HAMAP rule MF_00575
General rule information
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| Accession | MF_00575 |
| Dates | 31-JUL-2002 (Created)
3-SEP-2024 (Last updated, Version 33) |
| Name | LpxH |
| Scope(s) |
Bacteria Pseudomonadota |
| Template(s) | P43341 (LPXH_ECOLI); P44046 (LPXH_HAEIN); Q9I2V0 (LPXH_PSEAE); [ Recover all ] |
| Triggered by |
HAMAP; MF_00575 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| 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 | Name=lpxH; |
Comments
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| 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 | Reaction=UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D- glucosamine + H2O = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D- glucosaminyl 1-phosphate + UMP + 2 H(+); Xref=Rhea:RHEA:25213, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57865, ChEBI:CHEBI:57957, ChEBI:CHEBI:78847; EC=3.6.1.54; |
| COFACTOR | Name=Mn(2+); Xref=ChEBI:CHEBI:29035; 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
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| Cell inner membrane |
| Cell membrane |
| Hydrolase |
| Lipid A biosynthesis |
| Lipid biosynthesis |
| Lipid metabolism |
| Manganese |
| Membrane |
| Metal-binding |
Gene Ontology
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| 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
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Features
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| From: LPXH_PSEAE (Q9I2V0) | ||||||||||||
| 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 | 160 | 160 | /ligand="substrate" | S | ||||||||
| BINDING | 164 | 164 | /ligand="substrate" | [TKNQED] | ||||||||
| BINDING | 167 | 167 | /ligand="substrate" | [KRQN] | ||||||||
| BINDING | 195 | 195 | /ligand="substrate" | H | ||||||||
Additional information
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| Size range | 234-268 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: 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 |