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 | 18 |
Details | BINDING SITE FOR RESIDUE 2B9 A 501 |
Chain | Residue |
A | TYR25 |
A | ILE256 |
A | LYS283 |
A | HOH622 |
A | HOH644 |
A | HOH667 |
B | GLY316 |
B | PRO317 |
B | THR318 |
B | HOH631 |
A | TRP64 |
A | SER123 |
A | GLY124 |
A | SER125 |
A | TYR157 |
A | HIS158 |
A | GLY159 |
A | ASP254 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 502 |
Chain | Residue |
A | ARG193 |
A | PHE231 |
A | ASP367 |
A | ARG369 |
A | HOH656 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | VAL108 |
A | ASP109 |
A | THR111 |
A | ALA113 |
A | HOH688 |
A | HOH740 |
B | ARG235 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 2B9 B 501 |
Chain | Residue |
A | GLY316 |
A | PRO317 |
A | THR318 |
A | HOH603 |
B | TRP64 |
B | GLY124 |
B | SER125 |
B | TYR157 |
B | HIS158 |
B | GLY159 |
B | ASP254 |
B | ILE256 |
B | LYS283 |
B | HOH609 |
B | HOH648 |
B | HOH655 |
B | HOH761 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 502 |
Chain | Residue |
A | ARG235 |
A | HIS271 |
A | ALA272 |
A | HOH712 |
B | ARG246 |
B | TYR247 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 503 |
Chain | Residue |
A | LEU144 |
A | GLY212 |
A | HOH636 |
B | ARG154 |
B | PRO189 |
B | HOH616 |
B | HOH644 |
B | HOH749 |
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 |
B | TYR157 | |
B | GLY316 | |
A | TYR157 | |
A | GLY316 | |
B | TRP64 | |
A | TRP64 | |
Chain | Residue | Details |
A | LYS283 | |
A | PRO317 | |
B | GLY124 | |
B | ASP254 | |
B | LYS283 | |
B | PRO317 | |
A | GLY124 | |
A | ASP254 | |
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 | |