P43341 · LPXH_ECOLI
- ProteinUDP-2,3-diacylglucosamine hydrolase
- GenelpxH
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids240 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (PubMed:12000770).
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (PubMed:12000770, PubMed:12000771).
Is essential for E.coli growth (PubMed:12000771).
Does not cleave the unacylated UDP-GlcNAc, the mono-acylated UDP-3-O-(R)-3-hydroxymyristoyl-GlcNAc, and CDP-diacylglycerol (PubMed:12000770).
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (PubMed:12000770, PubMed:12000771).
Is essential for E.coli growth (PubMed:12000771).
Does not cleave the unacylated UDP-GlcNAc, the mono-acylated UDP-3-O-(R)-3-hydroxymyristoyl-GlcNAc, and CDP-diacylglycerol (PubMed:12000770).
Catalytic activity
- 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
Note: Binds 2 Mn2+ ions per subunit in a binuclear metal center.
Activity regulation
Inhibited by a sulfonyl piperazine compound that shows antibacterial activity against E.coli; LpxH is the cellular target of this compound (PubMed:25733621).
Inhibited by 0.01% (or more) Triton X-100 in vitro (PubMed:12000770).
Inhibited by 0.01% (or more) Triton X-100 in vitro (PubMed:12000770).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
61.7 μM | UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
17.2 μmol/min/mg |
Assays with partially purified enzyme.
pH Dependence
Optimum pH is 8.0.
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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 8 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 10 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 41 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 41 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 79 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 79-80 | substrate | ||||
Sequence: NR | ||||||
Binding site | 114 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 122 | substrate | ||||
Sequence: D | ||||||
Binding site | 160 | substrate | ||||
Sequence: S | ||||||
Binding site | 164 | substrate | ||||
Sequence: N | ||||||
Binding site | 167 | substrate | ||||
Sequence: K | ||||||
Binding site | 195 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 195 | substrate | ||||
Sequence: H | ||||||
Binding site | 197 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extrinsic component of plasma membrane | |
Molecular Function | manganese ion binding | |
Molecular Function | UDP-2,3-diacylglucosamine hydrolase activity | |
Biological Process | lipid A biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUDP-2,3-diacylglucosamine hydrolase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP43341
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
An insertion mutation defective in lpxH is not viable and accumulates UDP-2,3-diacylglucosamine.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000214108 | 1-240 | UDP-2,3-diacylglucosamine hydrolase | |||
Sequence: MATLFIADLHLCVEEPAITAGFLRFLAGEARKADALYILGDLFEAWIGDDDPNPLHRKMAAAIKAVSDSGVPCYFIHGNRDFLLGKRFARESGMTLLPEEKVLELYGRRVLIMHGDTLCTDDAGYQAFRAKVHKPWLQTLFLALPLFVRKRIAARMRANSKEANSSKSLAIMDVNQNAVVSAMEKHQVQWLIHGHTHRPAVHELIANQQPAFRVVLGAWHTEGSMVKVTADDVELIHFPF |
Proteomic databases
Structure
Sequence
- Sequence statusComplete
- Length240
- Mass (Da)26,894
- Last updated1997-11-01 v2
- Checksum5004A2E471B7A7E9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF311865 EMBL· GenBank· DDBJ | AAG47820.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U82664 EMBL· GenBank· DDBJ | AAB40277.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73626.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76301.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M19657 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |