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A2CAG7 (A2CAG7_PROM3) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | 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 HAMAP MF_00523

EC=2.3.1.- HAMAP MF_00523
Gene names
Name:lpxD HAMAP MF_00523
Ordered Locus Names:P9303_17351
OrganismProchlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP] EMBL ABM78477.1
Taxonomic identifier59922 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length347 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

UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] = UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + [acyl-carrier-protein]. SAAS SAAS020573

Pathway

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

Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 3/6. SAAS SAAS020573

Subunit structure

Homotrimer By similarity. HAMAP MF_00523

Sequence similarities

Belongs to the transferase hexapeptide repeat family. LpxD subfamily. HAMAP MF_00523

Sequences

Sequence LengthMass (Da)Tools
A2CAG7 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 685D2A6581906153

FASTA34736,081
        10         20         30         40         50         60 
MRFSQLIASL QQGSAGLQDH QLAEDPELLS CASLDQAKAN QLSFLEQGNA LTTQLSHSKV 

        70         80         90        100        110        120 
GAVLIPPQDD LRVIAEQRGL AFAVLRDPRL AFAEALEQLH PRSRPKAGVH PTAVIGDQVH 

       130        140        150        160        170        180 
LGQGISIGAH VVIGDGSRIG AYSVVHPGVV IYEDVVVGEA NELHANAVLQ PGSRLGLNCV 

       190        200        210        220        230        240 
VHSNAVVGSE GFGFVPTANG WRKMPQTGLV VLEDGVEVGC GSTIDRPSVG ETRIGAGTKI 

       250        260        270        280        290        300 
DNLVQIGHGV VTGQGCALAS QVGIAGGARL GDGVILAGQV GVANRAVIGD RAIASSKSGI 

       310        320        330        340 
HGEVEAGEVV SGYPAIPNRL WLRCSASFSK LPEMAKMLRK LTRDTPQ 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000554 Genomic DNA. Translation: ABM78477.1.
RefSeqYP_001017742.1. NC_008820.1.

3D structure databases

ProteinModelPortalA2CAG7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2CAG7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4776922.
GenomeReviewsGene locus P9303_17351 in contig CP000554_GR.
KEGGpmf:P9303_17351.
PATRIC23000952. VBIProMar17757_1786.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1044.
HOGENOMHBG469615.
OMACFVGKNT.
PhylomeDBA2CAG7.
ProtClustDBPRK00892.

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.
ProtoNetSearch...

Entry information

Entry nameA2CAG7_PROM3
AccessionPrimary (citable) accession number: A2CAG7
Entry history
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)