Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B6EJW7 (LPXB_ALISL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:VSAL_I2414
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP]
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length383 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 – 383383Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000191458

Sequences

Sequence LengthMass (Da)Tools
B6EJW7 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 1DEC4146FE77622D

FASTA38342,929
        10         20         30         40         50         60 
MTKPLRIGIV AGELSGDTLG EGFIKSVKAQ YPNAEFVGIG GPKMIAQGCE SLFDMEELAV 

        70         80         90        100        110        120 
MGLVEVLGRL PRLLKVKAEL VRYFSQNPPD VFIGIDAPDF NLRLEKTLKD SGIKTVHYVS 

       130        140        150        160        170        180 
PSVWAWRPKR IFKIDAATDL VLAFLPFEKV FYDKYNVACE FIGHTLADAI PMQSDKIAAR 

       190        200        210        220        230        240 
KLLGLELDRQ WLAVLPGSRG GEVALIAKPF IETCQRIHQK HPNMGFVVAA VNEKRREQFE 

       250        260        270        280        290        300 
VIWKETAPEL KFIIIQDTAR NVMTAADSVL LASGTVALEC MLIKRPMVVG YQVNKLTGWI 

       310        320        330        340        350        360 
AQKLSITEFV SLPNVLAGKE LVQEFIQEEC HPDFLYPAME KVLSQDNSEL IDRFTEMHQW 

       370        380 
IKKDADKQAA NAVLRLINKE TAE 

« Hide

References

[1]"The genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238 shows extensive evidence of gene decay."
Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.
BMC Genomics 9:616-616(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LFI1238.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM178379 Genomic DNA. Translation: CAQ80098.1.
RefSeqYP_002263768.1. NC_011312.1.

3D structure databases

ProteinModelPortalB6EJW7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316275.VSAL_I2414.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ80098; CAQ80098; VSAL_I2414.
GeneID6989138.
KEGGvsa:VSAL_I2414.
PATRIC20855249. VBIAliSal95923_2629.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

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_ALISL
AccessionPrimary (citable) accession number: B6EJW7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: May 14, 2014
This is version 39 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