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Q5L612 (LPXD_CHLAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:CAB466
OrganismChlamydophila abortus [Complete proteome] [HAMAP]
Taxonomic identifier83555 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length359 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 – 359359UDP-3-O-acylglucosamine N-acyltransferase HAMAP MF_00523
PRO_0000264357

Sites

Active site2481Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L612 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 92A94CDEAEAC9BF7

FASTA35938,764
        10         20         30         40         50         60 
MPQELVYTLQ QLADLLKVEV QGNTETPISG VEEISAAKAH HVTFLDNEKY ARFIKITEAG 

        70         80         90        100        110        120 
AIILSKAQAQ KYGHLNKNFL IVSEFPSIAF QKCIELFISP VDSGFPGIHP TAVIHPTASI 

       130        140        150        160        170        180 
GKDVCIEPYA VICQHACIGD STYIGTGSVI GAYSTLGEHC LVHPKVVVRE RVEIGKRVII 

       190        200        210        220        230        240 
QPGAVIGSCG FGYITNAFGR HKHLKHLGKV IIEDDVEIGA NTTIDRGRFK NSVIREGTKI 

       250        260        270        280        290        300 
DNQVQIAHHV EVGKHSMIVA QAGIAGSTKI GNHVIIGGQT GITGHISITD HVIMMAQTGV 

       310        320        330        340        350 
TKSISSPGIY GGAPARPYQE IHRQVAKIRS LPKLEERLGM LEEKVKGLSA QSTELQITP 

« Hide

References

[1]"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation."
Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.
Genome Res. 15:629-640(2005) [PubMed: 15837807] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S26/3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR848038 Genomic DNA. Translation: CAH63919.1.
RefSeqYP_219880.1. NC_004552.2.

3D structure databases

ProteinModelPortalQ5L612.
SMRQ5L612. Positions 7-348.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3337456.
GenomeReviewsGene locus CAB466 in contig CR848038_GR.
KEGGcab:CAB466.
PATRIC20202409. VBIChlAbo21869_0520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG469615.
OMASYPAKIM.
PhylomeDBQ5L612.
ProtClustDBPRK00892.

Enzyme and pathway databases

BioCycCABO218497:CAB466-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_CHLAB
AccessionPrimary (citable) accession number: Q5L612
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 21, 2005
Last modified: January 25, 2012
This is version 41 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