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Reviewed, UniProtKB/Swiss-Prot A1AEN2 (LUXS_ECOK1)

Last modified January 19, 2010. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    S-ribosylhomocysteine lyase
    EC=4.4.1.21
Alternative name(s):
    Autoinducer-2 production protein luxS
    AI-2 synthesis protein
Gene names
Name: luxS
Ordered Locus Names: Ecok1_26280
ORF Names: APECO1_3834
OrganismEscherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]
Taxonomic identifier405955 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length171 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD) By similarity. HAMAP MF_00091

Catalytic activity

S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. HAMAP MF_00091

Cofactor

Binds 1 iron ion per subunit By similarity. HAMAP MF_00091

Subunit structure

Homodimer By similarity. HAMAP MF_00091

Sequence similarities

Belongs to the luxS family.

Ontologies

Keywords
   Biological processAutoinducer synthesis
Quorum sensing
   LigandIron
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processquorum sensing

Inferred from electronic annotation. Source: HAMAP

   Molecular functionS-ribosylhomocysteine lyase activity

Inferred from electronic annotation. Source: HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 171171S-ribosylhomocysteine lyase HAMAP MF_00091
PRO_0000297996

Sites

Metal binding541Iron By similarity
Metal binding581Iron By similarity
Metal binding1281Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A1AEN2-1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 131F57F1866DA105

FASTA17119,416
        10         20         30         40         50         60 
MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE RGIHTLEHLF 

        70         80         90        100        110        120 
AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMED VLKVQDQNQI 

       130        140        150        160        170 
PELNVYQCGT YQMHSLQEAQ DIARSILERD VRINSNEELA LPKEKLQELH I 

« Hide

References

[1]"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
J. Bacteriol. 189:3228-3236(2007) [PubMed: 17293413] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000468 Genomic DNA. Translation: ABJ02122.1.
RefSeqYP_853882.1.

3D structure databases

SMRA1AEN2. Positions 3-161.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1AEN2.

Genome annotation databases

GeneID4493105.
GenomeReviewsGene locus Ecok1_26280 in contig CP000468_GR.
KEGGecv:APECO1_3834.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHBG347473.
OMAVRIAKTM.

Family and domain databases

HAMAPMF_00091. LuxS.
[Tree]
InterProIPR011249. Metalloenz_metal-bd.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
Gene3DG3DSA:3.30.1360.80. S-ribosylhomocysteinase. 1 hit.
PfamPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFPIRSF006160. AI2. 1 hit.
PRINTSPR01487. LUXSPROTEIN.
ProDomPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameLUXS_ECOK1
AccessionPrimary (citable) accession number: A1AEN2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents