AC   MF_00523;
DC   Protein; auto
TR   HAMAP; MF_00523; -; 1; level=0
XX
Names: LpxD
XX
ID   LPXD
case <OC:Enterobacterales>
DE   RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase;
DE            Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase;
DE            EC=2.3.1.191;
DE   AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase;
else
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase;
DE            EC=2.3.1.191;
end case
GN   Name=lpxD;
XX
case <OC:Enterobacterales>
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
CC       (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as
CC       the acyl donor. Is involved in the biosynthesis of lipid A, a
CC       phosphorylated glycolipid that anchors the lipopolysaccharide to the
CC       outer membrane of the cell.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-
CC         alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, ChEBI:CHEBI:137748;
CC         EC=2.3.1.191;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] + UDP-
CC         2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:17817, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:71573,
CC         ChEBI:CHEBI:78474, ChEBI:CHEBI:78847;
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 3/6.
else
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-
CC       hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of
CC       lipid A, a phosphorylated glycolipid that anchors the
CC       lipopolysaccharide to the outer membrane of the cell.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-
CC         alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, ChEBI:CHEBI:137748;
CC         EC=2.3.1.191;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
end case
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC       subfamily.
XX
DR   Pfam; PF00132; Hexapep; 6-9; trigger=no
DR   Pfam; PF04613; LpxD; 1; trigger=no
DR   NCBIfam; TIGR01853; Lipid_A_lpxD; 1; trigger=no
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1-4; trigger=no
XX
KW   Acyltransferase
KW   Lipid A biosynthesis
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Repeat
KW   Transferase
XX
GO   GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups
GO   GO:0009245; P:lipid A biosynthetic process
XX
FT   From: LPXD_ECOLI (P21645)
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT   Condition: H
XX
Size: 316-380;
Related: MF_00387;
Template: P21645; P0CD76;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in KORVE, FRAT1, FRATH, FRATO, FRATT, GLOVI, LEGPA, LEGPH, LEGPL,
 NITWN, RHOPB, SULDN
Plasmid: None
Comments: The acyl chain added by LpxD varies depending on the species since there are differences
 in the structure of lipid A between different species. See Figure 9 from PubMed=19655786, the
 acyl chain length can vary from C10 to C20.
 The acyl chain present in the UDP-glucosamine substrate also seems to vary depending on the species
 (it is UDP-3-O-(hydroxymyristoyl)glucosamine in E.coli and UDP-3-O-myristoylglucosamine in
 Chlamydia trachomatis).
XX
# Revision 1.36 2023/06/01
//