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B1YKZ3 (LUXS_EXIS2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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:Exig_2345
OrganismExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15) [Complete proteome] [HAMAP]
Taxonomic identifier262543 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length154 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 – 154154S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_1000093307

Sites

Metal binding571Iron By similarity
Metal binding611Iron By similarity
Metal binding1241Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YKZ3 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 9768A7A6B2E27131

FASTA15417,540
        10         20         30         40         50         60 
MTIKKMNVES FNLDHTKVKA PYIRVAGYKD GKVDQVVKYD IRFTQPNVEQ MPMRAMHTLE 

        70         80         90        100        110        120 
HLLAENIRNY SDDVIDVSPM GCQTGFYMAM MNFDSVEKMS ELVEKTLKDV LAAEEIPAQN 

       130        140        150 
EVQCGFASAH DLKGAKHYAE KMLAGRDEWD IVFG 

« Hide

References

[1]"Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17290 / JCM 13490 / 255-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001022 Genomic DNA. Translation: ACB61795.1.
RefSeqYP_001814812.1. NC_010556.1.

3D structure databases

ProteinModelPortalB1YKZ3.
SMRB1YKZ3. Positions 5-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262543.Exig_2345.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB61795; ACB61795; Exig_2345.
GeneID6175326.
KEGGesi:Exig_2345.
PATRIC32138324. VBIExiSib53410_2384.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040372.
KOK07173.
OMALTKYDVR.
OrthoDBEOG68WRBM.
ProtClustDBPRK02260.

Enzyme and pathway databases

BioCycESIB262543:GHBP-2425-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_EXIS2
AccessionPrimary (citable) accession number: B1YKZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: April 16, 2014
This is version 41 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