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Q1QMM4 (LPXB_NITHX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Nham_1707
OrganismNitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]
Taxonomic identifier323097 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

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_0000255201

Sequences

Sequence LengthMass (Da)Tools
Q1QMM4 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: FD838EA70425C56F

FASTA39643,700
        10         20         30         40         50         60 
MADGTAANSS RRIFLIATEE SGDRLGSSLM KVLRRRLDDA VRFEGVGGRS MAREGLVSLF 

        70         80         90        100        110        120 
PIEDLSIMGF AAVVKQLPMI LRRIRETADA VIAAEPDMLV IIDSPDFTHR VARRVRARRP 

       130        140        150        160        170        180 
ALPIVDYVSP SVWAWRPGRA RAMRRYVDHV LALLPFEPEE YRRLAGPPCT YVGHPLIEQV 

       190        200        210        220        230        240 
GMLRPDAQER QRRDAPPPAL LVLPGSRRSE IDHHMAVFGE TLRTLQLDAG EMDVVLLTMP 

       250        260        270        280        290        300 
HLIEKVKAAV ASWPLQPRIV VGEQGKQAAF RVARAALTKS GTVTLELALA GVPMVTAYRG 

       310        320        330        340        350        360 
GAVEAWIAQR VIRTSSVILA NLVIGENVIP EFLQENCTPE NLAPALREIL TDSPLRRRQL 

       370        380        390 
KAFAKLDAIM ATGQHSPSER AADIVLETMH ASRGPE 

« Hide

References

[1]"Complete sequence of chromosome of Nitrobacter hamburgensis X14."
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., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X14 / DSM 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000319 Genomic DNA. Translation: ABE62523.1.
RefSeqYP_576983.1. NC_007964.1.

3D structure databases

ProteinModelPortalQ1QMM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323097.Nham_1707.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE62523; ABE62523; Nham_1707.
GeneID4030307.
KEGGnha:Nham_1707.
PATRIC22691076. VBINitHam61822_2560.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBCLSK911278.

Enzyme and pathway databases

BioCycNHAM323097:GHP7-1734-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_NITHX
AccessionPrimary (citable) accession number: Q1QMM4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 45 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