1VEF
Acetylornithine aminotransferase from Thermus thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 513 |
| Chain | Residue |
| A | GLY113 |
| A | HOH4015 |
| A | HOH4022 |
| A | HOH4032 |
| A | HOH4077 |
| B | THR1283 |
| B | HOH4005 |
| A | THR114 |
| A | PHE140 |
| A | SER141 |
| A | GLU192 |
| A | ASP225 |
| A | ILE227 |
| A | GLN228 |
| A | LYS254 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 1513 |
| Chain | Residue |
| A | THR283 |
| A | HOH4008 |
| B | SER1112 |
| B | GLY1113 |
| B | THR1114 |
| B | PHE1140 |
| B | SER1141 |
| B | GLU1192 |
| B | ASP1225 |
| B | ILE1227 |
| B | GLN1228 |
| B | LYS1254 |
| B | HOH4019 |
| B | HOH4024 |
| B | HOH4040 |
| B | HOH4079 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDEIqt.GMgRtGkrfafehfgivp....DILtlAKalgGG |
| Chain | Residue | Details |
| A | LEU222-GLY259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02084","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_02084","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LYS254 | |
| A | PHE140 | |
| A | ASP225 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | PHE1140 | |
| B | LYS1254 | |
| B | ASP1225 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | THR95 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | THR1095 |
