Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0009693 | biological_process | ethylene biosynthetic process |
A | 0009835 | biological_process | fruit ripening |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016847 | molecular_function | 1-aminocyclopropane-1-carboxylate synthase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042218 | biological_process | 1-aminocyclopropane-1-carboxylate biosynthetic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0009693 | biological_process | ethylene biosynthetic process |
B | 0009835 | biological_process | fruit ripening |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016847 | molecular_function | 1-aminocyclopropane-1-carboxylate synthase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0042218 | biological_process | 1-aminocyclopropane-1-carboxylate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP A 500 |
Chain | Residue |
A | GLY119 |
A | ALA120 |
A | THR121 |
A | TYR145 |
A | ASN202 |
A | ASP230 |
A | ILE232 |
A | TYR233 |
A | SER270 |
A | SER272 |
A | LYS273 |
A | ARG281 |
A | HOH521 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP B 500 |
Chain | Residue |
B | GLY119 |
B | ALA120 |
B | THR121 |
B | TYR145 |
B | ASN202 |
B | ILE232 |
B | TYR233 |
B | SER270 |
B | SER272 |
B | LYS273 |
B | ARG281 |
B | HOH527 |
site_id | ACT |
Number of Residues | 9 |
Details | IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT |
Chain | Residue |
B | TYR85 |
A | THR121 |
A | ASN202 |
A | ASP230 |
A | TYR233 |
A | SER270 |
A | LYS273 |
A | ARG281 |
A | ARG407 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKdlGLpGFRVG |
Chain | Residue | Details |
A | SER270-GLY283 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP84 | |
B | ASP84 | |
Chain | Residue | Details |
A | TYR145 | |
A | ASP151 | |
B | TYR145 | |
B | ASP151 | |
Chain | Residue | Details |
A | LYS273 | |
B | LYS273 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 418 |
Chain | Residue | Details |
A | TYR145 | activator, steric role |
A | ASP230 | electrostatic stabiliser |
A | ILE232 | steric role |
A | LYS273 | covalent catalysis, proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 418 |
Chain | Residue | Details |
B | TYR145 | activator, steric role |
B | ASP230 | electrostatic stabiliser |
B | ILE232 | steric role |
B | LYS273 | covalent catalysis, proton shuttle (general acid/base) |