UniProtKB - P43341 (LPXH_ECOLI)
Protein
UDP-2,3-diacylglucosamine hydrolase
Gene
lpxH
Organism
Escherichia coli (strain K12)
Status
Functioni
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).2 Publications
Catalytic activityi
- H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine = 2-N,3-O-bis(3-hydroxytetradecanoyl)-α-D-glucosaminyl 1-phosphate + 2 H+ + UMPUniRule annotation2 PublicationsEC:3.6.1.54UniRule annotation2 Publications
Cofactori
Mn2+UniRule annotation1 PublicationNote: Binds 2 Mn2+ ions per subunit in a binuclear metal center.UniRule annotation
Activity regulationi
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).2 Publications
Kineticsi
Assays with partially purified enzyme.1 Publication
- KM=61.7 µM for UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine1 Publication
- Vmax=17.2 µmol/min/mg enzyme1 Publication
pH dependencei
Optimum pH is 8.0.1 Publication
: lipid IV(A) biosynthesis Pathwayi
This protein is involved in step 4 of the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation2 PublicationsProteins known to be involved in the 6 steps of the subpathway in this organism are:
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA), Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
- UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC), UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC)
- UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD), UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD)
- UDP-2,3-diacylglucosamine hydrolase (lpxH), UDP-2,3-diacylglucosamine hydrolase (lpxH)
- Lipid-A-disaccharide synthase (lpxB), Lipid-A-disaccharide synthase (lpxB)
- Tetraacyldisaccharide 4'-kinase (lpxK), Tetraacyldisaccharide 4'-kinase (lpxK)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine, the pathway lipid IV(A) biosynthesis and in Glycolipid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 8 | Manganese 1UniRule annotation | 1 | |
Metal bindingi | 10 | Manganese 1; via tele nitrogenUniRule annotation | 1 | |
Metal bindingi | 41 | Manganese 1UniRule annotation | 1 | |
Metal bindingi | 41 | Manganese 2UniRule annotation | 1 | |
Metal bindingi | 79 | Manganese 2UniRule annotation | 1 | |
Metal bindingi | 114 | Manganese 2; via tele nitrogenUniRule annotation | 1 | |
Binding sitei | 122 | SubstrateUniRule annotation | 1 | |
Binding sitei | 160 | SubstrateUniRule annotation | 1 | |
Binding sitei | 164 | SubstrateUniRule annotation | 1 | |
Binding sitei | 167 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 195 | Manganese 2; via pros nitrogenUniRule annotation | 1 | |
Binding sitei | 195 | Substrate; via tele nitrogenUniRule annotation | 1 | |
Metal bindingi | 197 | Manganese 1; via tele nitrogenUniRule annotation | 1 |
GO - Molecular functioni
- manganese ion binding Source: EcoCyc
- UDP-2,3-diacylglucosamine hydrolase activity Source: UniProtKB
GO - Biological processi
- lipid A biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism |
Ligand | Manganese, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG12666-MONOMER MetaCyc:EG12666-MONOMER |
BRENDAi | 3.6.1.54, 2026 |
UniPathwayi | UPA00359;UER00480 |
Names & Taxonomyi
Protein namesi | Recommended name: UDP-2,3-diacylglucosamine hydrolase1 PublicationUniRule annotation (EC:3.6.1.54UniRule annotation2 Publications)Alternative name(s): UDP-2,3-diacylglucosamine diphosphataseUniRule annotation UDP-2,3-diacylglucosamine pyrophosphatase1 Publication |
Gene namesi | Name:lpxH1 PublicationUniRule annotation Synonyms:ybbF Ordered Locus Names:b0524, JW0513 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
- Cytoplasm 1 Publication
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
- extrinsic component of cytoplasmic side of plasma membrane Source: EcoCyc
- extrinsic component of plasma membrane Source: GO_Central
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, Cytoplasm, MembranePathology & Biotechi
Disruption phenotypei
An insertion mutation defective in lpxH is not viable and accumulates UDP-2,3-diacylglucosamine.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000214108 | 1 – 240 | UDP-2,3-diacylglucosamine hydrolaseAdd BLAST | 240 |
Proteomic databases
PaxDbi | P43341 |
PRIDEi | P43341 |
Interactioni
Protein-protein interaction databases
BioGRIDi | 4262817, 215 interactors |
DIPi | DIP-10125N |
IntActi | P43341, 20 interactors |
STRINGi | 511145.b0524 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P43341 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 79 – 80 | Substrate bindingUniRule annotation | 2 |
Sequence similaritiesi
Belongs to the LpxH family.UniRule annotation
Phylogenomic databases
eggNOGi | COG2908, Bacteria |
HOGENOMi | CLU_074586_0_0_6 |
InParanoidi | P43341 |
PhylomeDBi | P43341 |
Family and domain databases
HAMAPi | MF_00575, LpxH, 1 hit |
InterProi | View protein in InterPro IPR024654, Calcineurin-like_PHP_lpxH IPR043461, LpxH-like IPR010138, UDP-diacylglucosamine_Hdrlase |
PANTHERi | PTHR34990, PTHR34990, 1 hit PTHR34990:SF1, PTHR34990:SF1, 1 hit |
Pfami | View protein in Pfam PF12850, Metallophos_2, 1 hit |
TIGRFAMsi | TIGR01854, lipid_A_lpxH, 1 hit |
i Sequence
Sequence statusi: Complete.
P43341-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MATLFIADLH LCVEEPAITA GFLRFLAGEA RKADALYILG DLFEAWIGDD
60 70 80 90 100
DPNPLHRKMA AAIKAVSDSG VPCYFIHGNR DFLLGKRFAR ESGMTLLPEE
110 120 130 140 150
KVLELYGRRV LIMHGDTLCT DDAGYQAFRA KVHKPWLQTL FLALPLFVRK
160 170 180 190 200
RIAARMRANS KEANSSKSLA IMDVNQNAVV SAMEKHQVQW LIHGHTHRPA
210 220 230 240
VHELIANQQP AFRVVLGAWH TEGSMVKVTA DDVELIHFPF
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF311865 Genomic DNA Translation: AAG47820.1 U82664 Genomic DNA Translation: AAB40277.1 U00096 Genomic DNA Translation: AAC73626.1 AP009048 Genomic DNA Translation: BAE76301.1 M19657 Genomic DNA No translation available. |
PIRi | C64784 |
RefSeqi | NP_415057.1, NC_000913.3 WP_000212247.1, NZ_SSZK01000024.1 |
Genome annotation databases
EnsemblBacteriai | AAC73626; AAC73626; b0524 BAE76301; BAE76301; BAE76301 |
GeneIDi | 949053 |
KEGGi | ecj:JW0513 eco:b0524 |
PATRICi | fig|1411691.4.peg.1754 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF311865 Genomic DNA Translation: AAG47820.1 U82664 Genomic DNA Translation: AAB40277.1 U00096 Genomic DNA Translation: AAC73626.1 AP009048 Genomic DNA Translation: BAE76301.1 M19657 Genomic DNA No translation available. |
PIRi | C64784 |
RefSeqi | NP_415057.1, NC_000913.3 WP_000212247.1, NZ_SSZK01000024.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5WLY | X-ray | 2.00 | A | 1-240 | [»] | |
SMRi | P43341 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262817, 215 interactors |
DIPi | DIP-10125N |
IntActi | P43341, 20 interactors |
STRINGi | 511145.b0524 |
Proteomic databases
PaxDbi | P43341 |
PRIDEi | P43341 |
Genome annotation databases
EnsemblBacteriai | AAC73626; AAC73626; b0524 BAE76301; BAE76301; BAE76301 |
GeneIDi | 949053 |
KEGGi | ecj:JW0513 eco:b0524 |
PATRICi | fig|1411691.4.peg.1754 |
Organism-specific databases
EchoBASEi | EB2532 |
Phylogenomic databases
eggNOGi | COG2908, Bacteria |
HOGENOMi | CLU_074586_0_0_6 |
InParanoidi | P43341 |
PhylomeDBi | P43341 |
Enzyme and pathway databases
UniPathwayi | UPA00359;UER00480 |
BioCyci | EcoCyc:EG12666-MONOMER MetaCyc:EG12666-MONOMER |
BRENDAi | 3.6.1.54, 2026 |
Miscellaneous databases
PROi | PR:P43341 |
Family and domain databases
HAMAPi | MF_00575, LpxH, 1 hit |
InterProi | View protein in InterPro IPR024654, Calcineurin-like_PHP_lpxH IPR043461, LpxH-like IPR010138, UDP-diacylglucosamine_Hdrlase |
PANTHERi | PTHR34990, PTHR34990, 1 hit PTHR34990:SF1, PTHR34990:SF1, 1 hit |
Pfami | View protein in Pfam PF12850, Metallophos_2, 1 hit |
TIGRFAMsi | TIGR01854, lipid_A_lpxH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LPXH_ECOLI | |
Accessioni | P43341Primary (citable) accession number: P43341 Secondary accession number(s): P77440, Q2MBQ5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1997 | |
Last modified: | December 2, 2020 | |
This is version 147 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families