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Q2SWY5 (LPXB_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:BTH_I2040
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length388 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 – 388388Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255168

Sequences

Sequence LengthMass (Da)Tools
Q2SWY5 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: F0B56279745841C3

FASTA38842,128
        10         20         30         40         50         60 
MAFQPTPLRV ALVAGEPSGD LLGASLLGGL HAQLPASSRY YGIGGPRMTA VDFDAHWPME 

        70         80         90        100        110        120 
KLAVRGYVEA LKHIPEILRI RGELKRQLLA EPPDAFIGID APDFNFGLEQ ALRGAGIPTV 

       130        140        150        160        170        180 
HFVCPSIWAW RGGRIKKIVK AVDHMLCLFP FEPELLEKAG VAATFVGHPL ADEIPLEPDM 

       190        200        210        220        230        240 
HGARIALGLP DSGPVIAVLP GSRRSEIELI GPTFFDAMAL MQQREPGVRF VVPAATPALR 

       250        260        270        280        290        300 
ELLQPLVDAH PLLSVTLTEG RAQVAMTAAD AILVKSGTVT LEAALLKKPM VISYKVPWLT 

       310        320        330        340        350        360 
GQIMRRQGYL PYVGLPNILA GRFVVPELLQ HFATPEALAD ATLTQLRDDA NRRTLTGIFT 

       370        380 
DMHLALRQNT AQRAAEAVAR VIDSRKPH 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC37543.1.
RefSeqYP_442564.1. NC_007651.1.

3D structure databases

ProteinModelPortalQ2SWY5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING271848.BTH_I2040.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC37543; ABC37543; BTH_I2040.
GeneID3848338.
KEGGbte:BTH_I2040.
PATRIC19307122. VBIBurTha36512_4850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycBTHA271848:GJMY-2041-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_BURTA
AccessionPrimary (citable) accession number: Q2SWY5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 49 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