Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00866 |
| Number of Residues | 15 |
| Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASeggGGkG |
| Chain | Residue | Details |
| A | TYR343-GLY357 | |
| site_id | PS00867 |
| Number of Residues | 8 |
| Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL |
| Chain | Residue | Details |
| A | PHE472-LEU479 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 191 |
| Details | Domain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} |