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Q6ALW0 (LPXB_DESPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:DP1936
OrganismDesulfotalea psychrophila (strain LSv54 / DSM 12343) [Complete proteome] [HAMAP]
Taxonomic identifier177439 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea

Protein attributes

Sequence length386 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 – 386386Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255177

Sequences

Sequence LengthMass (Da)Tools
Q6ALW0 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 34559C7C93F5DAA3

FASTA38642,466
        10         20         30         40         50         60 
MDKQKRETGS EIMVVTGEAS GDIHGANLVR ALKEKDSSLS FSGMGGPELA SLGVEILYDA 

        70         80         90        100        110        120 
KKISVVGLVE VFSHLPSIFA AKKILQRRLK NKPPALLIII DLPDFNLMLA KKAKALGIPV 

       130        140        150        160        170        180 
FYYITPQVWA WRSGRIKTIG ERTDQLGVIL PFEEEFFRQR GQAASYVGHP LLDNVSIKLS 

       190        200        210        220        230        240 
REEFLTKHRI GPAAKYVGLL PGSREKEISA LLPDFLRAAK RLQDECSEKI SFLLPIAATI 

       250        260        270        280        290        300 
DREQLLENGL AEYQDLLDIH VISEDRYELM ACCDAVVAAS GTVTLELAIL EVPMLVVYRT 

       310        320        330        340        350        360 
SPISYWVGRK LVKIEFFSLV NLIAGREVVT ELLQDEVTPE RISIEIKELL YGAKGVAVGK 

       370        380 
GLREVHGLLG EAGASAKAAD LALSMI 

« Hide

References

[1]"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments."
Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.
Environ. Microbiol. 6:887-902(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR522870 Genomic DNA. Translation: CAG36665.1.
RefSeqYP_065672.1. NC_006138.1.

3D structure databases

ProteinModelPortalQ6ALW0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING177439.DP1936.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG36665; CAG36665; DP1936.
GeneID2944865.
KEGGdps:DP1936.
PATRIC21713822. VBIDesPsy67261_2104.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBCLSK2764922.

Enzyme and pathway databases

BioCycDPSY177439:GJW5-2000-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_DESPS
AccessionPrimary (citable) accession number: Q6ALW0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 54 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