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Protein

UDP-2,3-diacylglucosamine hydrolase

Gene

lpxH

Organism
Shewanella halifaxensis (strain HAW-EB4)
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 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:Shal_2773
OrganismiShewanella halifaxensis (strain HAW-EB4)
Taxonomic identifieri458817 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000001317 Componenti: Chromosome

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_10000823421 – 238UDP-2,3-diacylglucosamine hydrolaseAdd BLAST238

Interactioni

Protein-protein interaction databases

STRINGi458817.Shal_2773.

Structurei

3D structure databases

SMRiB0TLV4.
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:SF3. PTHR34990:SF3. 1 hit.
PfamiView protein in Pfam
PF00149. Metallophos. 1 hit.
SUPFAMiSSF56300. SSF56300. 1 hit.
TIGRFAMsiTIGR01854. lipid_A_lpxH. 1 hit.

Sequencei

Sequence statusi: Complete.

B0TLV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLFVGDLH LSTDRPDITQ AFLRFLDTQL HDTDALYILG DLFEVWVGDD
60 70 80 90 100
IAEPFAEQLA KAIYQASQKL PIFFIHGNRD FLISNAFAKR SGMTLLPEIY
110 120 130 140 150
TVDLYGIPTV ILHGDSLCTL DKPYQRFRKF RNLGWAKWLY AHLPKSKRLD
160 170 180 190 200
IAVKLRSKSQ SSNQQKSYSI MDVEPDAVLE LLNATKTEQM IHGHTHRPAI
210 220 230
HQLANGRRRI VVGDWYEQGS MLSVSQDKIE LIELPFGK
Length:238
Mass (Da):27,300
Last modified:April 8, 2008 - v1
Checksum:iDE9F0D9D98435912
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000931 Genomic DNA. Translation: ABZ77326.1.
RefSeqiWP_012277854.1. NC_010334.1.

Genome annotation databases

EnsemblBacteriaiABZ77326; ABZ77326; Shal_2773.
KEGGishl:Shal_2773.

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_SHEHH
AccessioniPrimary (citable) accession number: B0TLV4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: July 5, 2017
This is version 62 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