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 | 16 |
Details | binding site for residue PLP A 501 |
Chain | Residue |
A | GLY124 |
A | LYS283 |
A | HOH669 |
A | HOH693 |
A | HOH764 |
B | PRO317 |
B | THR318 |
B | HOH713 |
A | SER125 |
A | TYR157 |
A | HIS158 |
A | GLY159 |
A | GLU220 |
A | ASP254 |
A | ILE256 |
A | ALA257 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue 3VW A 502 |
Chain | Residue |
A | TYR25 |
A | TRP64 |
A | TRP65 |
A | GLY225 |
A | ALA226 |
A | MET229 |
A | LYS283 |
A | PHE402 |
A | TYR407 |
A | HOH693 |
B | GLY316 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue EPE A 503 |
Chain | Residue |
A | TYR25 |
A | SER26 |
A | SER27 |
A | GLU31 |
A | TRP64 |
A | ARG400 |
A | HOH699 |
A | HOH710 |
A | HOH806 |
A | HOH840 |
A | HOH872 |
B | GLY93 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | HIS271 |
A | ALA272 |
A | HOH635 |
B | ARG246 |
B | TYR247 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue 3VW B 501 |
Chain | Residue |
A | GLY316 |
B | TYR25 |
B | TRP64 |
B | TRP65 |
B | ALA226 |
B | LYS283 |
B | PHE402 |
B | TYR407 |
B | HOH712 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue EPE B 503 |
Chain | Residue |
A | GLY93 |
B | PRO24 |
B | TYR25 |
B | SER26 |
B | GLU31 |
B | TRP64 |
B | ARG400 |
B | HOH722 |
B | HOH734 |
B | HOH735 |
B | HOH762 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue ACN B 504 |
Chain | Residue |
B | TYR138 |
B | TRP139 |
B | VAL249 |
B | LEU250 |
B | HOH746 |
B | HOH794 |
B | HOH833 |
site_id | AC8 |
Number of Residues | 24 |
Details | binding site for Di-peptide PLP B 502 and LYS B 283 |
Chain | Residue |
A | PRO317 |
A | THR318 |
A | PHE319 |
A | HOH668 |
A | HOH698 |
B | TRP64 |
B | TRP65 |
B | THR66 |
B | GLY124 |
B | SER125 |
B | TYR157 |
B | HIS158 |
B | GLU220 |
B | ASP254 |
B | ILE256 |
B | ALA257 |
B | GLY282 |
B | ALA284 |
B | LEU285 |
B | 3VW501 |
B | HOH689 |
B | HOH712 |
B | HOH716 |
B | HOH730 |
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 | |