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

B2I7N8 (LPXB_XYLF2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:XfasM23_0318
OrganismXylella fastidiosa (strain M23) [Complete proteome] [HAMAP]
Taxonomic identifier405441 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

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_1000123069

Sequences

Sequence LengthMass (Da)Tools
B2I7N8 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 1A95C0596A8E0531

FASTA38542,557
        10         20         30         40         50         60 
MIQAPRIAII AGEASGDHLG AGLIQQLRLH FATAEFIGIG GDMMRSAGCQ TWFDTSELAV 

        70         80         90        100        110        120 
MGLTEVLRHL PRLLKIRREF CKRALAWHPD VLIGIDAPDF NLTVERWFKQ RHIRTVHYVS 

       130        140        150        160        170        180 
PSIWAWREKR AAKIGASVDR VLCLFPMEPP IYARYGIDAR FVGHPMADEI PYQTDRATAR 

       190        200        210        220        230        240 
TALGLPLLSP VLAVLPGSRH SEISQLGNTF LEAAGQLSEH LPGLHVVIPA ANTQCKPLLA 

       250        260        270        280        290        300 
EQLSRSTLPV MHSHLLDSSA RTAMLAADVV LVASGTATLE AMLLKRPMVV AYKVAPLTYR 

       310        320        330        340        350        360 
IVKTLKLLKI NRFALPNILA GEDLVPELIQ KDCTAPALCA ALLDCFKHPQ KVTALQNRYL 

       370        380 
QLHTQLRRNA STRAAEAIAE LLQQR 

« Hide

References

[1]"Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) causing almond leaf scorch disease in California."
Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.
J. Bacteriol. 192:4534-4534(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M23.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001011 Genomic DNA. Translation: ACB91766.1.
RefSeqYP_001829040.1. NC_010577.1.

3D structure databases

ProteinModelPortalB2I7N8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405441.XfasM23_0318.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB91766; ACB91766; XfasM23_0318.
GeneID6204147.
KEGGxfn:XfasM23_0318.
PATRIC24142495. VBIXylFas85937_0435.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycXFAS405441:GJJI-336-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_XYLF2
AccessionPrimary (citable) accession number: B2I7N8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 36 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