Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006523 | biological_process | alanine biosynthetic process |
A | 0006531 | biological_process | aspartate metabolic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009058 | biological_process | biosynthetic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0047688 | molecular_function | aspartate 4-decarboxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP A 900 |
Chain | Residue |
A | ARG37 |
A | TYR289 |
A | SER312 |
A | LYS315 |
A | ARG323 |
A | TYR134 |
A | GLY173 |
A | GLY174 |
A | THR175 |
A | PHE204 |
A | TYR207 |
A | ASN256 |
A | ASP286 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKyfGAtGWRLG |
Chain | Residue | Details |
A | SER312-GLY325 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY115 | |
A | ASN256 | |
A | ARG497 | |
Chain | Residue | Details |
A | LYS315 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | PHE204 | |
A | ASP286 | |
A | LYS315 | |