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Annotation rule MF_00575
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General rule information [?]

Accession MF_00575
Dates 31-JUL-2002 (Created)
18-NOV-2019 (Last updated, Version 24)
Name LpxH
Scope
Bacteria; Proteobacteria
Templates P43341 (LPXH_ECOLI); P44046 (LPXH_HAEIN); Q9I2V0 (LPXH_PSEAE): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
LPXH
Protein name
RecName: Full=UDP-2,3-diacylglucosamine hydrolase;
EC 3.6.1.54;
AltName: Full=UDP-2,3-diacylglucosamine diphosphatase;
Gene name
lpxH

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(3-hydroxytetradecanoyl)-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
EC 3.6.1.54
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 [?]

Cell inner membrane
Cell membrane
Hydrolase
Lipid A biosynthesis
Lipid biosynthesis
Lipid metabolism
Manganese
Membrane
Metal-binding

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 [?]

From: LPXH_PSEAE (Q9I2V0)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     79     80       Substrate binding     N-[RH]  
METAL     8     8       Manganese 1     D  
METAL     10     10       Manganese 1; via tele nitrogen     H  
METAL     41     41       Manganese 1     D  
METAL     41     41       Manganese 2     D  
METAL     79     79       Manganese 2     N  
METAL     114     114       Manganese 2; via tele nitrogen     H  
METAL     195     195       Manganese 2; via pros nitrogen     H  
METAL     197     197       Manganese 1; via tele nitrogen     H  
BINDING     122     122       Substrate     D  
BINDING (Optional)     160     160       Substrate     S  
BINDING (Optional)     164     164       Substrate     [TKNQED]  
BINDING (Optional)     167     167       Substrate     [KRQN]  
BINDING     195     195       Substrate; via tele nitrogen     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 Chlamydiae. 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


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