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

P0C111 (LPXD_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
UDP-3-O-acylglucosamine N-acyltransferase

EC=2.3.1.-
Gene names
Name:lpxD
Ordered Locus Names:BruAb1_1159
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. HAMAP-Rule MF_00523

Catalytic activity

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + UDP-3-O-acyl-alpha-D-glucosamine = UDP-2,3-diacyl-alpha-D-glucosamine + [acyl-carrier-protein]. HAMAP-Rule MF_00523

Pathway

Bacterial outer membrane biogenesis; LPS lipid A biosynthesis. HAMAP-Rule MF_00523

Subunit structure

Homotrimer By similarity. HAMAP-Rule MF_00523

Sequence similarities

Belongs to the transferase hexapeptide repeat family. LpxD subfamily.

Ontologies

Keywords
   Biological processLipid A biosynthesis
Lipid biosynthesis
Lipid metabolism
   DomainRepeat
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processlipid A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functiontransferase activity, transferring acyl groups other than amino-acyl groups

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351UDP-3-O-acylglucosamine N-acyltransferase HAMAP-Rule MF_00523
PRO_0000059652

Sites

Active site2571Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C111 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: ECC1ED7ED029D01A

FASTA35136,357
        10         20         30         40         50         60 
MADPIFFKPS RELTIGDVAD FTGASLRDPK LAPRSVERLA SLKDAGEGAL VFVEGKKNVS 

        70         80         90        100        110        120 
SLVGLKAAGV LCTESLADSV PSGIAVLVSR HPHRDFSAVG RMLFPASVRP ESWLGETGIS 

       130        140        150        160        170        180 
PAAFIHPTAQ IEDGATVEAG AVIGSGVTIG AGTLIAATAV IGQNCQIGRN SYIAPGVSVQ 

       190        200        210        220        230        240 
CAFIGNNVSL HPGVRIGQDG FGYVPGAAGL DKVPQLGRVI IQDNVEIGAN TTVDRGSLDD 

       250        260        270        280        290        300 
TVIGEGTKID NLVQIAHNVR IGRFCLVAAH CGISGSCVIG DQTMLGGRVG LADHLIIGSR 

       310        320        330        340        350 
VQVAAASGVM NDIPDGERWG GIPARPIKQW FRDIANIRSI GQSRKDASSD E 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX74498.1.
RefSeqYP_221859.1. NC_006932.1.

3D structure databases

ProteinModelPortalP0C111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb1_1159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX74498; AAX74498; BruAb1_1159.
GeneID3339833.
KEGGbmb:BruAb1_1159.
PATRIC17824006. VBIBruAbo15061_1225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1044.
HOGENOMHOG000294340.
KOK02536.
OMASHIHIGH.
OrthoDBEOG6JB11D.

Enzyme and pathway databases

BioCycBABO262698:GJC2-1181-MONOMER.
UniPathwayUPA00973.

Family and domain databases

HAMAPMF_00523. LpxD.
InterProIPR001451. Hexapep_transf.
IPR018357. Hexapep_transf_CS.
IPR011004. Trimer_LpxA-like.
IPR007691. UDP-3-O_GlcNAc_AcTrfase.
IPR020573. UDP_GlcNAc_AcTrfase_non-rep.
[Graphical view]
PfamPF00132. Hexapep. 3 hits.
PF04613. LpxD. 1 hit.
[Graphical view]
SUPFAMSSF51161. SSF51161. 1 hit.
TIGRFAMsTIGR01853. lipid_A_lpxD. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXD_BRUAB
AccessionPrimary (citable) accession number: P0C111
Secondary accession number(s): P0A3P6, Q44630, Q57CY6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 51 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

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names