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Q5QYW1 (LPXB_IDILO) 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:IL0832
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length379 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 – 379379Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255189

Sequences

Sequence LengthMass (Da)Tools
Q5QYW1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 774238F0BB3A3A0B

FASTA37942,324
        10         20         30         40         50         60 
MSRNQPPKIA IVAGEHSGDL LGAGLMQAIA KRHPNATFIG VGGPLMAERG MDSFFAMDDL 

        70         80         90        100        110        120 
AVMGIAEVFQ QLPKLLKHRK NLVNYLISEQ PDVMIGIDAP DFNLTVEARL KKAGISTIHY 

       130        140        150        160        170        180 
VSPSVWAWRE GRIKGIKKAV DHVLCLLPFE KDFYDKHQLP ATFVGHPLAD DIPMQWQQTE 

       190        200        210        220        230        240 
ARNELELEPA VMYLAILPGS RKGEIARMAP VFLKVANKLA ERYPELRFVA PMISEARAAQ 

       250        260        270        280        290        300 
FRELVDQYSP ELNIVLPVGE SRKVMAAANY LLLTSGTVAL EALLIKRPMV VAYRFHWLSY 

       310        320        330        340        350        360 
QIIKRLFHAP FFSLPNLLAG KEIVPELAQS DASEEAIEQA LVQLIEQDNE PLLEQFTNIH 

       370 
QQLQVSASEK AADVVESFL 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV81672.1.
RefSeqYP_155221.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QYW1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL0832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV81672; AAV81672; IL0832.
GeneID3172392.
KEGGilo:IL0832.
PATRIC22139697. VBIIdiLoi21852_0834.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAIARMLVN.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycILOI283942:GI0U-832-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_IDILO
AccessionPrimary (citable) accession number: Q5QYW1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 4, 2005
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