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A8FY29 (LPXB_SHESH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:Ssed_3148
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length380 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 – 380380Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000080286

Sequences

Sequence LengthMass (Da)Tools
A8FY29 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 8EE224D7DF3C63EC

FASTA38042,011
        10         20         30         40         50         60 
MSETTHPTFA MVAGELSGDI LGAGLIKALQ HQYPDARFVG IGGPRMEALG FESIFSFEEL 

        70         80         90        100        110        120 
AVMGIVEVLS RLQRLLKVRK TLIDEICSIE PACFIGIDAP DFNIGLELKL KARGIKTVHY 

       130        140        150        160        170        180 
VSPSVWAWRP KRIFKIAKAT DMVLSLLPFE KAFYDKHDVP CTFVGHTLAD DIPLISDKTA 

       190        200        210        220        230        240 
ARNLLGLDAD AEYLAVLPGS RGGELKQLAE PFVKAASLIK KRYPDIRFVT PLVNQKRREQ 

       250        260        270        280        290        300 
FEEALKLHAP DLEITLVEGH SREVMAASDC ILLASGTATL EAMLVKRPMV VAYRVSPITY 

       310        320        330        340        350        360 
KIAKGMMQID QYSLPNLLSG ETLVTELIQE NCTESLIADA ISEQLDSDFS PLKEKFMQLH 

       370        380 
KGLKCNASER AAEAVIKLIQ 

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000821 Genomic DNA. Translation: ABV37752.1.
RefSeqYP_001474880.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FY29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING425104.Ssed_3148.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV37752; ABV37752; Ssed_3148.
GeneID5610179.
KEGGsse:Ssed_3148.
PATRIC23564057. VBISheSed62411_3345.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSED425104:GH7Q-3266-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_SHESH
AccessionPrimary (citable) accession number: A8FY29
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 42 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