Aminotransferase, class-II, pyridoxal-phosphate binding site

Definition

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 ([ec:2.3.1.50]), Histidinol-phosphate aminotransferase ([ec:2.6.1.9]), Glycine acetyltransferase [ec:2.3.1.29]), 5-aminolevulinic acid synthase ([ec:2.3.1.37]) and 8-amino-7-oxononanoate synthase ([ec:2.3.1.47]). The crystal structures of a number of the aminotransferases have been determined including the structure of l-histidinol phosphate aminotransferase from Escherichia coli (HisC) PMID:11518529. HisC is a dimeric enzyme with a mass of approximately 80kDa. Like most pyridoxal-5'-phosphate (PLP)-dependent enzymes, each HisC monomer consists of two domains, a larger PLP-binding domain having an α/β/α 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.

5 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (5 proteins: gene, accession, name)

• ALAS1
• ALAS2
• GCAT
• SPTLC2
• SPTLC3