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 | 0009085 | biological_process | lysine biosynthetic process |
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 | 0009085 | biological_process | lysine biosynthetic process |
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 | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | GLY113 | |
A | THR283 | |
B | GLY1113 | |
B | THR1283 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000305|Ref.2 |
Chain | Residue | Details |
A | PHE140 | |
A | ARG143 | |
A | ASP225 | |
A | THR282 | |
B | PHE1140 | |
B | ARG1143 | |
B | ASP1225 | |
B | THR1282 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_02084, ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | LYS254 | |
B | LYS1254 |
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 |