Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 35 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | ILE149 |
| A | GLY209 |
| A | GLY212 |
| A | ALA213 |
| A | PHE226 |
| A | THR227 |
| A | GLY228 |
| A | GLY229 |
| A | THR232 |
| A | LYS235 |
| A | VAL236 |
| A | GLY150 |
| A | GLU251 |
| A | LEU252 |
| A | GLY253 |
| A | CYS285 |
| A | GLU386 |
| A | PHE388 |
| A | HOH601 |
| A | HOH608 |
| A | HOH618 |
| A | HOH743 |
| A | ALA151 |
| A | HOH772 |
| A | HOH787 |
| A | HOH826 |
| A | HOH888 |
| A | HOH1001 |
| A | HOH1033 |
| A | TRP152 |
| A | ASN153 |
| A | LYS176 |
| A | SER178 |
| A | GLU179 |
| A | ASP208 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | LEU6 |
| A | ARG8 |
| A | HIS15 |
| A | HOH773 |
| A | HOH927 |
| A | HOH1057 |
| B | TYR4 |
| B | GLY5 |
| B | LEU6 |
| B | GLN7 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| A | SER2 |
| A | GLY5 |
| A | ARG37 |
| B | ASP17 |
| B | GLN39 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | binding site for Di-peptide NAD B 501 and CYS B 285 |
| Chain | Residue |
| B | ILE149 |
| B | GLY150 |
| B | TRP152 |
| B | ASN153 |
| B | LYS176 |
| B | SER178 |
| B | GLU179 |
| B | ASP208 |
| B | GLY209 |
| B | GLY212 |
| B | ALA213 |
| B | PHE226 |
| B | THR227 |
| B | GLY228 |
| B | GLY229 |
| B | THR232 |
| B | VAL236 |
| B | GLU251 |
| B | LEU252 |
| B | GLY253 |
| B | VAL284 |
| B | THR286 |
| B | ASN287 |
| B | GLU386 |
| B | PHE388 |
| B | LEU414 |
| B | HOH601 |
| B | HOH630 |
| B | HOH652 |
| B | HOH791 |
| B | HOH883 |
| B | HOH929 |
| B | HOH951 |
| B | HOH1009 |
| B | HOH1066 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | binding site for Di-peptide NAD B 501 and CYS B 285 |
| Chain | Residue |
| B | GLY229 |
| B | THR232 |
| B | VAL236 |
| B | GLU251 |
| B | LEU252 |
| B | GLY253 |
| B | VAL284 |
| B | THR286 |
| B | ASN287 |
| B | GLU386 |
| B | PHE388 |
| B | LEU414 |
| B | HOH601 |
| B | HOH630 |
| B | HOH652 |
| B | HOH791 |
| B | HOH883 |
| B | HOH929 |
| B | HOH951 |
| B | HOH1009 |
| B | HOH1066 |
| B | ILE149 |
| B | GLY150 |
| B | TRP152 |
| B | ASN153 |
| B | LYS176 |
| B | SER178 |
| B | GLU179 |
| B | ASP208 |
| B | GLY209 |
| B | GLY212 |
| B | ALA213 |
| B | PHE226 |
| B | THR227 |
| B | GLY228 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfSAGQVCTNGT |
| Chain | Residue | Details |
| A | PHE278-THR289 | |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. MELGGKSP |
| Chain | Residue | Details |
| A | MET250-PRO257 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"6WSB","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"6WSB","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Seems to be a necessary countercharge to the potassium cations","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"HAMAP-Rule","id":"MF_00804","evidenceCode":"ECO:0000255"}]} |
