HAMAP logo

HAMAP rule MF_00575

Send feedback

General rule information [?]

Accession MF_00575
Dates 31-JUL-2002 (Created)
17-FEB-2023 (Last updated, Version 30)
Name LpxH
Bacteria; Pseudomonadota
Templates P43341 (LPXH_ECOLI); P44046 (LPXH_HAEIN); Q9I2V0 (LPXH_PSEAE): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=UDP-2,3-diacylglucosamine hydrolase;
AltName: Full=UDP-2,3-diacylglucosamine diphosphatase;
Gene name

Comments [?]

Function Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic activity RHEA:25213: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Cofactor Mn(2+)
Note: Binds 2 Mn(2+) ions per subunit in a binuclear metal center
Pathway Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Subcellular location Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Similarity Belongs to the LpxH family.

Keywords [?]

Gene Ontology [?]

GO:0008758; Molecular function: UDP-2,3-diacylglucosamine hydrolase activity.
GO:0030145; Molecular function: manganese ion binding.
GO:0009245; Biological process: lipid A biosynthetic process.
GO:0019897; Cellular component: extrinsic component of plasma membrane.

Cross-references [?]

Pfam PF00149; Metallophos; 1;
PF12850; Metallophos_2; 1;
TIGRFAMs TIGR01854; Lipid_A_lpxH; 1;

Features [?]

Key     From     To       Description   Tag   Condition   FTGroup
BINDING     79     80       /ligand="substrate     N-[RH]  
BINDING     8     8       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     D  
BINDING     10     10       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     H  
BINDING     41     41       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     D  
BINDING     41     41       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     D  
BINDING     79     79       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     N  
BINDING     114     114       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     H  
BINDING     195     195       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="2     H  
BINDING     197     197       /ligand="Mn(2+)" /ligand_id="ChEBI:CHEBI:29035" /ligand_label="1     H  
BINDING     122     122       /ligand="substrate     D  
BINDING (Optional)     160     160       /ligand="substrate     S  
BINDING (Optional)     164     164       /ligand="substrate     [TKNQED]  
BINDING (Optional)     167     167       /ligand="substrate     [KRQN]  
BINDING     195     195       /ligand="substrate     H  

Additional information [?]

Size range 234-268 amino acids
Related rules None
Fusion 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 RALSO