Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| A | 0004141 | molecular_function | dethiobiotin synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| B | 0004141 | molecular_function | dethiobiotin synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | GLY124 |
| A | LYS283 |
| A | HOH708 |
| A | HOH759 |
| A | HOH785 |
| A | HOH788 |
| A | HOH838 |
| B | PRO317 |
| B | THR318 |
| B | HOH695 |
| A | SER125 |
| A | TYR157 |
| A | HIS158 |
| A | GLY159 |
| A | GLU220 |
| A | ASP254 |
| A | ILE256 |
| A | ALA257 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue 3G8 A 502 |
| Chain | Residue |
| A | PRO24 |
| A | TYR25 |
| A | TRP64 |
| A | GLY172 |
| A | ARG400 |
| A | HOH793 |
| A | HOH852 |
| A | HOH922 |
| B | GLY93 |
| B | GLY316 |
| B | PRO317 |
| B | THR318 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | HIS271 |
| A | ALA272 |
| A | HOH602 |
| A | HOH616 |
| B | ARG246 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | PRO234 |
| A | HIS271 |
| A | HOH616 |
| A | HOH796 |
| A | HOH933 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ARG154 |
| A | PHE187 |
| A | ALA188 |
| A | PRO189 |
| A | HOH822 |
| A | HOH897 |
| A | HOH903 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | SER200 |
| A | ALA201 |
| A | GLU204 |
| A | ASP239 |
| A | ASP242 |
| A | ILE243 |
| A | ARG246 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | ARG344 |
| A | ILE413 |
| A | CYS414 |
| A | THR415 |
| A | PRO416 |
| A | HOH782 |
| A | HOH987 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue PLP B 501 |
| Chain | Residue |
| A | PRO317 |
| A | THR318 |
| A | HOH696 |
| B | GLY124 |
| B | SER125 |
| B | TYR157 |
| B | HIS158 |
| B | GLU220 |
| B | ASP254 |
| B | ILE256 |
| B | ALA257 |
| B | LYS283 |
| B | HOH681 |
| B | HOH709 |
| B | HOH741 |
| B | HOH742 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue 3G8 B 502 |
| Chain | Residue |
| A | GLY93 |
| A | GLY316 |
| A | PRO317 |
| A | THR318 |
| B | PRO24 |
| B | TYR25 |
| B | TRP64 |
| B | GLY172 |
| B | HOH817 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 503 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | VAL222 |
| B | HIS232 |
| B | PRO234 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | HOH848 |
| B | VAL108 |
| B | ASP109 |
| B | THR111 |
| B | PRO112 |
| B | ALA113 |
| B | GLY114 |
| B | LEU115 |
| B | HOH717 |
| B | HOH804 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 506 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEIat.GFgRtGalfaadhagvsp....DIMcvGKaltGG |
| Chain | Residue | Details |
| A | LEU251-GLY288 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | TRP64 | |
| B | GLY124 | |
| B | TYR157 | |
| B | ASP254 | |
| B | LYS283 | |
| B | GLY316 | |
| B | PRO317 | |
| B | ARG400 | |
| A | GLY124 | |
| A | TYR157 | |
| A | ASP254 | |
| A | LYS283 | |
| A | GLY316 | |
| A | PRO317 | |
| A | ARG400 | |
| B | TRP64 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR25 | |
| B | TYR25 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS283 | |
| B | LYS283 | |
