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Q6N5R2 (LPXB_RHOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:RPA2909
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length393 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 – 393393Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255214

Sequences

Sequence LengthMass (Da)Tools
Q6N5R2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 301A25B00E36408F

FASTA39342,699
        10         20         30         40         50         60 
MSGAAKTGDR VRTVYLIATE ESGDRLGAAL MRELRARLGS KVRFAGVGGH CMAGEGLASL 

        70         80         90        100        110        120 
FPIEELSIIG FAAVVQRLPM ILKLIRRAVD AVLTAKPDIL VIIDSPDFTH RVARRVRQRD 

       130        140        150        160        170        180 
PSIPIVDYVS PTVWAWRPGR ARAMLGYVDH VLALLPFEPA EYRRLQGPPC SYVGHPLTEQ 

       190        200        210        220        230        240 
FGSLRPDAAE QARREASPPV LLVLPGSRRS EVRHHAAAFG DTLARLKHEG VAFEAVLPTT 

       250        260        270        280        290        300 
PHLEGLVRAA VASWEVQPRI VVGEQDKRAA FRIAHAALAK SGTVTLELAI AGVPMVTAYR 

       310        320        330        340        350        360 
AGSVEIWIAR RVVRPGTVIL ANLVMGDDVI PEFIQEDCVP DKLVPAVRDL LGNTPARRRQ 

       370        380        390 
LAGFAKIDDI LSTGEQTPSG RAADIVLDVM RHA 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris."
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.
Nat. Biotechnol. 22:55-61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX572602 Genomic DNA. Translation: CAE28350.1.
RefSeqNP_948250.1. NC_005296.1.

3D structure databases

ProteinModelPortalQ6N5R2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING258594.RPA2909.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE28350; CAE28350; RPA2909.
GeneID2691083.
KEGGrpa:RPA2909.
PATRIC23290255. VBIRhoPal84835_3054.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBCLSK911278.

Enzyme and pathway databases

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_RHOPA
AccessionPrimary (citable) accession number: Q6N5R2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 52 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