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B4RVJ5 (LPXB_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:MADE_1005380
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

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_1000191459

Sequences

Sequence LengthMass (Da)Tools
B4RVJ5 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 71832D847E3CC0F3

FASTA38242,334
        10         20         30         40         50         60 
MSKPIRIGMV AGEPSGDILA AGMVAELKRQ YPDAIIEGIG GPNMIDAGFH SLFDMETLSV 

        70         80         90        100        110        120 
MGLVEVLAHL PAILKVKKQL LAHFEQNPPD IFVGVDAPDF NLRVEKALKA RGIKTMHYVS 

       130        140        150        160        170        180 
PTVWAWREKR IHKIAKAANR VLGLFPFEQQ VYDKYHVPYT FVGHTMADAI AIEPDQNAAR 

       190        200        210        220        230        240 
QELGVESNAY VLAVLPGSRR GEVETLLPVF LETIEAIHVK RSDIQFLIPA ANEHRLAQIK 

       250        260        270        280        290        300 
AFLQEANNAE ERLPIQVTQG TSRDAMIASD VILLASGTAT LEAMLCKRPM VAAYLLSPLT 

       310        320        330        340        350        360 
YKIMQRLYKA PFFTLPNLLA NEAIIPELLQ EEVNAENMSN QLLNFFESDN SALIARFTDL 

       370        380 
HHTLKCNADK TAAKAVVEEL FA 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001103 Genomic DNA. Translation: AEA97222.1.
RefSeqYP_004426220.1. NC_011138.3.

3D structure databases

ProteinModelPortalB4RVJ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314275.MADE_01385.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA97222; AEA97222; MADE_1005380.
GeneID10556419.
KEGGamc:MADE_1005380.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
KOK00748.
OMAVSPITYR.

Enzyme and pathway databases

BioCycAMAC314275:GHA7-1093-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_ALTMD
AccessionPrimary (citable) accession number: B4RVJ5
Secondary accession number(s): F2G288
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 44 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