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Q485F5 (LPXB_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:CPS_1568
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

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_0000255175

Sequences

Sequence LengthMass (Da)Tools
Q485F5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 380EDA95FF7BB4CC

FASTA39343,815
        10         20         30         40         50         60 
MTTQNQNTHQ QTVFAMVVGE HSGDTLGAGL ITSLRQTHPH AKFIGIGGPK MLALGFESLF 

        70         80         90        100        110        120 
AMDELSVMGL VEVLGRIRRL LHVRKTLTDF FITNKPDVFI GIDAPDFNIG LELKLKVKGI 

       130        140        150        160        170        180 
KTVHYVSPSV WAWREKRIFK IAKATDMVLA LLPFEKAFYD KHNVPCTFVG HPLADDIPMQ 

       190        200        210        220        230        240 
SDKVLARDKL GLAQDKKILA LMPGSRGGEL SRLLEDFFES AKQLQAQDSE LLFVAPMISE 

       250        260        270        280        290        300 
QRANQFNALK AELAPDLDIE IVLNQTQQVM AASDCLLTAS GTVTLEAALI KRPMVICYKF 

       310        320        330        340        350        360 
SPITFFLGRR FVKLKWFSLP NLLTNKSLVP ELLQKDVCPE NIVPLVKERL YQDQSQLNDS 

       370        380        390 
FTAIHQQLKC DASKQAAKAV LDVLSSKLLS NNK 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ28777.1.
RefSeqYP_268310.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ485F5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167879.CPS_1568.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ28777; AAZ28777; CPS_1568.
GeneID3523039.
KEGGcps:CPS_1568.
PATRIC21466341. VBIColPsy94388_1422.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCPSY167879:GI48-1568-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_COLP3
AccessionPrimary (citable) accession number: Q485F5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 46 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