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 | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 301 |
| Chain | Residue |
| A | LYS148 |
| C | HOH485 |
| A | LYS149 |
| A | PRO176 |
| A | GOL302 |
| C | GLY151 |
| C | PHE152 |
| C | SER153 |
| C | GOL301 |
| C | HOH402 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 302 |
| Chain | Residue |
| A | PHE152 |
| A | SER153 |
| A | GOL301 |
| A | HOH407 |
| B | LYS148 |
| B | LYS149 |
| B | GLY151 |
| B | PRO176 |
| C | GOL301 |
| C | HOH485 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | SER164 |
| A | TYR165 |
| A | ASP169 |
| A | HOH449 |
| A | HOH467 |
| A | HOH522 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 304 |
| Chain | Residue |
| A | HOH442 |
| A | HOH499 |
| A | HOH534 |
| C | HOH552 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| A | THR143 |
| A | VAL222 |
| B | HIS210 |
| B | LEU211 |
| B | HOH443 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 301 |
| Chain | Residue |
| A | GOL301 |
| A | GOL302 |
| B | PHE152 |
| B | SER153 |
| B | HOH406 |
| C | LYS149 |
| C | GLY151 |
| C | PRO176 |
| C | HOH485 |
| C | HOH503 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 302 |
| Chain | Residue |
| B | THR143 |
| B | VAL222 |
| B | HOH512 |
| C | HIS210 |
| C | LEU211 |
| C | PRO214 |
| C | HOH466 |
| C | HOH522 |
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"}]} |
