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Q47F79 (LPXB_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Daro_1755
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length382 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 – 382382Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255176

Sequences

Sequence LengthMass (Da)Tools
Q47F79 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: E4BF34C68E6D804D

FASTA38242,578
        10         20         30         40         50         60 
MGSAVRIAMV AGEASGDLLA SHLIAALKTH LPDAVFYGIG GPKMQAQGFD SWWPMEKLSV 

        70         80         90        100        110        120 
MGYWDALKHY REIAGIRRQL KKRLLDLKPD IFIGVDAPDF NLGLETNLKA AGVRTIHYVS 

       130        140        150        160        170        180 
PSIWAWRGGR VKKIAKAVNR VLALFPMEPA LYEKERVPVT YVGHPLADII PLQTSKQAVR 

       190        200        210        220        230        240 
EKLSLPRDYP IFAMLPGSRQ GELAMMAETF VETAKIIRER HLPNAMFVVP LATRETRLQF 

       250        260        270        280        290        300 
ELAIYNRQAG DVPFRLLFGH AQDALGAADV SLVASGTATL EAALIKRPMV ITYKIAKFSY 

       310        320        330        340        350        360 
WLMKRMAYLP YVGLPNVLAG RFVVPEILQD EATPENLAEA LVKLYEDKEN AEAVEEAFTE 

       370        380 
IHLQLRQNTA EKAARAVIEC LN 

« Hide

References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ46502.1.
RefSeqYP_284972.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47F79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_1755.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ46502; AAZ46502; Daro_1755.
GeneID3568710.
KEGGdar:Daro_1755.
PATRIC21602152. VBIDecAro89105_1740.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycDARO159087:GI5B-1809-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_DECAR
AccessionPrimary (citable) accession number: Q47F79
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 13, 2005
Last modified: May 14, 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