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Q3BVL7 (LPXB_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipid-A-disaccharide synthase

EC=2.4.1.182
Gene names
Name:lpxB
Ordered Locus Names:XCV1465
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. HAMAP-Rule MF_00392

Catalytic activity

UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate = UDP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. HAMAP-Rule MF_00392

Pathway

Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 5/6. HAMAP-Rule MF_00392

Sequence similarities

Belongs to the LpxB family.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid biosynthesis
Lipid metabolism
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionlipid-A-disaccharide synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255233

Sequences

Sequence LengthMass (Da)Tools
Q3BVL7 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: A74B1FD9A3FC4D43

FASTA43947,534
        10         20         30         40         50         60 
MKEIGNRESG IVDGQRNGAS VGSDPTALPI PHSPLPIPGA HARPPRIALI AGEASGDILG 

        70         80         90        100        110        120 
AGLIEQLRLR YPNAEFVGIG GDAMRGVGCQ TWFDASELAV MGLTEVLRHL PRLLKLRSAF 

       130        140        150        160        170        180 
RERVLAWKPD VFIGIDAPDF NLPVERWLKQ RGIKTVHYVS PSVWAWREKR AEKIGVSADL 

       190        200        210        220        230        240 
VLCLFPMEPP IYARHGVDAR FVGHPMADDI AYQADRAAAR ATLGLSASST VLAVLPGSRH 

       250        260        270        280        290        300 
GEISRLGDTF FQAAWLVSEH LPNLHVLVPA ANPGCKQLLA EQLSRSSLPV MRSHLLDGQA 

       310        320        330        340        350        360 
RTAMLAADVV LLASGTATLE AMLVKRPMVV GYKVAPLTYR IVKLLGLLKV NRYALPNILA 

       370        380        390        400        410        420 
NDDLAPELMQ DDCAPERLCV ALLDWFKHPD KVAALQPRYL ALHAQLRRDA SARAADAVAG 

       430 
LLEGRDSEVG IWDSAGAKA 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ23096.1.
RefSeqYP_363196.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BVL7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV1465.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ23096; CAJ23096; XCV1465.
GeneID3733693.
KEGGxcv:XCV1465.
PATRIC24092408. VBIXanCam71633_1699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBPRK00025.

Enzyme and pathway databases

BioCycXCAM316273:GJF8-1505-MONOMER.
UniPathwayUPA00359; UER00481.

Family and domain databases

HAMAPMF_00392. LpxB.
InterProIPR003835. Glyco_trans_19.
[Graphical view]
PfamPF02684. LpxB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00215. lpxB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLPXB_XANC5
AccessionPrimary (citable) accession number: Q3BVL7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways