1A5K
K217E VARIANT OF KLEBSIELLA AEROGENES UREASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009039 | molecular_function | urease activity |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019627 | biological_process | urea metabolic process |
| A | 0043419 | biological_process | urea catabolic process |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009039 | molecular_function | urease activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0035550 | cellular_component | urease complex |
| B | 0043419 | biological_process | urea catabolic process |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009039 | molecular_function | urease activity |
| C | 0016151 | molecular_function | nickel cation binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0043419 | biological_process | urea catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 438 |
| Details | Domain: {"description":"Urease","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"via carbamate group"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10913264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7754395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8702515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8718850","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1kra |
| Chain | Residue | Details |
| C | ASP221 | |
| C | HIS320 | |
| C | ARG336 | |
| C | HIS219 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 87 |
| Chain | Residue | Details |
| C | HIS134 | metal ligand |
| C | ASP360 | activator, metal ligand |
| C | HIS136 | metal ligand |
| C | GLU217 | activator, metal ligand |
| C | HIS219 | proton acceptor, proton donor, proton relay |
| C | ASP221 | activator, proton acceptor, proton donor |
| C | HIS246 | metal ligand |
| C | HIS272 | metal ligand |
| C | HIS320 | proton acceptor, proton donor |
| C | ARG336 | activator |
