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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE S1A A 1000 |
| Chain | Residue |
| A | LYS274 |
| A | ARG277 |
| A | SER278 |
| A | GLU593 |
| A | MET594 |
| A | VAL598 |
| A | ASN599 |
| A | PHE704 |
Functional Information from PROSITE/UniProt
| site_id | PS00866 |
| Number of Residues | 15 |
| Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. FPLMIKASeggGGkG |
| Chain | Residue | Details |
| A | PHE449-GLY463 | |
| site_id | PS00867 |
| Number of Residues | 8 |
| Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL |
| Chain | Residue | Details |
| A | PHE578-LEU585 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| 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 | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q13085","evidenceCode":"ECO:0000250"}]} |
