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Q9Z5X1 (LUXS_VIBCB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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:VIBHAR_03484
OrganismVibrio campbellii (strain ATCC BAA-1116 / BB120) [Complete proteome] [HAMAP]
Taxonomic identifier338187 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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). Ref.1

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 ABU72429.1 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

Initiator methionine11Removed By similarity
Chain2 – 172171S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_0000172275

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q9Z5X1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2B36D46F68118E89

FASTA17219,143
        10         20         30         40         50         60 
MPLLDSFTVD HTRMNAPAVR VAKTMQTPKG DTITVFDLRF TAPNKDILSE KGIHTLEHLY 

        70         80         90        100        110        120 
AGFMRNHLNG DSVEIIDISP MGCRTGFYMS LIGTPSEQQV ADAWIAAMED VLKVENQNKI 

       130        140        150        160        170 
PELNEYQCGT AAMHSLDEAK QIAKNILEVG VAVNKNDELA LPESMLRELR ID 

« Hide

References

« Hide 'large scale' references
[1]"Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi: a new family of genes responsible for autoinducer production."
Surette M.G., Miller M.B., Bassler B.L.
Proc. Natl. Acad. Sci. U.S.A. 96:1639-1644(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]The Vibrio harveyi Genome Sequencing Project
Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C., Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J., Wilson R.K.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1116 / BB120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF120098 Genomic DNA. Translation: AAD17292.1.
CP000789 Genomic DNA. Translation: ABU72429.1. Different initiation.
RefSeqYP_001446656.2. NC_009783.1.

3D structure databases

ProteinModelPortalQ9Z5X1.
SMRQ9Z5X1. Positions 3-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338187.VIBHAR_03484.

Chemistry

BindingDBQ9Z5X1.
ChEMBLCHEMBL4682.

Proteomic databases

PRIDEQ9Z5X1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU72429; ABU72429; VIBHAR_03484.
GeneID5553795.
KEGGvha:VIBHAR_03484.
PATRIC20133582. VBIVibHar24526_3318.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040371.
KOK07173.
OrthoDBEOG68WRBM.

Enzyme and pathway databases

BioCycVHAR338187:GJCH-3475-MONOMER.
BRENDA4.4.1.21. 6632.
SABIO-RKQ9Z5X1.

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_VIBCB
AccessionPrimary (citable) accession number: Q9Z5X1
Secondary accession number(s): A7MYV6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 84 of the entry and version 3 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