Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016829 | molecular_function | lyase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016829 | molecular_function | lyase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016829 | molecular_function | lyase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 301 |
| Chain | Residue |
| A | GLU238 |
| C | LYS51 |
| C | PRO200 |
| C | ARG201 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| B | HOH406 |
| A | LYS148 |
| A | LYS149 |
| A | GLY151 |
| B | PHE152 |
| B | SER153 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 303 |
| Chain | Residue |
| A | ASN161 |
| A | TYR165 |
| C | TYR188 |
| C | GLU195 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 304 |
| Chain | Residue |
| A | LYS178 |
| A | HOH465 |
| A | HOH471 |
| B | ARG173 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 305 |
| Chain | Residue |
| A | ASN60 |
| A | HIS104 |
| A | ARG182 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 306 |
| Chain | Residue |
| A | LYS19 |
| A | ARG23 |
| A | TYR58 |
| A | ASP59 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 301 |
| Chain | Residue |
| B | THR2 |
| B | VAL6 |
| B | LEU8 |
| B | GLN39 |
| B | ALA40 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 301 |
| Chain | Residue |
| C | LYS19 |
| C | ARG23 |
| C | ASP59 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 302 |
| Chain | Residue |
| C | ARG45 |
| C | LEU89 |
| C | ASP92 |
| C | CYS93 |
| C | HOH438 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 303 |
| Chain | Residue |
| C | ASN60 |
| C | HIS104 |
| C | ARG182 |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaMQGhgiGGGfvmgLfADI |
| Chain | Residue | Details |
| A | ILE98-ILE118 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"32948786","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Q1K","evidenceCode":"ECO:0007744"}]} |
