Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016866 | molecular_function | intramolecular transferase activity |
| A | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
| A | 0031419 | molecular_function | cobalamin binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016866 | molecular_function | intramolecular transferase activity |
| B | 0019652 | biological_process | lactate fermentation to propionate and acetate |
| B | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
| B | 0031419 | molecular_function | cobalamin binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 43 |
| Details | binding site for residue B12 A 1000 |
| Chain | Residue |
| A | TYR105 |
| A | GLY349 |
| A | TRP350 |
| A | LEU352 |
| A | GLU386 |
| A | ALA387 |
| A | ALA389 |
| A | LEU390 |
| A | GLN470 |
| A | GLY628 |
| A | HIS629 |
| A | PHE133 |
| A | ASP630 |
| A | ARG631 |
| A | GLY632 |
| A | GLY672 |
| A | SER674 |
| A | LEU676 |
| A | ALA678 |
| A | GLY704 |
| A | GLY705 |
| A | PHE724 |
| A | LEU135 |
| A | PRO725 |
| A | PRO726 |
| A | THR728 |
| A | 5AD1001 |
| A | NJS1002 |
| A | HOH1213 |
| A | HOH1219 |
| A | HOH1228 |
| A | HOH1233 |
| A | HOH1317 |
| A | HIS138 |
| A | HOH1323 |
| A | HOH1343 |
| A | HOH1359 |
| A | HOH1376 |
| A | ALA155 |
| A | VAL222 |
| A | ARG223 |
| A | THR225 |
| A | GLU263 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue K A 1003 |
| Chain | Residue |
| A | THR137 |
| A | TYR141 |
| A | ILE159 |
| A | ASP160 |
| A | HOH1175 |
| site_id | AC3 |
| Number of Residues | 49 |
| Details | binding site for residues 5AD A 1001 and NJS A 1002 |
| Chain | Residue |
| A | TYR91 |
| A | THR93 |
| A | MET94 |
| A | ASN97 |
| A | GLN98 |
| A | THR101 |
| A | ARG103 |
| A | TYR105 |
| A | GLY107 |
| A | ALA132 |
| A | ALA155 |
| A | SER180 |
| A | THR182 |
| A | THR211 |
| A | GLN213 |
| A | ARG223 |
| A | ASN252 |
| A | TYR259 |
| A | HIS260 |
| A | ARG299 |
| A | SER301 |
| A | PHE303 |
| A | ARG342 |
| A | THR343 |
| A | HIS344 |
| A | GLN346 |
| A | GLN377 |
| A | SER378 |
| A | ASN382 |
| A | GLU386 |
| A | LEU390 |
| A | PRO391 |
| A | B121000 |
| A | HOH1117 |
| A | HOH1144 |
| A | HOH1145 |
| A | HOH1168 |
| A | HOH1174 |
| A | HOH1210 |
| A | HOH1211 |
| A | HOH1212 |
| A | HOH1273 |
| A | HOH1282 |
| A | HOH1301 |
| A | HOH1321 |
| A | HOH1329 |
| A | HOH1339 |
| A | HOH1388 |
| A | HOH1389 |
Functional Information from PROSITE/UniProt
| site_id | PS00213 |
| Number of Residues | 12 |
| Details | LIPOCALIN Lipocalin signature. DLE..QVRGRWRNA |
| Chain | Residue | Details |
| B | ASP11-ALA22 | |
| site_id | PS00544 |
| Number of Residues | 26 |
| Details | METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTqlVLqQEsgttRpiDPwGGS |
| Chain | Residue | Details |
| A | ARG397-SER422 | |
| B | ARG365-SER390 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 132 |
| Details | Domain: {"description":"B12-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00666","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 25 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11653","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P11653","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P11653","evidenceCode":"ECO:0000250"}]} |
