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 | 14 |
Details | BINDING SITE FOR RESIDUE PLP A 501 |
Chain | Residue |
A | GLY124 |
A | HOH466 |
A | HOH574 |
B | PRO317 |
B | THR318 |
B | HOH567 |
A | SER125 |
A | TYR157 |
A | HIS158 |
A | GLU220 |
A | ASP254 |
A | ILE256 |
A | ALA257 |
A | LYS283 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP B 501 |
Chain | Residue |
A | PRO317 |
A | THR318 |
A | HOH462 |
B | GLY124 |
B | SER125 |
B | TYR157 |
B | HIS158 |
B | GLY159 |
B | GLU220 |
B | ASP254 |
B | ILE256 |
B | ALA257 |
B | LYS283 |
B | HOH469 |
B | HOH515 |
B | HOH682 |
B | HOH769 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 438 |
Chain | Residue |
A | TYR25 |
A | TRP64 |
A | ARG400 |
A | HOH672 |
A | HOH849 |
B | GLY93 |
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 | GLY316 | |
B | TRP64 | |
A | TRP64 | |
A | TYR157 | |
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 | |