Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

UDP-2,3-diacylglucosamine hydrolase

Gene

lpxH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP.1 Publication

Catalytic activityi

UDP-2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + H2O = 2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate + UMP.UniRule annotation2 Publications

Enzyme regulationi

Inhibited by Triton X-100.

Kineticsi

  1. KM=61.7 µM for UDP-2,3-bis((3R)-3-hydroxymyristoyl)-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 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. 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.

GO - Molecular functioni

  • UDP-2,3-diacylglucosamine hydrolase activity Source: UniProtKB

GO - Biological processi

  • lipid A biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciEcoCyc:EG12666-MONOMER.
ECOL316407:JW0513-MONOMER.
MetaCyc:EG12666-MONOMER.
BRENDAi3.6.1.54. 2026.
UniPathwayiUPA00359; UER00480.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-2,3-diacylglucosamine hydrolaseUniRule annotation (EC:3.6.1.54UniRule annotation2 Publications)
Alternative name(s):
UDP-2,3-diacylglucosamine diphosphataseUniRule annotation
Gene namesi
Name:lpxHUniRule annotation
Synonyms:ybbF
Ordered Locus Names:b0524, JW0513
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12666. lpxH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240UDP-2,3-diacylglucosamine hydrolasePRO_0000214108Add
BLAST

Proteomic databases

PaxDbiP43341.

Interactioni

Protein-protein interaction databases

BioGridi4262817. 203 interactions.
DIPiDIP-10125N.
IntActiP43341. 20 interactions.
STRINGi511145.b0524.

Structurei

3D structure databases

ProteinModelPortaliP43341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LpxH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105F10. Bacteria.
COG2908. LUCA.
HOGENOMiHOG000261930.
InParanoidiP43341.
KOiK03269.
OMAiFMHGNRD.
OrthoDBiEOG6FNHR2.
PhylomeDBiP43341.

Family and domain databases

Gene3Di3.60.21.10. 2 hits.
HAMAPiMF_00575. LpxH.
InterProiIPR024654. Calcineurin-like_PHP_lpxH.
IPR029052. Metallo-depent_PP-like.
IPR010138. UDP-diacylglucosamine_Hdrlase.
[Graphical view]
PfamiPF12850. Metallophos_2. 1 hit.
[Graphical view]
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.
PATRICi32116208. VBIEscCol129921_0545.

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

3D structure databases

ProteinModelPortaliP43341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262817. 203 interactions.
DIPiDIP-10125N.
IntActiP43341. 20 interactions.
STRINGi511145.b0524.

Proteomic databases

PaxDbiP43341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73626; AAC73626; b0524.
BAE76301; BAE76301; BAE76301.
GeneIDi949053.
KEGGiecj:JW0513.
eco:b0524.
PATRICi32116208. VBIEscCol129921_0545.

Organism-specific databases

EchoBASEiEB2532.
EcoGeneiEG12666. lpxH.

Phylogenomic databases

eggNOGiENOG4105F10. Bacteria.
COG2908. LUCA.
HOGENOMiHOG000261930.
InParanoidiP43341.
KOiK03269.
OMAiFMHGNRD.
OrthoDBiEOG6FNHR2.
PhylomeDBiP43341.

Enzyme and pathway databases

UniPathwayiUPA00359; UER00480.
BioCyciEcoCyc:EG12666-MONOMER.
ECOL316407:JW0513-MONOMER.
MetaCyc:EG12666-MONOMER.
BRENDAi3.6.1.54. 2026.

Miscellaneous databases

PROiP43341.

Family and domain databases

Gene3Di3.60.21.10. 2 hits.
HAMAPiMF_00575. LpxH.
InterProiIPR024654. Calcineurin-like_PHP_lpxH.
IPR029052. Metallo-depent_PP-like.
IPR010138. UDP-diacylglucosamine_Hdrlase.
[Graphical view]
PfamiPF12850. Metallophos_2. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR01854. lipid_A_lpxH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis."
    Babinski K.J., Ribeiro A.A., Raetz C.R.H.
    J. Biol. Chem. 277:25937-25946(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Identification and sequence analysis of Escherichia coli purE and purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de novo purine biosynthesis."
    Watanabe W., Sampei G., Aiba A., Mizobuchi K.
    J. Bacteriol. 171:198-204(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 151-240.
  6. "Detection of new genes in a bacterial genome using Markov models for three gene classes."
    Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.
    Nucleic Acids Res. 23:3554-3562(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene."
    Babinski K.J., Kanjilal S.J., Raetz C.R.H.
    J. Biol. Chem. 277:25947-25956(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION.

Entry informationi

Entry nameiLPXH_ECOLI
AccessioniPrimary (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: January 20, 2016
This is version 118 of the entry and version 2 of the sequence. [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

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.