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Protein

UDP-2,3-diacylglucosamine hydrolase

Gene

lpxH

Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
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 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

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:ECH74115_0625
OrganismiEscherichia coli O157:H7 (strain EC4115 / EHEC)
Taxonomic identifieri444450 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

Subcellular locationi

  • 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_10001295181 – 240UDP-2,3-diacylglucosamine hydrolaseAdd BLAST240

Structurei

3D structure databases

ProteinModelPortaliB5YPN9.
SMRiB5YPN9.
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

HOGENOMiHOG000261930.
KOiK03269.
OMAiFDFWFEY.

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.

B5YPN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATLFIADLH LCVEEPAITA GFLRFLAGEA RKADALYILG DLFEAWIGDD
60 70 80 90 100
DPNPLHRQMA AAIKAVSDSG VPCYFIHGNR DFLLGKRFAR ESGMTLLPEE
110 120 130 140 150
KVLELYGRRV LIMHGDTLCT DDAGYQAFRT KVHKPWLQTL FLALPLFVRK
160 170 180 190 200
RIAVRMRANS KEANSSKSLA IMDVNQNAVV SAMEKHQVQW LIHGHTHRPA
210 220 230 240
VHELIANQQP AFRVVLGAWH TEGSMVKVTA DDVELIHFPF
Length:240
Mass (Da):26,952
Last modified:November 25, 2008 - v1
Checksum:i79802A080C071581
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001164 Genomic DNA. Translation: ACI37743.1.
RefSeqiWP_000212254.1. NC_011353.1.

Genome annotation databases

EnsemblBacteriaiACI37743; ACI37743; ECH74115_0625.
KEGGiecf:ECH74115_0625.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiLPXH_ECO5E
AccessioniPrimary (citable) accession number: B5YPN9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: July 5, 2017
This is version 64 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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