AC   PRU00700;
DC   Domain;
TR   PROSITE; PS51368; UREASE_3; 1; level=0
XX
Names: 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.
XX
case <FT:2> and <FTGroup:1> and <FTGroup:2> and not <OC:Bacteria> and not <OC:Archaea>
DE   + AltName: Full=Urease;
DE            EC=3.5.1.5;
DE   AltName: Full=Urea amidohydrolase;
end case
XX
case <FT:2> and <FTGroup:1> and <FTGroup:2>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
end case
case <FTGroup:1> or <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC       Note=Binds #(Ni(2+),ion) per subunit.;
end case
case <OC:Bacteria>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
case <OC:Eukaryota> and <AnyFeature:Nter~350,~PS51368>
CC   -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent
CC       hydrolases superfamily. Urease alpha subunit family.
else
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Urease alpha subunit family.
end case
XX
case <FT:3> and <FT:4>
DR   PROSITE; PS01120; UREASE_1; 1; trigger=no
end case
case <FT:2>
DR   PROSITE; PS00145; UREASE_2; 1; trigger=no
end case
XX
case <FT:2>
GO   GO:0016787; F:hydrolase activity
end case
case <FTGroup:1> or <FTGroup:2>
GO   GO:0046872; F:metal ion binding
GO   GO:0016151; F:nickel cation binding
end case
case <OC:Bacteria>
GO   GO:0005737; C:cytoplasm
end case
XX
case <OC:Bacteria>
KW   Cytoplasm
end case
case <FT:2>
KW   Hydrolase
end case
case <FTGroup:1> or <FTGroup:2>
KW   Metal-binding
KW   Nickel
end case
XX
FT   From: PS51368
FT   DOMAIN          from..to
FT                   /note="Urease #"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         6
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="#1"
FT   Group: 1; Condition: H
FT   BINDING         8
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="#1"
FT   Group: 1; Condition: H
FT   BINDING         89
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="#1"
FT                   /note="via carbamate group"
FT   Group: 1; Condition: K
FT   BINDING         89
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="#2"
FT                   /note="via carbamate group"
FT   Group: 1; Condition: K
FT   BINDING         118
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="#2"
FT   Group: 2; Condition: H
FT   BINDING         144
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="#2"
FT   Group: 2; Condition: H
FT   BINDING         232
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="#1"
FT   Group: 2; Condition: D
FT   BINDING         91
FT                   /ligand="substrate"
FT   Condition: H
XX
Chop: Nter=0; Cter=0;
Size: 420-470;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q5KCQ6;
Scope:
 Eukaryota
 Bacteria
 Archaea
Comments: None
XX
# Revision 1.21 2022/11/19
//