
MOD_RES | 217 | 217 | N6-carboxylysine | K |
Additional information
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Size range | 556-598 amino acids |
Related rules | None |
Fusion | None |