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

Q2SBR1 (LPXB_HAHCH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:HCH_05238
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHahellaceaeHahella

Protein attributes

Sequence length396 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 – 396396Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255187

Sequences

Sequence LengthMass (Da)Tools
Q2SBR1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: B231BF9EA1441D0F

FASTA39644,033
        10         20         30         40         50         60 
MTPISERPIR IGIVAGEASG DLLGAGLMQE IKALYPQATF EGIGGERMLK EGFNTFFQME 

        70         80         90        100        110        120 
RLSIMGLVEV LGRLPELLAM RRRIVDHFTA TPPDLFLGID SPDFTIGIEL KLRQAGIKTA 

       130        140        150        160        170        180 
HYVSPSVWAW RQNRVFKIAK AVDLMLTLLP FEARFYREHN VPVKFVGHPL AEIIPLHPDK 

       190        200        210        220        230        240 
VAMRHELGID ASGEVIAVLP GSRGGEVSRL GPTFIETIAW LHQRRPDVRF VIPAANQARK 

       250        260        270        280        290        300 
TQIEQQLQSH GGRLPVTLID QHSRECMMAA DAILLASGTA TLEAMLVKRP MVVAYKLATL 

       310        320        330        340        350        360 
SYWIMRRLLK AKYISLPNLL ADKALVPELI QNDATPAKLG EALLKELNVE RRRSLEDEFE 

       370        380        390 
GLHKLIRQNA SVAAAQAVAE LIEKGRVATH DAREGH 

« Hide

References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KCTC 2396.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000155 Genomic DNA. Translation: ABC31913.1.
RefSeqYP_436338.1. NC_007645.1.

3D structure databases

ProteinModelPortalQ2SBR1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349521.HCH_05238.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3839772.
KEGGhch:HCH_05238.
PATRIC22090834. VBIHahChe29232_4768.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycHCHE349521:GHAL-5047-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_HAHCH
AccessionPrimary (citable) accession number: Q2SBR1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 49 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