Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0016874 | molecular_function | ligase activity |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0016874 | molecular_function | ligase activity |
| C | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| C | 0016874 | molecular_function | ligase activity |
| D | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| D | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE RCP A 1 |
| Chain | Residue |
| A | VAL2128 |
| A | GLU2236 |
| B | LEU1965 |
| B | VAL1968 |
| D | GLY1970 |
| A | ARG2158 |
| A | PHE2160 |
| A | SER2161 |
| A | GLY2162 |
| A | LEU2229 |
| A | GLU2230 |
| A | GLU2232 |
| A | GLY2233 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RCP B 2 |
| Chain | Residue |
| A | THR1960 |
| A | LEU1965 |
| A | VAL1968 |
| B | VAL2128 |
| B | ARG2158 |
| B | GLY2159 |
| B | PHE2160 |
| B | GLY2162 |
| B | LEU2229 |
| B | GLU2230 |
| B | GLY2233 |
| B | GLU2236 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE RCP C 3 |
| Chain | Residue |
| B | GLY1970 |
| C | VAL2128 |
| C | ARG2158 |
| C | GLY2159 |
| C | PHE2160 |
| C | SER2161 |
| C | GLY2162 |
| C | LEU2229 |
| C | GLU2230 |
| C | GLY2233 |
| C | GLU2236 |
| D | ALA1964 |
| D | LEU1965 |
| D | VAL1968 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RCP D 4 |
| Chain | Residue |
| C | LEU1965 |
| C | VAL1968 |
| D | VAL2128 |
| D | GLY2159 |
| D | PHE2160 |
| D | SER2161 |
| D | GLY2162 |
| D | LEU2229 |
| D | GLU2230 |
| D | GLU2232 |
| D | GLY2233 |
| D | GLU2236 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 330 |
| Details | Domain: {"description":"CoA carboxyltransferase N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01136","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1264 |
| Details | Domain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 650 |
| Details | Region: {"description":"Carboxyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01138","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| A | ILE1938 | |
| A | GLY1937 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| B | ILE1938 | |
| B | GLY1937 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| C | ILE1938 | |
| C | GLY1937 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| D | ILE1938 | |
| D | GLY1937 | |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| A | GLY2202 | |
| A | SER2203 | |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| B | GLY2202 | |
| B | SER2203 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| C | GLY2202 | |
| C | SER2203 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1xny |
| Chain | Residue | Details |
| D | GLY2202 | |
| D | SER2203 | |
