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IPR011334 is a UDP-3-O-acyl N-acetylglucosamine deacetylase, C-terminal.
<p>This superfamily represents the C-terminal domain.</p> <p>UDP-3-O-N-acetylglucosamine deacetylases are zinc-dependent metalloamidases that catalyse the second and committed step in the biosynthesis of lipid A. Lipid A anchors lipopolysaccharide (the major constituent of the outer membrane) into the membrane in Gram-negative bacteria. LpxC shows no homology to mammalian metalloamidases and is essential for cell viability, making it an important target for the development of novel antibacterial compounds [[cite:PUB00032543]]. The structure of UDP-3-O-N-acetylglucosamine deacetylase (LpxC) from Aquifex aeolicus has a two-layer α/β structure similar to that of the second domain of ribosomal protein S5, only in LpxC there is a duplication giving two structural repeats of this fold, each repeat being elaborated with additional structures forming the active site. LpxC contains a zinc-binding motif, which resides at the base of an active site cleft and adjacent to a hydrophobic tunnel occupied by a fatty acid [[cite:PUB00029703]]. This tunnel accounts for the specificity of LpxC toward substrates and inhibitors bearing appropriately positioned 3-O-fatty acid substituents [[cite:PUB00035690]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity | Catalysis of the removal of an acetyl group from the 2-N position of glucosamine in the lipid A precursor UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. | ||
| Biological process | Lipid A biosynthetic process | The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: probable UDP-3-O-[3]-hydroxymyristoyl] gi|502123766|ref|XP_004498250.1| | 10 | ||
| – | UDP-3-O-acyl N-acetylglucosamine deacetylase; TAIR: AT1G24793.1 UDP-3-O-acyl N-acetylglycosamine deacetylase family protein; Swiss-Prot: sp|F4IAT8|LPXC1_ARATH Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 1; TrEMBL-Plants: tr|I1JDH4|I1JDH4_SOYBN Uncharacterized protein; Found in the gene: LotjaGi2g1v0071800 | 11 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| TIGR00325 | TIGRFAM | 1 | 50.00 |