Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004733 | molecular_function | pyridoxamine phosphate oxidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042816 | biological_process | vitamin B6 metabolic process |
| A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 340 |
| Chain | Residue |
| A | GLU114 |
| A | LYS119 |
| A | GLN174 |
| A | SER175 |
| A | HOH495 |
| A | HOH579 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN A 300 |
| Chain | Residue |
| A | LEU97 |
| A | LEU98 |
| A | PHE110 |
| A | THR111 |
| A | SER115 |
| A | ARG116 |
| A | LYS117 |
| A | TYR132 |
| A | GLN139 |
| A | ARG141 |
| A | GLN174 |
| A | SER175 |
| A | TRP219 |
| A | ARG229 |
| A | PLP320 |
| A | HOH428 |
| A | HOH429 |
| A | HOH436 |
| A | HOH465 |
| A | GLU77 |
| A | ARG95 |
| A | MET96 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLP A 320 |
| Chain | Residue |
| A | LEU98 |
| A | LYS100 |
| A | TYR157 |
| A | ARG161 |
| A | SER165 |
| A | GLN174 |
| A | ARG225 |
| A | HIS227 |
| A | PRO261 |
| A | FMN300 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 360 |
| Chain | Residue |
| A | CYS72 |
| A | PRO135 |
Functional Information from PROSITE/UniProt
| site_id | PS01064 |
| Number of Residues | 14 |
| Details | PYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. MEFWQgqtnRLHDR |
| Chain | Residue | Details |
| A | MET216-ARG229 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12824491","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AFI7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1g79 |
| Chain | Residue | Details |
| A | ARG225 | |
