Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0033014 | biological_process | tetrapyrrole biosynthetic process |
A | 0042286 | molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PMP A 431 |
Chain | Residue |
A | GLY118 |
A | GLY299 |
A | THR300 |
A | HOH474 |
A | HOH510 |
A | HOH616 |
A | HOH698 |
A | HOH705 |
A | THR119 |
A | TYR145 |
A | HIS146 |
A | GLU207 |
A | ASN212 |
A | ASP240 |
A | VAL242 |
A | LYS268 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 37 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVmt.GF.RvDyncaqgyfgvtp....DLTclGKvigGG |
Chain | Residue | Details |
A | LEU237-GLY273 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS268 | |