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

A4Y556 (LPXB_SHEPC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:Sputcn32_1361
OrganismShewanella putrefaciens (strain CN-32 / ATCC BAA-453) [Complete proteome] [HAMAP]
Taxonomic identifier319224 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length384 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 – 384384Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000049417

Sequences

Sequence LengthMass (Da)Tools
A4Y556 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: B746AF9CC8C68D25

FASTA38442,409
        10         20         30         40         50         60 
MSKKSQLVFA MVAGELSGDI LGAGLMAALQ KSHPDARFVG IGGPRMEALG FESLFAMEEL 

        70         80         90        100        110        120 
AVMGIVEVLS RLPRLLKVRA SLIKDITALK PDCFIGIDAP DFNIGLELKL KARGIKTVHY 

       130        140        150        160        170        180 
VSPSVWAWRP KRIFKIAKAT HMVLSLLPFE KAFYDKHQVP CTFVGHTLAD DIPLRSDKAA 

       190        200        210        220        230        240 
ARQLLELDAD AEYLAILPGS RGGELKQLAE PFVKAALLIK ENFPDIRFVT PLVNQKRRDQ 

       250        260        270        280        290        300 
FEQALKDHAP DLEIHMVEGK SREVMTAADG ILLASGTATL EAMLVKRPMV VAYRVSPLTY 

       310        320        330        340        350        360 
RIAKSMMQVN RFSLPNLLAG KDVVPELIQD DCTPEKIAAA VTVELNRDFA PLNAEFERLH 

       370        380 
QMLRCDASQK AADAVMRLVE TKEG 

« Hide

References

[1]"Complete sequence of Shewanella putrefaciens CN-32."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J., Tiedje J., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CN-32 / ATCC BAA-453.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000681 Genomic DNA. Translation: ABP75089.1.
RefSeqYP_001182888.1. NC_009438.1.

3D structure databases

ProteinModelPortalA4Y556.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319224.Sputcn32_1361.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP75089; ABP75089; Sputcn32_1361.
GeneID5080556.
KEGGspc:Sputcn32_1361.
PATRIC23551373. VBIShePut135485_1400.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSPUT319224:GHAP-1385-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_SHEPC
AccessionPrimary (citable) accession number: A4Y556
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 43 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