Aminotransferase class IV (IPR001544)

Short name: Aminotrans_IV

Overlapping homologous superfamilies

Family relationships


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 [PMID: 1644759] into subfamilies.

One of these, called class-IV, currently consists of proteins of about 270 to 415 amino-acid residues that share a few regions of sequence similarity. Surprisingly, the best conserved region does not include the lysine residue to which the pyridoxal-phosphate group is known to be attached, in ilvE, but is located some 40 residues at the C terminus side of the pyridoxal-phosphate-lysine. The D-amino acid transferases (D-AAT), which are among the members of this entry, are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity [PMID: 7626635, PMID: 9163511].

This group also includes transaminase htyB from Aspergillus rugulosus, which is one of the enzymes required for the biosynthesis of the antifungal agent echinocandin B. HtyB catalyses the production of L-homotyrosine from the intermediate 2-oxo-4-(4-hydroxybenzyl)butanoic acid [PMID: 22998630]. Also included in this group is branched-chain amino acid aminotransferase gloG from the yeast Glarea lozoyensis, which is required for biosynthesis of the mycotoxin pneumocandin, also a lipohexapeptide of the echinocandin family [PMID: 27705900].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0003824 catalytic activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.