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UniProt functional annotation for P18314 | ||
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| UniProt code: P18314. |
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| Organism: | |
Klebsiella aerogenes (Enterobacter aerogenes). |
| Taxonomy: | |
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella. |
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| Catalytic activity: | |
Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10500143, ECO:0000269|PubMed:11015224, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:2211515, ECO:0000269|PubMed:7721685, ECO:0000269|PubMed:7855593, ECO:0000269|PubMed:7909161, ECO:0000269|PubMed:8318888, ECO:0000269|PubMed:8808930}; |
| Cofactor: | |
Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:1624427, ECO:0000269|PubMed:8318888}; Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:1624427, ECO:0000269|PubMed:8318888}; |
| Activity regulation: | |
The apoenzyme can be activated in vitro in the presence of nickel ions and carbon dioxide, which promotes carboxylation of Lys-217. {ECO:0000269|PubMed:10500143, ECO:0000269|PubMed:11015224, ECO:0000269|PubMed:7855593, ECO:0000269|PubMed:8808930}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=2.3 mM for urea {ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:8318888}; Vmax=1.9 mmol/min/mg enzyme {ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:8318888}; pH dependence: Optimum pH is 7.75. {ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:8318888}; |
| Pathway: | |
Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01953}. |
| Subunit: | |
Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme. The apoenzyme interacts with an accessory complex composed of UreD, UreF and UreG, which is required for the assembly of the nickel containing metallocenter of UreC. The UreE protein may also play a direct role as a metallochaperone in nickel transfer to the urease apoprotein. {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10500143, ECO:0000269|PubMed:10555581, ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:14749331, ECO:0000269|PubMed:7721685, ECO:0000269|PubMed:7754395, ECO:0000269|PubMed:7909161, ECO:0000269|PubMed:8702515, ECO:0000269|PubMed:8718850, ECO:0000269|PubMed:8808930, ECO:0000269|PubMed:9201965, ECO:0000269|PubMed:9558361}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}. |
| Ptm: | |
Carboxylation allows a single lysine to coordinate two nickel ions. {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:7754395, ECO:0000269|PubMed:8702515, ECO:0000269|PubMed:8718850}. |
| Similarity: | |
Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}. |
Annotations taken from UniProtKB at the EBI.