Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016726 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor |
| A | 0019877 | biological_process | diaminopimelate biosynthetic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | LYS138 |
| A | SER143 |
| A | GLY144 |
| A | THR145 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | HIS135 |
| A | LYS138 |
Functional Information from PROSITE/UniProt
| site_id | PS01298 |
| Number of Residues | 18 |
| Details | DAPB Dihydrodipicolinate reductase signature. EViElHhpnKlDapSGTA |
| Chain | Residue | Details |
| A | GLU129-ALA146 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00102","evidenceCode":"ECO:0000255"}]} |
