Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008710 | molecular_function | 8-amino-7-oxononanoate synthase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | LEU147 |
| A | ARG148 |
| A | ARG149 |
| A | HOH1203 |
| A | HOH1245 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | HOH1238 |
| A | ARG22 |
| A | ARG23 |
| A | ARG101 |
| A | LEU256 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 500 |
| Chain | Residue |
| A | SER179 |
| A | KAM400 |
| A | HOH1069 |
| A | HOH1092 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE KAM A 400 |
| Chain | Residue |
| A | ARG21 |
| A | SER76 |
| A | SER107 |
| A | GLY108 |
| A | PHE109 |
| A | HIS133 |
| A | GLU175 |
| A | SER179 |
| A | ASP204 |
| A | ALA206 |
| A | HIS207 |
| A | THR233 |
| A | LYS236 |
| A | ILE263 |
| A | TYR264 |
| A | SER265 |
| A | THR266 |
| A | ILE348 |
| A | THR352 |
| A | MG500 |
| A | HOH1004 |
| A | HOH1013 |
| A | HOH1092 |
| A | HOH1161 |
| A | HOH1237 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFGKGFGVSG |
| Chain | Residue | Details |
| A | THR233-GLY242 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ARG21 | |
| A | HIS133 | |
| A | THR233 | |
| A | THR352 | |
| Chain | Residue | Details |
| A | GLY108 | |
| A | SER179 | |
| A | HIS207 | |
| Chain | Residue | Details |
| A | LYS236 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | ASP204 | |
| A | GLU175 | |
| A | LYS236 | |
| A | HIS133 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | HIS207 | |
| A | PHE238 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | HIS207 | |
| A | LYS236 | |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 430 |
| Chain | Residue | Details |
| A | ASN47 | electrostatic stabiliser |
| A | HIS133 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | GLU175 | electrostatic stabiliser |
| A | SER179 | modifies pKa |
| A | ASP204 | electrostatic stabiliser |
| A | HIS207 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | LYS236 | covalent catalysis, proton shuttle (general acid/base) |
