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 | 19 |
Details | BINDING SITE FOR RESIDUE PLP A 501 |
Chain | Residue |
A | TRP65 |
A | ALA257 |
A | LYS283 |
A | KAP502 |
A | HOH2104 |
A | HOH2105 |
A | HOH2107 |
A | HOH2196 |
B | GLY316 |
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 | 12 |
Details | BINDING SITE FOR RESIDUE KAP A 502 |
Chain | Residue |
A | TYR25 |
A | TRP64 |
A | TYR157 |
A | ALA226 |
A | LYS283 |
A | ARG400 |
A | PLP501 |
A | HOH2032 |
A | HOH2291 |
A | HOH2305 |
B | GLY316 |
B | THR318 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG A 503 |
Chain | Residue |
A | ARG193 |
A | HIS232 |
A | PRO234 |
A | HOH2306 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | VAL181 |
A | HOH2307 |
A | HOH2308 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | SER34 |
A | PRO35 |
A | VAL36 |
A | HOH2016 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PLP B 501 |
Chain | Residue |
A | PRO317 |
A | THR318 |
A | HOH2103 |
A | HOH2232 |
B | TRP65 |
B | GLY124 |
B | SER125 |
B | TYR157 |
B | HIS158 |
B | GLY159 |
B | GLU220 |
B | ASP254 |
B | ILE256 |
B | ALA257 |
B | LYS283 |
B | KAP502 |
B | HOH2070 |
B | HOH2138 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE KAP B 502 |
Chain | Residue |
A | GLY316 |
A | THR318 |
B | TYR25 |
B | TRP64 |
B | TYR157 |
B | ALA226 |
B | LYS283 |
B | ARG400 |
B | PLP501 |
B | HOH2028 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG B 503 |
Chain | Residue |
B | VAL222 |
B | HIS232 |
B | HOH2216 |
B | HOH2217 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 504 |
Chain | Residue |
A | HOH2137 |
A | HOH2308 |
B | VAL181 |
B | HOH2218 |
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 | |