3R31
Crystal structure of betaine aldehyde dehydrogenase from Agrobacterium tumefaciens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004029 | molecular_function | aldehyde dehydrogenase (NAD+) activity |
| 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 | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 3318 |
| Chain | Residue |
| A | ALA69 |
| A | ARG76 |
| A | ARG148 |
| A | HOH569 |
| B | PRO138 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 3319 |
| Chain | Residue |
| A | PRO138 |
| B | ALA69 |
| B | ARG76 |
| B | ARG148 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FySSGQVCSNGT |
| Chain | Residue | Details |
| A | PHE285-THR296 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGKSP |
| Chain | Residue | Details |
| A | MET257-PRO264 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | LYS170 | |
| A | GLU469 | |
| B | LYS170 | |
| B | GLU469 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | GLU258 | |
| B | GLU258 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | CYS292 | |
| B | CYS292 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | SER34 | |
| A | LYS462 | |
| A | GLY465 | |
| B | SER34 | |
| B | ILE35 | |
| B | ASP101 | |
| B | GLY158 | |
| B | LYS184 | |
| B | SER237 | |
| B | LEU252 | |
| B | GLY260 | |
| A | ILE35 | |
| B | GLU392 | |
| B | LYS462 | |
| B | GLY465 | |
| A | ASP101 | |
| A | GLY158 | |
| A | LYS184 | |
| A | SER237 | |
| A | LEU252 | |
| A | GLY260 | |
| A | GLU392 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: covalent => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | CYS292 | |
| B | CYS292 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00804 |
| Chain | Residue | Details |
| A | CYS292 | |
| B | CYS292 |
