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 | 0016740 | molecular_function | transferase activity |
| 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 | 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 | 3GS502 |
| A | HOH643 |
| A | HOH648 |
| A | HOH650 |
| A | HOH686 |
| A | HOH698 |
| B | PRO317 |
| B | THR318 |
| A | SER125 |
| A | TYR157 |
| A | HIS158 |
| A | GLY159 |
| A | GLU220 |
| A | ASP254 |
| A | ILE256 |
| A | ALA257 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue 3GS A 502 |
| Chain | Residue |
| A | PRO24 |
| A | TYR25 |
| A | TRP64 |
| A | TYR157 |
| A | ARG400 |
| A | PHE402 |
| A | PLP501 |
| A | HOH686 |
| B | MET91 |
| B | GLY93 |
| B | GLY316 |
| B | PRO317 |
| B | THR318 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 503 |
| Chain | Residue |
| A | HIS232 |
| A | PRO234 |
| A | HIS271 |
| A | HOH733 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue PLP B 501 |
| Chain | Residue |
| A | THR318 |
| A | HOH644 |
| B | GLY124 |
| B | SER125 |
| B | TYR157 |
| B | HIS158 |
| B | GLU220 |
| B | ASP254 |
| B | ILE256 |
| B | ALA257 |
| B | LYS283 |
| B | 3GS502 |
| B | HOH659 |
| B | HOH662 |
| B | HOH666 |
| B | HOH674 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue 3GS B 502 |
| Chain | Residue |
| A | MET91 |
| A | PHE92 |
| A | GLY93 |
| A | GLY316 |
| A | PRO317 |
| A | THR318 |
| B | PRO24 |
| B | TYR25 |
| B | TRP64 |
| B | TYR157 |
| B | ARG400 |
| B | PLP501 |
| B | HOH662 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | THR152 |
| B | TRP153 |
| B | GLY156 |
| B | HIS158 |
| B | ILE167 |
| B | VAL219 |
| B | GLU220 |
| B | GLN224 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 505 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | LEU337 |
| B | GLN339 |
| B | ASP340 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| A | HIS271 |
| B | ARG246 |
| B | TYR247 |
| B | HOH601 |
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 site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
