Domain

Trimeric LpxA-like (IPR011004)

Short name: Trimer_LpxA-like

Domain relationships

None.

Description

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, EC:2.3.1.129) from Escherichia coli, the first enzyme in the lipid A biosynthetic pathway [PMID: 7481807]; galactoside acetyltransferase (GAT, LacA, EC:2.3.1.18) from E. coli, a gene product of the lac operon that may assist cellular detoxification [PMID: 11937062]; gamma-class Archaeon carbonic anhydrase (EC:4.2.1.1), a zinc-containing enzyme that catalyses the reversible hydration of carbon dioxide [PMID: 10924115]; tetrahydrodipicolinate-N-succinlytransferase (DapD) from Mycobacterium bovis, an enzyme from the lysine biosynthetic pathway that contains an extra N-terminal 3-helical domain [PMID: 11910040]; and the C-terminal domain of N-acetylglucosamine 1-phosphate uridyltransferase (GlmU, EC: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 [PMID: 11329257].

Contributing signatures

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