4I9B
Structure of aminoaldehyde dehydrogenase 1 from Solanum lycopersium (SlAMADH1) with a thiohemiacetal intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0031402 | molecular_function | sodium ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| A | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| A | 0110095 | biological_process | cellular detoxification of aldehyde |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008802 | molecular_function | betaine-aldehyde dehydrogenase (NAD+) activity |
| 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 | 0019145 | molecular_function | aminobutyraldehyde dehydrogenase (NAD+) activity |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0031402 | molecular_function | sodium ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047105 | molecular_function | 4-trimethylammoniobutyraldehyde dehydrogenase activity |
| B | 0047107 | molecular_function | gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity |
| B | 0110095 | biological_process | cellular detoxification of aldehyde |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | ILE158 |
| A | GLY223 |
| A | PHE236 |
| A | GLY238 |
| A | SER239 |
| A | THR242 |
| A | ILE246 |
| A | HOH753 |
| A | HOH873 |
| A | THR159 |
| A | TRP161 |
| A | LYS185 |
| A | PRO186 |
| A | SER187 |
| A | GLU188 |
| A | GLY218 |
| A | GLY222 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 602 |
| Chain | Residue |
| A | ILE31 |
| A | ASP99 |
| A | LEU189 |
| A | HOH778 |
| A | HOH866 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 603 |
| Chain | Residue |
| A | THR382 |
| A | ASP383 |
| A | VAL384 |
| A | VAL402 |
| A | THR404 |
| A | HOH832 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 604 |
| Chain | Residue |
| B | TYR143 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1KA A 605 |
| Chain | Residue |
| A | ASN162 |
| A | TYR163 |
| A | CYS295 |
| A | SER296 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD B 601 |
| Chain | Residue |
| B | ILE158 |
| B | THR159 |
| B | TRP161 |
| B | LYS185 |
| B | PRO186 |
| B | SER187 |
| B | GLU188 |
| B | GLY218 |
| B | GLY222 |
| B | GLY223 |
| B | PHE236 |
| B | GLY238 |
| B | SER239 |
| B | THR242 |
| B | ILE246 |
| B | HOH840 |
| B | HOH970 |
| B | HOH971 |
| B | HOH979 |
| B | HOH994 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 602 |
| Chain | Residue |
| B | ILE31 |
| B | ASP99 |
| B | LEU189 |
| B | HOH733 |
| B | HOH857 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 603 |
| Chain | Residue |
| A | TYR143 |
| B | THR454 |
| B | PHE455 |
| B | HOH810 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1KA B 604 |
| Chain | Residue |
| B | ASN162 |
| B | TYR163 |
| B | CYS295 |
| B | SER296 |
| B | TRP460 |
| B | HOH737 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FaNTGQVCSATS |
| Chain | Residue | Details |
| A | PHE288-SER299 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU259-PRO266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10007","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4I8Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I9B","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23408433","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4I8Q","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P20000","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
