AC MF_00388; DC Protein; auto TR HAMAP; MF_00388; -; 1; level=0 XX Names: LpxC XX ID LPXC DE RecName: Full=UDP-3-O-acyl-N-acetylglucosamine deacetylase; DE Short=UDP-3-O-acyl-GlcNAc deacetylase; DE EC=3.5.1.108; DE AltName: Full=UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase; GN Name=lpxC; XX case CC -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- CC acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the CC committed step in lipid A biosynthesis. end case case CC -!- FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- CC acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate. CC Involved in the biosynthesis of lipid A, a phosphorylated glycolipid CC that in bacteria anchors the lipopolysaccharide to the outer membrane CC of the cell. The target for the lipopolysaccharides produced in the CC chloroplast could either be the cell envelope of the eukaryote or the CC plastid membrane. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + CC H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate; CC Xref=Rhea:RHEA:67816, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:137740, ChEBI:CHEBI:173225; EC=3.5.1.108; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N- CC acetyl-alpha-D-glucosamine: step 2/6. case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the LpxC family. XX DR Pfam; PF03331; LpxC; 1; trigger=no DR NCBIfam; TIGR00325; lpxC; 1; trigger=no XX KW Hydrolase KW Lipid A biosynthesis KW Lipid biosynthesis KW Lipid metabolism KW Metal-binding KW Zinc XX GO GO:0008759; F:UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity GO GO:0009245; P:lipid A biosynthetic process case GO GO:0009507; C:chloroplast end case XX FT From: LPXC_ECOLI (P0A725) FT ACT_SITE 265 FT /note="Proton donor" FT Condition: H FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: H FT BINDING 238 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: H FT BINDING 242 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: D XX Size: 250-350; Related: None; Template: P0A725; O67648; P47205; Scope: Bacteria Plastid Fusion: Nter: None Cter: MF_00406 (fabZ) Duplicate: None Plasmid: None Comments: None XX # Revision 1.32 2023/06/01 //