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P0A3P9 (LUXS_STRP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:spyM18_1653
OrganismStreptococcus pyogenes serotype M18 (strain MGAS8232) [Complete proteome] [HAMAP]
Taxonomic identifier186103 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length160 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.

Sequence caution

The sequence AAL98199.1 differs from that shown. Reason: Erroneous initiation.

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 – 160160S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_0000172271

Sites

Metal binding571Iron By similarity
Metal binding611Iron By similarity
Metal binding1271Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A3P9 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: A45592396C76BD21

FASTA16017,979
        10         20         30         40         50         60 
MTKEVIVESF ELDHTIVKAP YVRLISEEFG PKGDRITNFD VRLVQPNQNS IETAGLHTIE 

        70         80         90        100        110        120 
HLLAKLIRQR IDGMIDCSPF GCRTGFHLIM WGKHSSTDIA KVIKSSLEEI ATGITWEDVP 

       130        140        150        160 
GTTLESCGNY KDHSLFAAKE WAQLIIDQGI SDDPFSRHVI 

« Hide

References

[1]"Genome sequence and comparative microarray analysis of serotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks."
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., Veasy L.G., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS8232.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009949 Genomic DNA. Translation: AAL98199.1. Different initiation.
RefSeqNP_607700.1. NC_003485.1.

3D structure databases

ProteinModelPortalP0A3P9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING186103.spyM18_1653.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL98199; AAL98199; spyM18_1653.
GeneID994586.
KEGGspm:spyM18_1653.
PATRIC19749814. VBIStrPyo4396_1481.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000040372.
KOK07173.
OrthoDBEOG68WRBM.

Enzyme and pathway databases

BioCycSPYO186103:GHJG-1429-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_STRP8
AccessionPrimary (citable) accession number: P0A3P9
Secondary accession number(s): Q99YL7, Q9EVB4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
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