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B0S194 (LUXS_FINM2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:FMG_0716
OrganismFinegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus) [Complete proteome] [HAMAP]
Taxonomic identifier334413 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XI. Incertae SedisFinegoldia

Protein attributes

Sequence length156 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 – 156156S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_1000093308

Sites

Metal binding531Iron By similarity
Metal binding571Iron By similarity
Metal binding1221Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
B0S194 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: BE5D1CA61F0010F9

FASTA15617,927
        10         20         30         40         50         60 
MNKIESFKIN HLKLMPGIYV SRKDYLGNEV LTTFDLRITA PNREPVMNTA EVHAIEHLGA 

        70         80         90        100        110        120 
TFLRNKLENE VIYFGPMGCR TGFYLILVGD KKSEDIVDLI KELFEFISNY EGEIPGQSAK 

       130        140        150 
DCGNYSDMNL SMAKFYSNKY LNVINNIKKE NLIYPE 

« Hide

References

[1]"Complete genome sequence of Finegoldia magna, an anaerobic opportunistic pathogen."
Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.
DNA Res. 15:39-47(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29328.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008971 Genomic DNA. Translation: BAG08134.1.
RefSeqYP_001692024.1. NC_010376.1.

3D structure databases

ProteinModelPortalB0S194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334413.FMG_0716.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG08134; BAG08134; FMG_0716.
GeneID6020185.
KEGGfma:FMG_0716.
PATRIC21887109. VBIFinMag33027_0921.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040372.
KOK07173.
OMAIANDIEW.
OrthoDBEOG68WRBM.

Enzyme and pathway databases

BioCycFMAG334413:GJ6M-767-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_FINM2
AccessionPrimary (citable) accession number: B0S194
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 43 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