Trimeric LpxA-like <p>This domain is characterised by trimeric LpxA-like enzymes that display a single-stranded left-handed beta-helix fold, composed of tandem repeats of a hexapeptide, as represented by the Bacterial transferase hexapeptide repeat, where the hexapeptide repeats correspond to individual strands. Many bacterial transferases contain this domain. The structures of several proteins with this domain have been determined, including UDP N-acetylglucosamine acyltransferase (LpxA, <db_xref db="EC" dbkey="2.3.1.129"/>) from <taxon tax_id="562">Escherichia coli</taxon>, the first enzyme in the lipid A biosynthetic pathway [<cite idref="PUB00005215"/>]; galactoside acetyltransferase (GAT, LacA, <db_xref db="EC" dbkey="2.3.1.18"/>) from E. coli, a gene product of the lac operon that may assist cellular detoxification [<cite idref="PUB00013969"/>]; gamma-class Archaeon carbonic anhydrase (<db_xref db="EC" dbkey="4.2.1.1"/>), a zinc-containing enzyme that catalyses the reversible hydration of carbon dioxide [<cite idref="PUB00013970"/>]; tetrahydrodipicolinate-N-succinlytransferase (DapD) from <taxon tax_id="1765">Mycobacterium bovis</taxon>, an enzyme from the lysine biosynthetic pathway that contains an extra N-terminal 3-helical domain [<cite idref="PUB00013971"/>]; and the C-terminal domain of N-acetylglucosamine 1-phosphate uridyltransferase (GlmU, <db_xref db="EC" dbkey="2.7.7.23"/>) from E. coli, a trimeric bifunctional enzyme that catalyses the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine, an essential precursor for many biomolecules [<cite idref="PUB00007906"/>].</p>