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Q66E63 (LUXS_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
S-ribosylhomocysteine lyase

EC=4.4.1.21
Alternative name(s):
AI-2 synthesis protein
Autoinducer-2 production protein LuxS
Gene names
Name:luxS
Ordered Locus Names:YPTB0830
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

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-Rule MF_00091

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity. HAMAP-Rule MF_00091

Subunit structure

Homodimer By similarity. HAMAP-Rule 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: UniProtKB-HAMAP

   Molecular_functionS-ribosylhomocysteine lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 171171S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_0000172281

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q66E63 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: B46F3D9BD23663E1

FASTA17119,396
        10         20         30         40         50         60 
MPLLDSFTVD HTIMKAPAVR VAKTMKTPHG DEITVFDLRF CVPNKEVMPE KGIHTLEHLF 

        70         80         90        100        110        120 
AGFMRDHLNG DGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMAD VLKVTDQRKI 

       130        140        150        160        170 
PELNEYQCGT YHMHSLEEAQ SIAKDILDRD VRINHNEELA LPKEKLTELH I 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH20070.1.
RefSeqYP_069371.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ66E63.
SMRQ66E63. Positions 3-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB0830.

Proteomic databases

PRIDEQ66E63.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH20070; CAH20070; YPTB0830.
GeneID2955974.
KEGGyps:YPTB0830.
PATRIC18639988. VBIYerPse22266_1082.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040371.
KOK07173.
OMARFKQPNQ.
OrthoDBEOG68WRBM.
ProtClustDBPRK02260.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-876-MONOMER.

Family and domain databases

Gene3D3.30.1360.80. 1 hit.
HAMAPMF_00091. LuxS.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
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]
SUPFAMSSF63411. SSF63411. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLUXS_YERPS
AccessionPrimary (citable) accession number: Q66E63
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 58 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