Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | SER123 |
| A | LYS283 |
| A | HOH455 |
| A | HOH525 |
| A | HOH543 |
| A | HOH582 |
| B | PRO317 |
| B | THR318 |
| B | HOH465 |
| A | GLY124 |
| A | SER125 |
| A | TYR157 |
| A | HIS158 |
| A | GLU220 |
| A | ASP254 |
| A | ILE256 |
| A | ALA257 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SFG A 600 |
| Chain | Residue |
| A | TRP64 |
| A | TYR157 |
| A | ALA226 |
| A | ARG400 |
| A | PRO401 |
| A | PHE402 |
| A | HOH455 |
| A | HOH591 |
| B | GLY316 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP B 502 |
| Chain | Residue |
| A | PRO317 |
| A | THR318 |
| A | HOH443 |
| B | TRP65 |
| B | GLY124 |
| B | SER125 |
| B | TYR157 |
| B | HIS158 |
| B | GLU220 |
| B | ASP254 |
| B | ILE256 |
| B | ALA257 |
| B | LYS283 |
| B | HOH446 |
| B | HOH455 |
| B | HOH456 |
| B | HOH506 |
| B | HOH555 |
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
| Chain | Residue | Details |
| A | TRP64 | |
| A | TYR157 | |
| A | GLY316 | |
| B | TRP64 | |
| B | TYR157 | |
| B | GLY316 | |
| Chain | Residue | Details |
| A | GLY124 | |
| A | ASP254 | |
| A | LYS283 | |
| A | PRO317 | |
| B | GLY124 | |
| B | ASP254 | |
| B | LYS283 | |
| B | PRO317 | |
| Chain | Residue | Details |
| A | ARG400 | |
| B | ARG400 | |
| site_id | SWS_FT_FI4 |
| 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:0000305|PubMed:20565114 |
| Chain | Residue | Details |
| A | TYR25 | |
| B | TYR25 | |
| Chain | Residue | Details |
| A | LYS283 | |
| B | LYS283 | |
