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Q21HI5 (LPXB_SACD2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:Sde_2584
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

Protein attributes

Sequence length388 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 – 388388Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255220

Sequences

Sequence LengthMass (Da)Tools
Q21HI5 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: AC341C9DF3A03F65

FASTA38842,934
        10         20         30         40         50         60 
MSSLKRVAIV VGEASGDILG AGLMAALKKR YPDCEFEGIG GPKMLALGFN SLYQMDRLAV 

        70         80         90        100        110        120 
MGFVEPLKRL PELLGIRKSL RQRYLTNPPD VFIGIDAPDF NLNLEVNLRE AGVPVVHYVS 

       130        140        150        160        170        180 
PSVWAWRRGR LKKIAKAVDL MLTLFPFESS FFNEQNIPNL FVGHPLADTI PLENEKTGAR 

       190        200        210        220        230        240 
ERLGLSAENN ERWVALLPGS RGGEVEHLCE RFLLAAQQSF AGRPNLRIII PAANDARHSQ 

       250        260        270        280        290        300 
ISEVLKRYSE LPVTLLHGQS HDAMLAADAI LIASGTATLE AMLLKRPMVI AYHMAAFSYW 

       310        320        330        340        350        360 
LLSKLVKSKF VGLPNLLADK ELVPELLQHN ATPSQLSAAL NVYLDSEKTT QQLIEQFNAI 

       370        380 
HLQLRRDASE TAAQGIVDML AAKRDIAR 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2-40 / ATCC 43961 / DSM 17024.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD81844.1.
RefSeqYP_528056.1. NC_007912.1.

3D structure databases

ProteinModelPortalQ21HI5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203122.Sde_2584.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD81844; ABD81844; Sde_2584.
GeneID3968634.
KEGGsde:Sde_2584.
PATRIC23404238. VBISacDeg56404_2784.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBCLSK2528760.

Enzyme and pathway databases

BioCycSDEG203122:GI2M-2629-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_SACD2
AccessionPrimary (citable) accession number: Q21HI5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 48 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