2UBP
STRUCTURE OF NATIVE UREASE FROM BACILLUS PASTEURII
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 | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| 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 | 0019627 | biological_process | urea metabolic process |
| 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 | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 C 900 |
| Chain | Residue |
| C | HIS249 |
| C | GLY280 |
| C | HIS323 |
| C | ARG339 |
| C | HOH972 |
| C | HOH1046 |
| C | HOH1167 |
| C | HOH1168 |
| C | HOH1245 |
| C | HIS222 |
| C | GLU223 |
| C | ASP224 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NI C 901 |
| Chain | Residue |
| C | KCX220 |
| C | HIS222 |
| C | HIS249 |
| C | HIS275 |
| C | GLY280 |
| C | NI902 |
| C | HOH972 |
| C | HOH990 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NI C 902 |
| Chain | Residue |
| C | HIS137 |
| C | HIS139 |
| C | KCX220 |
| C | ASP363 |
| C | NI901 |
| C | HOH990 |
| C | HOH1043 |
| site_id | CAT |
| Number of Residues | 6 |
| Details | THE COORDINATION OF THE 2 NICKEL 2+ METALLOCENTER IS COMPLETED BY A CLUSTER OF WATERS |
| Chain | Residue |
| C | HIS137 |
| C | HIS139 |
| C | KCX220 |
| C | HIS249 |
| C | HIS275 |
| C | ASP363 |
Functional Information from PROSITE/UniProt
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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => 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 |
| Chain | Residue | Details |
| C | VAL138 | |
| C | ALA364 | |
| C | VAL276 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30969470 |
| Chain | Residue | Details |
| C | THR171 | |
| C | GLU223 | |
| C | SER250 | |
| C | MET367 | |
| C | PHE140 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: via carbamate group => 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 |
| 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 |
