AC MF_01953; DC Protein; auto TR HAMAP; MF_01953; -; 1; level=0 XX Names: Urease_alpha XX ID URE1 case not DE RecName: Full=Urease subunit alpha; DE EC=3.5.1.5; DE AltName: Full=Urea amidohydrolase subunit alpha; GN Name=ureC; else case DE RecName: Full=Urease subunit beta; DE EC=3.5.1.5; DE AltName: Full=Urea amidohydrolase subunit beta; GN Name=ureB; end case XX 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; case and CC -!- COFACTOR: CC Name=Ni cation; Xref=ChEBI:CHEBI:25516; CC Note=Binds 2 nickel ions per subunit.; end case CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from CC urea (urease route): step 1/1. case CC -!- SUBUNIT: Heterohexamer of 3 UreA (alpha) and 3 UreB (beta) subunits. else case or CC -!- SUBUNIT: Heterohexamer of 3 UreC (alpha) and 3 UreAB (gamma/beta) CC subunits. else case or CC -!- SUBUNIT: May form a heterohexamer of 3 UreC (alpha) and 3 UreAB CC (gamma/beta) subunits. May also form a heterotrimer of UreA (gamma), CC UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to CC form the active enzyme. else CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) CC subunits. Three heterotrimers associate to form the active enzyme. end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. case CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel CC ions. end case CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Urease alpha subunit family. case CC -!- CAUTION: The orthologous protein is known as the alpha subunit (UreC) CC in most other bacteria. end case XX DR PROSITE; PS01120; UREASE_1; 1; trigger=no DR PROSITE; PS00145; UREASE_2; 1; trigger=no DR PROSITE; PS51368; UREASE_3; 1; trigger=yes DR Pfam; PF01979; Amidohydro_1; 1; trigger=no DR Pfam; PF00449; Urease_alpha; 1; trigger=no DR PRINTS; PR01752; UREASE; 1; trigger=no DR NCBIfam; TIGR01792; Urease_alph; 1; trigger=no XX KW Cytoplasm KW Hydrolase case or KW Metal-binding KW Nickel end case XX GO GO:0009039; F:urease activity case or GO GO:0016151; F:nickel cation binding end case GO GO:0019627; P:urea metabolic process GO GO:0005737; C:cytoplasm XX FT From: URE1_KLEAE (P18314) FT ACT_SITE 320 FT /note="Proton donor" FT Condition: H FT BINDING 134 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT Group: 2; Condition: H FT BINDING 136 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT Group: 2; Condition: H FT BINDING 217 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 217 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT /note="via carbamate group" FT Group: 2; Condition: K FT BINDING 246 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT Group: 1; Condition: H FT BINDING 272 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="2" FT Group: 1; Condition: H FT BINDING 360 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="1" FT Group: 2; Condition: D FT BINDING 219 FT /ligand="substrate" FT Condition: H FT MOD_RES 217 FT /note="N6-carboxylysine" FT Condition: K XX Size: 556-598; Related: None; Template: P18314; P77837; P69996; Scope: Bacteria Archaea; Sulfolobales Archaea; Halobacteria Fusion: Nter: None Cter: None Duplicate: in BRUA2, BRUAB, BRUME, BRUSU, ECO57, PSEU2, STRAW, STRCO Plasmid: in CLOPE, ECOLX, HALMA Comments: None XX # Revision 1.36 2023/06/01 //