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Q215D6 (LPXB_RHOPB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:RPC_2449
OrganismRhodopseudomonas palustris (strain BisB18) [Complete proteome] [HAMAP]
Taxonomic identifier316056 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length396 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 – 396396Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255215

Sequences

Sequence LengthMass (Da)Tools
Q215D6 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 1301C262E03031FB

FASTA39643,002
        10         20         30         40         50         60 
MTAVATHAVR KIFLIATEES GDRLGASLMR ELRDRLGAAV RFEGVGGRAM AREGLTSLFP 

        70         80         90        100        110        120 
IEELSIIGLS AVARRLPTIL RHIRTAAHAA LQAAPDVLVI IDSPDFTHRV ARRVRARDPS 

       130        140        150        160        170        180 
IPIVNYVSPT VWAWRPGRAK VMRKYVDHVL ALLPFEPDEY RRLQGPPCSY VGHPLTEQIA 

       190        200        210        220        230        240 
TLRPNPEEQL RRDAAPPVLL VLPGSRRSEI RHHMAVFGEA LGLLQAQGVA FELILPTMPH 

       250        260        270        280        290        300 
LEALIAEALK HWPLQPRVVV GENDKRAAFR IARAALAKSG TVTLELAVAG VPMVTAYRAG 

       310        320        330        340        350        360 
QLEAWIVRRR ITSASVILAN LVVGENVAPE YLQEECTAPT LAAALRDVLA DSPLRQRQLA 

       370        380        390 
AFGRIDAIMS TGAQSPSACA ADIVLGLLPA AAPALR 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisB18."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BisB18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000301 Genomic DNA. Translation: ABD88000.1.
RefSeqYP_532319.1. NC_007925.1.

3D structure databases

ProteinModelPortalQ215D6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316056.RPC_2449.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Proteomic databases

PRIDEQ215D6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD88000; ABD88000; RPC_2449.
GeneID3971379.
KEGGrpc:RPC_2449.
PATRIC23269634. VBIRhoPal29154_2513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMARRSEIRH.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycRPAL316056:GH3E-2478-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_RHOPB
AccessionPrimary (citable) accession number: Q215D6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 18, 2006
Last modified: May 14, 2014
This is version 47 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