4I8Q
Structure of the aminoaldehyde dehydrogenase 1 E260A mutant from Solanum lycopersicum (SlAMADH1-E260A)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008802 | molecular_function | betaine-aldehyde dehydrogenase 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 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 activity |
| A | 0110095 | biological_process | cellular detoxification of aldehyde |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAD A 601 |
| Chain | Residue |
| A | ILE158 |
| A | GLY218 |
| A | GLY222 |
| A | GLY223 |
| A | PHE236 |
| A | THR237 |
| A | GLY238 |
| A | SER239 |
| A | THR242 |
| A | ILE246 |
| A | ALA260 |
| A | THR159 |
| A | LEU261 |
| A | GLY262 |
| A | CYS295 |
| A | GLU394 |
| A | PHE396 |
| A | TRP460 |
| A | PRO160 |
| A | TRP161 |
| A | ASN162 |
| A | LYS185 |
| A | PRO186 |
| A | SER187 |
| A | GLU188 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 602 |
| Chain | Residue |
| A | THR35 |
| A | GLU37 |
| A | LYS372 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 603 |
| Chain | Residue |
| A | ILE324 |
| A | HIS369 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 605 |
| Chain | Residue |
| A | ASN26 |
| A | ILE38 |
| A | ILE39 |
| A | GLY40 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG A 607 |
| Chain | Residue |
| A | GLU493 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 608 |
| Chain | Residue |
| A | PRO241 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 609 |
| Chain | Residue |
| A | ASP113 |
| A | TRP170 |
| A | ASN456 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 612 |
| Chain | Residue |
| A | ILE31 |
| A | ASP99 |
| A | LEU189 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10007, ECO:0000269|PubMed:23408433 |
| Chain | Residue | Details |
| A | ALA260 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10008, ECO:0000269|PubMed:23408433 |
| Chain | Residue | Details |
| A | CYS295 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23408433, ECO:0007744|PDB:4I8Q, ECO:0007744|PDB:4I9B |
| Chain | Residue | Details |
| A | ASP99 | |
| A | THR159 | |
| A | LYS185 | |
| A | LEU189 | |
| A | GLY238 | |
| A | ILE31 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23408433, ECO:0007744|PDB:4I8Q |
| Chain | Residue | Details |
| A | TRP460 | |
| A | LEU261 | |
| A | GLU394 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P20000 |
| Chain | Residue | Details |
| A | ASN162 |
