1C7G
TYROSINE PHENOL-LYASE FROM ERWINIA HERBICOLA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006570 | biological_process | tyrosine metabolic process |
| A | 0009072 | biological_process | aromatic amino acid metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0050371 | molecular_function | tyrosine phenol-lyase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006570 | biological_process | tyrosine metabolic process |
| B | 0009072 | biological_process | aromatic amino acid metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0050371 | molecular_function | tyrosine phenol-lyase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006570 | biological_process | tyrosine metabolic process |
| C | 0009072 | biological_process | aromatic amino acid metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0050371 | molecular_function | tyrosine phenol-lyase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006570 | biological_process | tyrosine metabolic process |
| D | 0009072 | biological_process | aromatic amino acid metabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0050371 | molecular_function | tyrosine phenol-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP A 1000 |
| Chain | Residue |
| A | GLN98 |
| A | LYS257 |
| A | HOH543 |
| A | HOH682 |
| A | GLY99 |
| A | ARG100 |
| A | GLU103 |
| A | PHE123 |
| A | ASP214 |
| A | THR216 |
| A | ARG217 |
| A | SER254 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP B 1000 |
| Chain | Residue |
| B | GLN98 |
| B | GLY99 |
| B | ARG100 |
| B | GLU103 |
| B | PHE123 |
| B | ASP214 |
| B | THR216 |
| B | ARG217 |
| B | SER254 |
| B | LYS257 |
| B | HOH554 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP C 1000 |
| Chain | Residue |
| C | GLN98 |
| C | GLY99 |
| C | ARG100 |
| C | GLU103 |
| C | PHE123 |
| C | ASP214 |
| C | THR216 |
| C | ARG217 |
| C | SER254 |
| C | LYS257 |
| C | HOH767 |
| C | HOH811 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP D 1000 |
| Chain | Residue |
| D | GLN98 |
| D | GLY99 |
| D | ARG100 |
| D | GLU103 |
| D | PHE123 |
| D | ASP214 |
| D | THR216 |
| D | ARG217 |
| D | SER254 |
| D | LYS257 |
| D | HOH920 |
Functional Information from PROSITE/UniProt
| site_id | PS00853 |
| Number of Residues | 19 |
| Details | BETA_ELIM_LYASE Beta-eliminating lyases pyridoxal-phosphate attachment site. YaDgctMSGKKDcLVnIGG |
| Chain | Residue | Details |
| A | TYR247-GLY265 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS257 | |
| B | LYS257 | |
| C | LYS257 | |
| D | LYS257 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | TYR122 | |
| A | ASP214 |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | TYR71 | |
| B | ARG381 | |
| B | PHE123 | |
| B | ASP214 |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | TYR71 | |
| C | ARG381 | |
| C | PHE123 | |
| C | ASP214 |
| site_id | CSA12 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | TYR71 | |
| D | ARG381 | |
| D | PHE123 | |
| D | ASP214 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | ASP214 | |
| A | LYS256 | |
| A | PHE128 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | ASP214 | |
| B | LYS256 | |
| B | PHE128 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | ASP214 | |
| C | LYS256 | |
| C | PHE128 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | ASP214 | |
| D | LYS256 | |
| D | PHE128 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | TYR122 | |
| D | ASP214 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | TYR122 | |
| C | ASP214 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | TYR122 | |
| B | ASP214 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | PHE123 | |
| A | ASP214 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| B | PHE123 | |
| B | ASP214 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| C | PHE123 | |
| C | ASP214 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| D | PHE123 | |
| D | ASP214 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ax4 |
| Chain | Residue | Details |
| A | TYR71 | |
| A | ARG381 | |
| A | PHE123 | |
| A | ASP214 |
