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Protein

UDP-2,3-diacylglucosamine hydrolase

Gene

lpxH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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.UniRule annotation2 Publications

Cofactori

Mn2+UniRule annotation1 PublicationNote: Binds 2 Mn2+ ions per subunit in a binuclear metal center.UniRule annotation

Enzyme 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
  1. KM=61.7 µM for UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine1 Publication
  1. Vmax=17.2 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

Pathwayi: lipid IV(A) biosynthesis

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 Publications
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (lpxA)
  2. UDP-3-O-acyl-N-acetylglucosamine deacetylase (lpxC)
  3. UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (lpxD)
  4. UDP-2,3-diacylglucosamine hydrolase (lpxH)
  5. Lipid-A-disaccharide synthase (lpxB)
  6. Tetraacyldisaccharide 4'-kinase (lpxK)
This subpathway is part of the pathway lipid IV(A) biosynthesis, which is itself part of Glycolipid biosynthesis.
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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi8Manganese 1UniRule annotation1
Metal bindingi10Manganese 1; via tele nitrogenUniRule annotation1
Metal bindingi41Manganese 1UniRule annotation1
Metal bindingi41Manganese 2UniRule annotation1
Metal bindingi79Manganese 2UniRule annotation1
Metal bindingi114Manganese 2; via tele nitrogenUniRule annotation1
Binding sitei122SubstrateUniRule annotation1
Binding sitei160SubstrateUniRule annotation1
Binding sitei164SubstrateUniRule annotation1
Binding sitei167SubstrateUniRule annotation1
Metal bindingi195Manganese 2; via pros nitrogenUniRule annotation1
Binding sitei195Substrate; via tele nitrogenUniRule annotation1
Metal bindingi197Manganese 1; via tele nitrogenUniRule annotation1

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • UDP-2,3-diacylglucosamine hydrolase activity Source: UniProtKB

GO - Biological processi

  • lipid A biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionHydrolase
Biological processLipid A biosynthesis, Lipid biosynthesis, Lipid metabolism
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12666-MONOMER.
MetaCyc:EG12666-MONOMER.
BRENDAi3.6.1.54. 2026.
UniPathwayiUPA00359; 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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12666. lpxH.

Subcellular locationi

  • Cell inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication
  • Cytoplasm 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

Pathology & 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 keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002141081 – 240UDP-2,3-diacylglucosamine hydrolaseAdd BLAST240

Proteomic databases

PaxDbiP43341.
PRIDEiP43341.

Interactioni

Protein-protein interaction databases

BioGridi4262817. 203 interactors.
DIPiDIP-10125N.
IntActiP43341. 20 interactors.
STRINGi316385.ECDH10B_0480.

Structurei

3D structure databases

ProteinModelPortaliP43341.
SMRiP43341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni79 – 80Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the LpxH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105F10. Bacteria.
COG2908. LUCA.
HOGENOMiHOG000261930.
InParanoidiP43341.
KOiK03269.
PhylomeDBiP43341.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
HAMAPiMF_00575. LpxH. 1 hit.
InterProiView protein in InterPro
IPR024654. Calcineurin-like_PHP_lpxH.
IPR029052. Metallo-depent_PP-like.
IPR010138. UDP-diacylglucosamine_Hdrlase.
PANTHERiPTHR34990:SF3. PTHR34990:SF3. 1 hit.
PfamiView protein in Pfam
PF12850. Metallophos_2. 1 hit.
SUPFAMiSSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR01854. lipid_A_lpxH. 1 hit.

Sequencei

Sequence statusi: Complete.

P43341-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:240
Mass (Da):26,894
Last modified:November 1, 1997 - v2
Checksum:i5004A2E471B7A7E9
GO

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.
PIRiC64784.
RefSeqiNP_415057.1. NC_000913.3.
WP_000212247.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73626; AAC73626; b0524.
BAE76301; BAE76301; BAE76301.
GeneIDi949053.
KEGGiecj:JW0513.
eco:b0524.
PATRICifig|1411691.4.peg.1754.

Similar proteinsi

Entry informationi

Entry nameiLPXH_ECOLI
AccessioniPrimary (citable) accession number: P43341
Secondary accession number(s): P77440, Q2MBQ5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: August 30, 2017
This is version 127 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families