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

Q0HGW8 (LPXB_SHESM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Shewmr4_2628
OrganismShewanella sp. (strain MR-4) [Complete proteome] [HAMAP]
Taxonomic identifier60480 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length385 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 – 385385Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000049419

Sequences

Sequence LengthMass (Da)Tools
Q0HGW8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: C508C087C9A77E78

FASTA38542,423
        10         20         30         40         50         60 
MSKKSQLVFA MVAGELSGDI LGAGLMAALQ KTHPNARFVG IGGPRMEALG FESLFAMEEL 

        70         80         90        100        110        120 
AVMGIVEVLS RLPRLLHVRS SLIKSITELK PDCFIGIDAP DFNIGLELKL KAQGIKTVHY 

       130        140        150        160        170        180 
VSPSVWAWRP KRIFKIAKAT NMVLSLLPFE KAFYDKHQVP CTFVGHTLAD DIPLESDKAS 

       190        200        210        220        230        240 
ARQLLELDPD AEYLAILPGS RGGELKQLAE PFVKAALLIK QQFPDIRFVT PLVNQKRREQ 

       250        260        270        280        290        300 
FEQALKAHAP DLEIHMVEGK SREVMAAADG ILLASGTATL EAMLIKRPMV VAYRVSPLTY 

       310        320        330        340        350        360 
QIAKTMMQVN RFSLPNLLAG RDVVPELIQH DCTPEKIAAA VGVELNRDFA PIKAEFERLH 

       370        380 
QMLRCDASQK AAEAVLALVD AKDVN 

« Hide

References

[1]"Complete sequence of Shewanella sp. MR-4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MR-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000446 Genomic DNA. Translation: ABI39699.1.
RefSeqYP_734756.1. NC_008321.1.

3D structure databases

ProteinModelPortalQ0HGW8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING60480.Shewmr4_2628.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI39699; ABI39699; Shewmr4_2628.
GeneID4253199.
KEGGshe:Shewmr4_2628.
PATRIC23582018. VBISheSp133532_2724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycSSP60480:GI2N-2743-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_SHESM
AccessionPrimary (citable) accession number: Q0HGW8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 50 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