Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NI C 900 |
| Chain | Residue |
| C | HIS275 |
| C | GLY280 |
| C | 2PA902 |
| C | KCX220 |
| C | HIS222 |
| C | HIS249 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI C 901 |
| Chain | Residue |
| C | HIS137 |
| C | HIS139 |
| C | KCX220 |
| C | ASP363 |
| C | 2PA902 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 2PA C 902 |
| Chain | Residue |
| C | HIS137 |
| C | HIS139 |
| C | ALA170 |
| C | KCX220 |
| C | HIS222 |
| C | HIS249 |
| C | HIS275 |
| C | GLY280 |
| C | HIS323 |
| C | ASP363 |
| C | ALA366 |
| C | MET367 |
| C | NI900 |
| C | NI901 |
| site_id | CAT |
| Number of Residues | 6 |
| Details | THE DINUCLEAR NICKEL 2+ METALLOCENTER IS INHIBITED BY A MOLECULE OF DIAMIDOPHOSPHATE, MIMICKING THE TETRAHEDRAL TRANSITION STATE OF UREA HYDROLYSIS |
| Chain | Residue |
| C | HIS137 |
| C | HIS139 |
| C | KCX220 |
| C | HIS249 |
| C | HIS275 |
| C | ASP363 |
Functional Information from PROSITE/UniProt
| site_id | PS00145 |
| Number of Residues | 17 |
| Details | UREASE_2 Urease active site. MVCHHLkqnIpeDVaFA |
| Chain | Residue | Details |
| C | MET320-ALA336 | |
| site_id | PS01120 |
| Number of Residues | 14 |
| Details | UREASE_1 Urease nickel ligands signature. TAGGIDtHVHfinP |
| Chain | Residue | Details |
| C | THR130-PRO143 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305 |
| Chain | Residue | Details |
| C | HIS324 | |
| Chain | Residue | Details |
| C | VAL138 | |
| C | VAL276 | |
| C | ALA364 | |
| Chain | Residue | Details |
| C | PHE140 | |
| C | THR171 | |
| C | GLU223 | |
| C | SER250 | |
| C | MET367 | |
| Chain | Residue | Details |
| C | ILE221 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231, ECO:0007744|PDB:1IE7, ECO:0007744|PDB:1S3T, ECO:0007744|PDB:1UBP, ECO:0007744|PDB:2UBP, ECO:0007744|PDB:4UBP |
| Chain | Residue | Details |
| C | ILE221 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1kra |
| Chain | Residue | Details |
| C | HIS323 | |
| C | ASP224 | |
| C | ARG339 | |
| C | HIS222 | |
