1F14
L-3-HYDROXYACYL-COA DEHYDROGENASE (APO)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0007283 | biological_process | spermatogenesis |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0009725 | biological_process | response to hormone |
| A | 0014823 | biological_process | response to activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030154 | biological_process | cell differentiation |
| A | 0032868 | biological_process | response to insulin |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046676 | biological_process | negative regulation of insulin secretion |
| A | 0050796 | biological_process | regulation of insulin secretion |
| A | 0070403 | molecular_function | NAD+ binding |
| A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
| B | 0003857 | molecular_function | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0007283 | biological_process | spermatogenesis |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0009725 | biological_process | response to hormone |
| B | 0014823 | biological_process | response to activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030154 | biological_process | cell differentiation |
| B | 0032868 | biological_process | response to insulin |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046676 | biological_process | negative regulation of insulin secretion |
| B | 0050796 | biological_process | regulation of insulin secretion |
| B | 0070403 | molecular_function | NAD+ binding |
| B | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
Functional Information from PROSITE/UniProt
| site_id | PS00067 |
| Number of Residues | 25 |
| Details | 3HCDH 3-hydroxyacyl-CoA dehydrogenase signature. DtpGFIvNRllvPYLmeair.LYerG |
| Chain | Residue | Details |
| A | ASP201-GLY225 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10231530","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10840044","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10840044","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 18 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61425","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"29192674","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2hdh |
| Chain | Residue | Details |
| A | ASN208 | |
| A | SER137 | |
| A | HIS158 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 2hdh |
| Chain | Residue | Details |
| B | ASN208 | |
| B | SER137 | |
| B | HIS158 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 336 |
| Chain | Residue | Details |
| A | SER137 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS158 | proton acceptor, proton donor |
| A | GLU170 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
| A | ASN208 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 336 |
| Chain | Residue | Details |
| B | SER137 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS158 | proton acceptor, proton donor |
| B | GLU170 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
| B | ASN208 | electrostatic stabiliser, hydrogen bond donor |
