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Q2W4D7 (LPXB_MAGSA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:amb2484
OrganismMagnetospirillum magneticum (strain AMB-1 / ATCC 700264) [Complete proteome] [HAMAP]
Taxonomic identifier342108 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum

Protein attributes

Sequence length390 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 – 390390Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255196

Sequences

Sequence LengthMass (Da)Tools
Q2W4D7 [UniParc].

Last modified January 10, 2006. Version 1.
Checksum: 6654FB66F2025349

FASTA39041,913
        10         20         30         40         50         60 
MLIYLIAGEP SGDLLGGRLM AALKERLGEG VSFAGIGGES MRAEGLTSLF PMTELSVMGL 

        70         80         90        100        110        120 
VEVLPRIPKI LRRVKQTISD IETKRPDALV TIDSWGFNGR IQAGLKARGV PVPRIHYVAP 

       130        140        150        160        170        180 
MVWAWKSGRT KTLARVLDLL LTLLPNEPEW FEKEGLKTLH VGHPVIEGAA SRGDGAAFRV 

       190        200        210        220        230        240 
RHGFAPDRKL LCVLPGSRHS ETAKLLAPFG ETIALLARRF PDLAVVVPTV ETVADEVSQA 

       250        260        270        280        290        300 
VKSWALPSMV VRGPEKYDAF AACDAALAAS GTVALELAMA RLPAVITYKV SPVSAFIATR 

       310        320        330        340        350        360 
FLGLSLKFVT LVNILVDEAV MPELLQDDCR PDKLAAAVEH LLTDEAARAL QAAGARRALE 

       370        380        390 
KLGLGGESPG KRAADAVIDF IRQGKEQRNG 

« Hide

References

[1]"Complete genome sequence of the facultative anaerobic magnetotactic bacterium Magnetospirillum sp. strain AMB-1."
Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.
DNA Res. 12:157-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AMB-1 / ATCC 700264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007255 Genomic DNA. Translation: BAE51288.1.
RefSeqYP_421847.1. NC_007626.1.

3D structure databases

ProteinModelPortalQ2W4D7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342108.amb2484.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE51288; BAE51288; amb2484.
GeneID3804689.
KEGGmag:amb2484.
PATRIC22439206. VBIMagMag129836_2442.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycMMAG342108:GJNU-2514-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_MAGSA
AccessionPrimary (citable) accession number: Q2W4D7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 10, 2006
Last modified: May 14, 2014
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways