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Q5PF11 (LUXS_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. 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:SPA2675
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length171 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) 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

Initiator methionine11Removed By similarity
Chain2 – 171170S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_0000172247

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q5PF11 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 359A88331FF56CDF

FASTA17119,308
        10         20         30         40         50         60 
MPLLDSFAVD HTRMQAPAVR VAKTMNTPHG DAITVFDLRF CIPNKEVMPE KGIHTLEHLF 

        70         80         90        100        110        120 
AGFMRDHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV ADAWKAAMAD VLKVQDQNQI 

       130        140        150        160        170 
PELNVYQCGT YQMHSLSEAQ DIARHILERD VRVNSNKELA LPKEKLQELH I 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV78537.1.
RefSeqYP_151849.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PF11.
SMRQ5PF11. Positions 3-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA2675.

Proteomic databases

PRIDEQ5PF11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV78537; AAV78537; SPA2675.
PATRIC32354898. VBISalEnt134188_2851.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040371.
OMARFKQPNQ.
OrthoDBEOG68WRBM.
ProtClustDBPRK02260.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-2673-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_SALPA
AccessionPrimary (citable) accession number: Q5PF11
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 57 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