| Type: | Binding_site | Name: | Aminotransferase, class-II, pyridoxal-phosphate binding site |
| Description: | Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped into subfamilies. One of these, is called class-II. It consists of Serine palmitoyltransferase (), Histidinol-phosphate aminotransferase (), Glycine acetyltransferase ), 5-aminolevulinic acid synthase () and 8-amino-7-oxononanoate synthase ().The crystal structures of a number of the aminotransferases have been determined including the structure of l-histidinol phosphate aminotransferase from Escherichia coli(HisC) []. HisC is a dimeric enzyme with a mass of approximately 80 kDa. Like most pyridoxal-5'-phosphate (PLP)-dependent enzymes, each HisC monomer consists of two domains, a larger PLP-binding domain having an alpha/beta/alpha topology, and a smaller domain. The N-terminal arm contributes to the dimerization of the two monomers. The PLP-binding domain of HisC shows weak sequence similarity, but significant structural similarity with the PLP-binding domains of a number of PLP-dependent enzymes. | Short Name: | Aminotrans_II_pyridoxalP_BS |
| DB identifier | Type | Name |
|---|---|---|
| IPR005861 | Family | Histidinol-phosphate aminotransferase family |
| IPR015424 | Domain | Pyridoxal phosphate-dependent transferase |
| IPR015421 | Domain | Pyridoxal phosphate-dependent transferase, major region, subdomain 1 |
| IPR004839 | Domain | Aminotransferase, class I/classII |
| IPR010961 | Domain | Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase |
