AC   MF_00575;
DC   Protein; auto
TR   HAMAP; MF_00575; -; 1; level=0
XX
Names: LpxH
XX
ID   LPXH
DE   RecName: Full=UDP-2,3-diacylglucosamine hydrolase;
DE            EC=3.6.1.54;
DE   AltName: Full=UDP-2,3-diacylglucosamine diphosphatase;
GN   Name=lpxH;
XX
CC   -!- FUNCTION: Hydrolyzes the pyrophosphate bond of UDP-2,3-
CC       diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X)
CC       and UMP by catalyzing the attack of water at the alpha-P atom. Involved
CC       in the biosynthesis of lipid A, a phosphorylated glycolipid that
CC       anchors the lipopolysaccharide to the outer membrane of the cell.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC         glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-
CC         glucosaminyl 1-phosphate + 2 H(+) + UMP; Xref=Rhea:RHEA:25213,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:57957, ChEBI:CHEBI:78847; EC=3.6.1.54;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Binds 2 Mn(2+) ions per subunit in a binuclear metal center
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 4/6.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC       Cytoplasmic side.
CC   -!- SIMILARITY: Belongs to the LpxH family.
XX
DR   Pfam; PF00149; Metallophos; 1; trigger=no
DR   Pfam; PF12850; Metallophos_2; 1; trigger=no
DR   NCBIfam; TIGR01854; Lipid_A_lpxH; 1; trigger=no
XX
KW   Cell inner membrane
KW   Cell membrane
KW   Hydrolase
KW   Lipid A biosynthesis
KW   Lipid biosynthesis
KW   Lipid metabolism
KW   Manganese
KW   Membrane
KW   Metal-binding
XX
GO   GO:0008758; F:UDP-2,3-diacylglucosamine hydrolase activity
GO   GO:0030145; F:manganese ion binding
GO   GO:0009245; P:lipid A biosynthetic process
GO   GO:0019897; C:extrinsic component of plasma membrane
XX
FT   From: LPXH_PSEAE (Q9I2V0)
FT   BINDING         79..80
FT                   /ligand="substrate"
FT   Condition: N-[RH]
FT   BINDING         8
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         10
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         41
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         41
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         79
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: N
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT   Condition: H
FT   BINDING         197
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         122
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         160
FT                   /ligand="substrate"
FT   Optional; Condition: S
FT   BINDING         164
FT                   /ligand="substrate"
FT   Optional; Condition: [TKNQED]
FT   BINDING         167
FT                   /ligand="substrate"
FT   Optional; Condition: [KRQN]
FT   BINDING         195
FT                   /ligand="substrate"
FT   Condition: H
XX
Size: 234-268;
Related: None;
Template: P43341; P44046; Q9I2V0;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: This step in lipid A biosynthesis is carried out by LpxH in beta- and gammaproteobacteria,
 by LpxI in alphaproteobacteria, and by LpxG in Chlamydiota.
 LpxH and LpxG are unique members of the metal-dependent calcineurin-like phosphoesterase (CLP) family,
 although they share limited sequence similarity. LpxI, on the other hand, is structurally and mechanistically
 unrelated to LpxH and LpxG. LpxI uses water to attack the beta-phosphate, whereas LpxH and LpxG use water
 to attack the alpha-phosphate on the common UDP-DAGn substrate.
 Among these three enzymes, LpxH is most widespread, functioning in ~70% of Gram-negative bacteria and
 the vast majority of Gram-negative pathogens. (from PubMed:27780190)
 Possible wrong start in RALN1
XX
# Revision 1.32 2023/11/28
//