Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2LVL8 (LPXB_SYNAS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:SYNAS_22450
ORF Names:SYN_01565
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length383 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 – 383383Lipid-A-disaccharide synthase HAMAP-Rule MF_00392
PRO_0000255228

Sequences

Sequence LengthMass (Da)Tools
Q2LVL8 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: 6086447ADAB7F983

FASTA38341,277
        10         20         30         40         50         60 
MNSKLVLIVA GEASGDLHGA SLVGAMVKRE PGIRFYGIGG VNLKTAGVDL WADAADMAVV 

        70         80         90        100        110        120 
GLTEVASKLR GILTVMHRLK KSMQLLKPDL VILIDYPDFN LPLARSAKKN GIPVFYYISP 

       130        140        150        160        170        180 
QVWAWRKGRL RTISGLVDRM AVILPFEEPL YRQAGVDVSF VGHPLLDVVQ ATSSRDETLR 

       190        200        210        220        230        240 
MFGLREDVTT VALLPGSRKG EVTRLLPVML KAARILTENI CPVQFLLPMA NTLDETWMKD 

       250        260        270        280        290        300 
QIAKADPPGV RLIRGATYDA VAAADAAVVV SGTATLETAL LGTPLIVIYK VSALSYLIGR 

       310        320        330        340        350        360 
MLISVDHIGL VNIVAGKTVA PELIQGAANP ERIAAEILAI LGQPDRRKAI QEELSHLRDK 

       370        380 
LGLPGAAERA AVMALTLIKK SDC 

« Hide

References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000252 Genomic DNA. Translation: ABC78124.1.
RefSeqYP_462292.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LVL8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_01565.

Protein family/group databases

CAZyGT19. Glycosyltransferase Family 19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC78124; ABC78124; SYN_01565.
GeneID3883758.
KEGGsat:SYN_01565.
PATRIC23865278. VBISynAci70500_2421.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0763.
HOGENOMHOG000018004.
KOK00748.
OMAVSPITYR.
OrthoDBEOG6FBWZR.

Enzyme and pathway databases

BioCycSACI56780:GHXT-2294-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_SYNAS
AccessionPrimary (citable) accession number: Q2LVL8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: February 21, 2006
Last modified: May 14, 2014
This is version 48 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