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A8GID3 (LPXB_SERP5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:Spro_3777
OrganismSerratia proteamaculans (strain 568) [Complete proteome] [HAMAP]
Taxonomic identifier399741 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length382 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 – 382382Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_1000060774

Sequences

Sequence LengthMass (Da)Tools
A8GID3 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 544FC0A596EBAC34

FASTA38242,312
        10         20         30         40         50         60 
MQNRPLTIGL VAGETSGDIL GAGLIRALKA QIPDARFVGV AGPLMQAEGC ETWYEMEELA 

        70         80         90        100        110        120 
VMGVVEVLER LPRLLKIRKD LTRRFSDLAP DVFVGIDAPD FNITLEGRLK QRGIRTIHYV 

       130        140        150        160        170        180 
SPSVWAWRQK RVFKIGKATD LVLAFLPFEK AFYDRFNVPC RFIGHTMADA MPLQPDKLAA 

       190        200        210        220        230        240 
RAKLGIAADA RCLALLPGSR GAEVEMLSAD FLKTAQLLRT RYPELELVVP LVNAKRREQF 

       250        260        270        280        290        300 
ERIKAEVAPE LRVHLLNGQG REAMIASDAA LLASGTAALE CMLAKCPMVV GYRMKPFTFW 

       310        320        330        340        350        360 
IAQRLVKTPY VSLPNLLAGR EIVTELLQHD CVPDKLAASV MPLLEDSPQT DELKQTFLTL 

       370        380 
HQSIRCGADE QAAQAVLELA KA 

« Hide

References

[1]"Complete sequence of chromosome of Serratia proteamaculans 568."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 568.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000826 Genomic DNA. Translation: ABV42873.1.
RefSeqYP_001480001.1. NC_009832.1.

3D structure databases

ProteinModelPortalA8GID3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399741.Spro_3777.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV42873; ABV42873; Spro_3777.
GeneID5607353.
KEGGspe:Spro_3777.
PATRIC32420370. VBISerPro44537_3837.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018003.
KOK00748.
OMAYIAPQEW.
OrthoDBEOG6FBWZR.
ProtClustDBPRK00025.

Enzyme and pathway databases

BioCycSPRO399741:GI55-3857-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_SERP5
AccessionPrimary (citable) accession number: A8GID3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 38 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