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Q3I354 (LUXS_CAMJJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:CJJ81176_1213
OrganismCampylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]
Taxonomic identifier354242 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length164 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 – 164164S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_0000297988

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q3I354 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 91807C03A5D01ACB

FASTA16418,257
        10         20         30         40         50         60 
MPLLDSFKVN HTKMPAPAVR LAKVMKTPKG DDISVFDLRF CVPNKDIMSE KGTHTLEHLF 

        70         80         90        100        110        120 
AGFMRDHLNS DSVEIIDISP MGCRTGFYMS LIGTPDEKSV AKAWEEAMKD VLSVSDQSKI 

       130        140        150        160 
PELNIYQCGT CAMHSLDEAK QIAQKVLNLG ISIMNNKELK LENA 

« Hide

References

« Hide 'large scale' references
[1]"Onset time as an objective parameter for evaluating AI-2 activity in the Vibrio harveyi bioluminescence assay."
Chen C.-Y., Irwin P.L.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Fouts D.E., Nelson K.E., Sebastian Y.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 81-176.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ143940 Genomic DNA. Translation: ABA26840.1.
CP000538 Genomic DNA. Translation: EAQ72038.1.
RefSeqYP_001000873.1. NC_008787.1.

3D structure databases

ProteinModelPortalQ3I354.
SMRQ3I354. Positions 3-163.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING354242.CJJ81176_1213.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAQ72038; EAQ72038; CJJ81176_1213.
GeneID4683564.
KEGGcjj:CJJ81176_1213.
PATRIC20052399. VBICamJej103413_1212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040371.
KOK07173.
OMARDHLNSD.
OrthoDBEOG68WRBM.

Enzyme and pathway databases

BioCycCJEJ354242:GC51-1189-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_CAMJJ
AccessionPrimary (citable) accession number: Q3I354
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 52 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