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Q3IIW8 (LPXB_PSEHT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:PSHAa2017
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

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_0000255206

Sequences

Sequence LengthMass (Da)Tools
Q3IIW8 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 5EB17FDA1F34F8B2

FASTA38542,491
        10         20         30         40         50         60 
MNKDQKQLRI GIVAGELSGD ILGEGLIKAL KKHFPDAIFE GIAGPKMQAQ GCNTLYDMDE 

        70         80         90        100        110        120 
LSVMGLVEVL GRLPRLLKIR KQLVQHFIDN PPDVFIGIDA PDFNLRVEKP LKDAGIKTVQ 

       130        140        150        160        170        180 
YVSPSVWAWR EKRIHTISAA TNLVLALLPF EKEFYDKHQV PCTFVGHTLA DDIALEHDDS 

       190        200        210        220        230        240 
KARKELGLSP DDKVLALLPG SRGSEVGLLS ETYIKTAVQL QAQNPALKIV VPLVNAKRKA 

       250        260        270        280        290        300 
QFTEILNATA PTLKISLLDG QSKQAMQAAD AILLASGTAT LEGMLYKKPM VVGYKIKPLS 

       310        320        330        340        350        360 
YWIFKTLFTF NIKYFSLPNL LADEELVPEF LQSECNVANL TQALTPMLNT DNQALKARFL 

       370        380 
AIHKKIRLNA SEQAANAVAE LINAN 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TAC 125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954246 Genomic DNA. Translation: CAI87073.1.
RefSeqYP_340516.1. NC_007481.1.

3D structure databases

ProteinModelPortalQ3IIW8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326442.PSHAa2017.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI87073; CAI87073; PSHAa2017.
GeneID3710256.
KEGGpha:PSHAa2017.
PATRIC32297631. VBIPseHal105694_1944.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycPHAL326442:GJIU-2069-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_PSEHT
AccessionPrimary (citable) accession number: Q3IIW8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 8, 2005
Last modified: February 19, 2014
This is version 52 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