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Q7NVY4 (LPXD_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
UDP-3-O-acylglucosamine N-acyltransferase

EC=2.3.1.-
Gene names
Name:lpxD
Ordered Locus Names:CV_2206
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeChromobacterium

Protein attributes

Sequence length348 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 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 MF_00523

Pathway

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

Subunit structure

Homotrimer By similarity. HAMAP MF_00523

Sequence similarities

Belongs to the transferase hexapeptide repeat family. LpxD subfamily.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontransferase activity, transferring acyl groups other than amino-acyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348UDP-3-O-acylglucosamine N-acyltransferase HAMAP MF_00523
PRO_0000059666

Sites

Active site2381Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NVY4 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 69DDC6C7D1543544

FASTA34837,120
        10         20         30         40         50         60 
MSYTLEHIVK QLGGALRGPN REVSRLAPLE LAGAGEIAFV ASAKFRRQML ESAADALIVT 

        70         80         90        100        110        120 
EALAAELPDR SLIVAADPYL YFARLATLFH PPKAPRAGIH PRAVVGVGCR IGESSEIAAN 

       130        140        150        160        170        180 
ATIGDNVVIG ERCRLMPGVV VGDGCEIGDD VTLYPNVTIY HDCVIGNRVG VHSGSVIGGD 

       190        200        210        220        230        240 
GFGLAWDKDH WFKIPQTGRV VLEDDVEIGA NTTVDRGALV DTVIRKGAKI DNLVQIAHNV 

       250        260        270        280        290        300 
EIGEHTAIAG CVGIAGSTKI GARCTVGGAA MFVGHIEVAD RTHIGGGTLV SKSIKEAGNY 

       310        320        330        340 
ASSYPLQSMK DWLSNAVHVR HLDDFAKRVK QLERELETLK KSKEEPHE 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ59879.1.
RefSeqNP_901876.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NVY4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2549370.
GenomeReviewsGene locus CV_2206 in contig AE016825_GR.
KEGGcvi:CV_2206.
NMPDRfig|243365.1.peg.2206.
PATRIC21439194. VBIChrVio67196_2153.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG469615.
OMACFVGKNT.
PhylomeDBQ7NVY4.
ProtClustDBPRK00892.

Enzyme and pathway databases

BioCycCVIO243365:CV_2206-MONOMER.

Family and domain databases

HAMAPMF_00523. LpxD.
[Tree]
InterProIPR001451. Hexapep_transf.
IPR011004. Trimer_LpxA-like.
IPR007691. UDP-3-O_GlcNAc_AcTrfase.
IPR020573. UDP_GlcNAc_AcTrfase_non-rep.
[Graphical view]
KOK02536.
PfamPF00132. Hexapep. 5 hits.
PF04613. LpxD. 1 hit.
[Graphical view]
SUPFAMSSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMsTIGR01853. Lipid_A_lpxD. 1 hit.
PROSITEPS00101. HEXAPEP_TRANSFERASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLPXD_CHRVO
AccessionPrimary (citable) accession number: Q7NVY4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families