6VWF
Structure of ALDH9A1 complexed with NAD+ in space group C222
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006081 | biological_process | aldehyde metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| A | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0042429 | biological_process | serotonin catabolic process |
| A | 0045329 | biological_process | carnitine biosynthetic process |
| A | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0140087 | molecular_function | acetaldehyde dehydrogenase (NAD+) activity |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006081 | biological_process | aldehyde metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0018467 | molecular_function | formaldehyde dehydrogenase (NAD+) activity |
| B | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| B | 0036094 | molecular_function | small molecule binding |
| B | 0042429 | biological_process | serotonin catabolic process |
| B | 0045329 | biological_process | carnitine biosynthetic process |
| B | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0140087 | molecular_function | acetaldehyde dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | ILE153 |
| A | GLY154 |
| A | LYS180 |
| A | PRO183 |
| A | GLY212 |
| A | ALA213 |
| A | GLY216 |
| A | GLN217 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| B | GLY154 |
| B | LYS180 |
| B | SER182 |
| B | PRO183 |
| B | ALA213 |
| B | GLY216 |
| B | ILE153 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FlTQGQVCCNGT |
| Chain | Residue | Details |
| A | PHE281-THR292 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU253-PRO260 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P56533","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Heiserich L.","Gottlieb E."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9JLJ2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JLJ2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9JLJ2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
