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Protein

UDP-2,3-diacylglucosamine hydrolase

Gene

lpxH

Organism
Pseudomonas entomophila (strain L48)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.UniRule annotation

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 annotation

Cofactori

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

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 annotation
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. no protein annotated in this organism
  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 bindingi7Manganese 1UniRule annotation1
Metal bindingi9Manganese 1; via tele nitrogenUniRule annotation1
Metal bindingi40Manganese 1UniRule annotation1
Metal bindingi40Manganese 2UniRule annotation1
Metal bindingi78Manganese 2UniRule annotation1
Metal bindingi113Manganese 2; via tele nitrogenUniRule annotation1
Binding sitei121SubstrateUniRule annotation1
Binding sitei159SubstrateUniRule annotation1
Binding sitei163SubstrateUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Metal bindingi194Manganese 2; via pros nitrogenUniRule annotation1
Binding sitei194Substrate; via tele nitrogenUniRule annotation1
Metal bindingi196Manganese 1; via tele nitrogenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

UniPathwayiUPA00359; UER00480.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-2,3-diacylglucosamine hydrolaseUniRule annotation (EC:3.6.1.54UniRule annotation)
Alternative name(s):
UDP-2,3-diacylglucosamine diphosphataseUniRule annotation
Gene namesi
Name:lpxHUniRule annotation
Ordered Locus Names:PSEEN2084
OrganismiPseudomonas entomophila (strain L48)
Taxonomic identifieri384676 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000000658 Componenti: Chromosome

Subcellular locationi

Q1IBQ2:
  • Cell inner membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000250701 – 240UDP-2,3-diacylglucosamine hydrolaseAdd BLAST240

Interactioni

Protein-protein interaction databases

STRINGi384676.PSEEN2084.

Structurei

3D structure databases

ProteinModelPortaliQ1IBQ2.
SMRiQ1IBQ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni78 – 79Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the LpxH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105F10. Bacteria.
COG2908. LUCA.
HOGENOMiHOG000261930.
KOiK03269.
OMAiFDFWFEY.
OrthoDBiPOG091H064W.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
HAMAPiMF_00575. LpxH. 1 hit.
InterProiView protein in InterPro
IPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR010138. UDP-diacylglucosamine_Hdrlase.
PANTHERiPTHR34990:SF1. PTHR34990:SF1. 1 hit.
PfamiView protein in Pfam
PF00149. Metallophos. 1 hit.
SUPFAMiSSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR01854. lipid_A_lpxH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1IBQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILLISDLHL QEERPDITRA FLDLLDGRAR HAKALYILGD FFEAWIGDDA
60 70 80 90 100
MTPFQRSICQ ALRQLSDSGT TIYLMHGNRD FLIGQAFCQA AGCTLLDDPS
110 120 130 140 150
VIELGGEAVL LMHGDTLCTR DVGYMKLRRY LRNPLSLWIL RHLPLSTRQK
160 170 180 190 200
LARKLRSESK SQTRMKNTEI VDVTPDEVPK VMAAHGVRTL VHGHTHRPAI
210 220 230 240
HKLVIDGQPA RRIVLGDWDR RGWALQVDEQ GFQLAPFEFS
Length:240
Mass (Da):27,262
Last modified:June 13, 2006 - v1
Checksum:i1FC9129A115F4445
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT573326 Genomic DNA. Translation: CAK14913.1.
RefSeqiWP_011533316.1. NC_008027.1.

Genome annotation databases

EnsemblBacteriaiCAK14913; CAK14913; PSEEN2084.
GeneIDi32805292.
KEGGipen:PSEEN2084.

Similar proteinsi

Entry informationi

Entry nameiLPXH_PSEE4
AccessioniPrimary (citable) accession number: Q1IBQ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 13, 2006
Last modified: October 25, 2017
This is version 77 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families