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B0UW62 (LPXB_HISS2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:HSM_0257
OrganismHistophilus somni (strain 2336) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier228400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length389 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 – 389389Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000080280

Sequences

Sequence LengthMass (Da)Tools
B0UW62 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: BB1965D781641EBE

FASTA38944,097
        10         20         30         40         50         60 
MIDKKNITIG IVAGEVSGDI LGAGLIRALK IQYPQARFIG IAGKNMLAEG CKTLVDMEDI 

        70         80         90        100        110        120 
AVMGLVEVIK YLPRLLKIRR LVIDTMLAEK PDIFIGIDAP DFNLDIELKL KKQGIKTLHY 

       130        140        150        160        170        180 
VSPSVWAWRQ KRIFKIAQAT NLVLAFLPFE KAFYDRFNVP CRFVGHTMAD IIDLQPDRQD 

       190        200        210        220        230        240 
ACFQLNLEPK HRYVAILVGS REAEVQFLTP PFLQTAQLIK QRFPDVQFLV PLVNEKRRKQ 

       250        260        270        280        290        300 
FEQIKAQIAP HLEVIFLDGQ ARQAMIVAEA SLLASGTASL ECMLCKSPMV VGYKMKPFTY 

       310        320        330        340        350        360 
FLAKRLVKTK YISLPNLLAD DMLVPEMIQE DCTAEKLAEK LSVYLEQTES GIKNRQHLIQ 

       370        380 
QFTQLHQLIR CDADKQAAQA VIDLLNDEV 

« Hide

References

[1]"Complete sequence of Haemophilus somnus 2336."
US DOE Joint Genome Institute
Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F., Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M., Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S., Dyer D.W., Inzana T.J.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2336.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000947 Genomic DNA. Translation: ACA31884.1.
RefSeqYP_001783608.1. NC_010519.1.

3D structure databases

ProteinModelPortalB0UW62.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228400.HSM_0257.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA31884; ACA31884; HSM_0257.
GeneID6108024.
KEGGhsm:HSM_0257.
PATRIC20197511. VBIHaeSom93646_0269.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycHSOM228400:GHWT-264-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_HISS2
AccessionPrimary (citable) accession number: B0UW62
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 38 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