Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| A | 0009089 | biological_process | L-lysine biosynthetic process via diaminopimelate |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A1418 |
| Chain | Residue |
| A | TYR187 |
| A | THR188 |
| A | ILE198 |
| A | SER201 |
| A | LEU225 |
| A | GLY227 |
| A | HOH2119 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PLP A1419 |
| Chain | Residue |
| A | GLU68 |
| A | SER91 |
| A | ARG138 |
| A | HIS185 |
| A | TYR187 |
| A | THR190 |
| A | GLY228 |
| A | GLU269 |
| A | SER270 |
| A | GLY271 |
| A | ARG272 |
| A | CYS346 |
| A | TYR375 |
| A | HOH2159 |
| A | HOH2229 |
| A | HOH2230 |
| A | HOH2231 |
| A | SER47 |
| A | LYS49 |
Functional Information from PROSITE/UniProt
| site_id | PS00879 |
| Number of Residues | 14 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Giv....CeCINLGGGFG |
| Chain | Residue | Details |
| A | GLY217-GLY230 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | LYS49 | |
| A | LYS151 | |
