9IZU
Cryo-EM structure of ALDH6A1-P62S
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0003723 | molecular_function | RNA binding |
| C | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005759 | cellular_component | mitochondrial matrix |
| C | 0006210 | biological_process | thymine catabolic process |
| C | 0006573 | biological_process | valine metabolic process |
| C | 0006574 | biological_process | L-valine catabolic process |
| C | 0009083 | biological_process | branched-chain amino acid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0019859 | biological_process | thymine metabolic process |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0006210 | biological_process | thymine catabolic process |
| D | 0006573 | biological_process | valine metabolic process |
| D | 0006574 | biological_process | L-valine catabolic process |
| D | 0009083 | biological_process | branched-chain amino acid catabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0019859 | biological_process | thymine metabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgAAGQRCMALS |
| Chain | Residue | Details |
| C | PHE278-SER289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P42412","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9EQ20","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9EQ20","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9EQ20","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
