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 | SER123 |
| A | ALA257 |
| A | LYS283 |
| A | HOH629 |
| A | HOH665 |
| A | HOH681 |
| A | HOH688 |
| A | HOH694 |
| B | PRO317 |
| B | THR318 |
| A | GLY124 |
| A | SER125 |
| A | TYR157 |
| A | HIS158 |
| A | GLY159 |
| A | GLU220 |
| A | ASP254 |
| A | ILE256 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue 6SQ B 501 |
| Chain | Residue |
| A | MET91 |
| A | PHE92 |
| A | GLY93 |
| A | GLY316 |
| A | THR318 |
| B | TYR25 |
| B | TRP64 |
| B | GLY156 |
| B | TYR157 |
| B | ASP169 |
| B | GLY172 |
| B | GLY173 |
| B | ALA226 |
| B | ARG403 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide PLP B 502 and LYS B 283 |
| Chain | Residue |
| A | THR318 |
| A | HOH626 |
| B | TRP64 |
| B | TRP65 |
| B | THR66 |
| B | SER123 |
| B | GLY124 |
| B | SER125 |
| B | TYR157 |
| B | HIS158 |
| B | GLU220 |
| B | ASP254 |
| B | ILE256 |
| B | ALA257 |
| B | GLY282 |
| B | ALA284 |
| B | LEU285 |
| B | HOH662 |
| B | HOH680 |
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":[{"source":"HAMAP-Rule","id":"MF_00834","evidenceCode":"ECO:0000255"}]} |
| 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":[{"source":"HAMAP-Rule","id":"MF_00834","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00834","evidenceCode":"ECO:0000255"}]} |
