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

Q7MWT9 (LUXS_PORGI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. 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:PG_0498
OrganismPorphyromonas gingivalis (strain ATCC BAA-308 / W83) [Complete proteome] [HAMAP]
Taxonomic identifier242619 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas

Protein attributes

Sequence length159 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 – 159159S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_0000298019

Sites

Metal binding531Iron By similarity
Metal binding571Iron By similarity
Metal binding1241Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7MWT9 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: A56C9F19EF27E37B

FASTA15918,554
        10         20         30         40         50         60 
MEKIPSFQLD HIRLKRGIYV SRKDYIGGEV VTTFDIRMKE PNREPVLGAP ELHTIEHLAA 

        70         80         90        100        110        120 
TYLRNHPLYK DRIVFWGPMG CLTGNYFLMR GDYVSKDILP LMQETFRFIR DFEGEVPGTE 

       130        140        150 
PRDCGNCLLH NLPMAKYEAE KYLREVLDVA TEENLNYPD 

« Hide

References

[1]"Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83."
Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J., Granger D., Tettelin H. expand/collapse author list , Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E., Fraser C.M.
J. Bacteriol. 185:5591-5601(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-308 / W83.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015924 Genomic DNA. Translation: AAQ65692.1.
RefSeqNP_904793.1. NC_002950.2.

3D structure databases

ProteinModelPortalQ7MWT9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242619.PG0498.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ65692; AAQ65692; PG_0498.
GeneID2552279.
KEGGpgi:PG0498.
PATRIC22978092. VBIPorGin134034_0457.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
KOK07173.
OMATFDIRMK.
OrthoDBEOG68WRBM.
ProtClustDBPRK02260.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14563.
PGIN242619:GHX8-450-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_PORGI
AccessionPrimary (citable) accession number: Q7MWT9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: December 15, 2003
Last modified: April 16, 2014
This is version 64 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