6TNM
E. coli aerobic trifunctional enzyme subunit-alpha
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003857 | molecular_function | 3-hydroxyacyl-CoA dehydrogenase activity |
| A | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0008692 | molecular_function | 3-hydroxybutyryl-CoA epimerase activity |
| A | 0009062 | biological_process | fatty acid catabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016509 | molecular_function | long-chain-3-hydroxyacyl-CoA dehydrogenase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0036125 | cellular_component | fatty acid beta-oxidation multienzyme complex |
| A | 0044248 | biological_process | cellular catabolic process |
| A | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 801 |
| Chain | Residue |
| A | PHE73 |
| A | GLU119 |
| A | GLU139 |
| A | ILE144 |
| A | GLY147 |
| A | PHE148 |
| A | PHE277 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ATP A 802 |
| Chain | Residue |
| A | VAL400 |
| A | VAL401 |
| A | VAL406 |
| A | LYS584 |
| A | ASP343 |
| A | ILE344 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue NO3 A 803 |
| Chain | Residue |
| A | VAL66 |
| A | ILE70 |
| A | GLN297 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue NO3 A 804 |
| Chain | Residue |
| A | GLY115 |
| A | PRO138 |
| A | GLU139 |
| A | LEU142 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 A 805 |
| Chain | Residue |
| A | PHE531 |
| A | TRP674 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 A 807 |
| Chain | Residue |
| A | PRO454 |
| A | NO3809 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 A 808 |
| Chain | Residue |
| A | ARG134 |
| A | GLN177 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 A 809 |
| Chain | Residue |
| A | ARG457 |
| A | NO3807 |
Functional Information from PROSITE/UniProt
| site_id | PS00067 |
| Number of Residues | 25 |
| Details | 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DcpGFFvNRvlfPYFagfsq.LLrdG |
| Chain | Residue | Details |
| A | ASP493-GLY517 |
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVNGyalGGGcecvLaTDY |
| Chain | Residue | Details |
| A | ILE106-TYR126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: For 3-hydroxyacyl-CoA dehydrogenase activity => ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745 |
| Chain | Residue | Details |
| A | HIS450 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01621 |
| Chain | Residue | Details |
| A | ASP296 | |
| A | ASP343 | |
| A | VAL400 | |
| A | LYS407 | |
| A | SER429 | |
| A | ASN453 | |
| A | ASN500 | |
| A | TYR660 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000305 |
| Chain | Residue | Details |
| A | MET324 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01621 |
| Chain | Residue | Details |
| A | GLU119 | |
| A | GLU139 |
