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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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).UniRule annotation

Catalytic activityi

S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.UniRule annotation

Cofactori

Fe cationUniRule annotationNote: Binds 1 Fe cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541IronUniRule annotation
Metal bindingi58 – 581IronUniRule annotation
Metal bindingi126 – 1261IronUniRule annotation

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. S-ribosylhomocysteine lyase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. quorum sensing Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Autoinducer synthesis, Quorum sensing

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
S-ribosylhomocysteine lyaseUniRule annotation (EC:4.4.1.21UniRule annotation)
Alternative name(s):
AI-2 synthesis proteinUniRule annotation
Autoinducer-2 production protein LuxSUniRule annotation
Gene namesi
Name:luxSUniRule annotation
Ordered Locus Names:BCE_4946
OrganismiBacillus cereus (strain ATCC 10987)
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002527 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157S-ribosylhomocysteine lyasePRO_0000172205Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi222523.BCE_4946.

Structurei

3D structure databases

ProteinModelPortaliQ72YS4.
SMRiQ72YS4. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiLTKYDVR.
OrthoDBiEOG68WRBM.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamiPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFiPIRSF006160. AI2. 1 hit.
PRINTSiPR01487. LUXSPROTEIN.
ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63411. SSF63411. 1 hit.

Sequencei

Sequence statusi: Complete.

Q72YS4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSVESFELD HTIVKAPYVR HCGVHNVGSD GIVNKFDIRF CQPNKQAMKP
60 70 80 90 100
DVIHTLEHLL AFNLRKYIDR YPHFDIIDIS PMGCQTGYYL VVSGTPTVRE
110 120 130 140 150
IIDLLELTLK DAVQITEIPA ANETQCGQAK LHDLEGAKRL MNFWLSQDKD

ELEKVFG
Length:157
Mass (Da):17,856
Last modified:July 4, 2004 - v1
Checksum:i5D2BB8F36D754793
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS43847.1.
RefSeqiNP_981239.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS43847; AAS43847; BCE_4946.
KEGGibca:BCE_4946.
PATRICi18858486. VBIBacCer118379_4738.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS43847.1.
RefSeqiNP_981239.1. NC_003909.8.

3D structure databases

ProteinModelPortaliQ72YS4.
SMRiQ72YS4. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi222523.BCE_4946.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS43847; AAS43847; BCE_4946.
KEGGibca:BCE_4946.
PATRICi18858486. VBIBacCer118379_4738.

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiLTKYDVR.
OrthoDBiEOG68WRBM.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamiPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFiPIRSF006160. AI2. 1 hit.
PRINTSiPR01487. LUXSPROTEIN.
ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63411. SSF63411. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
    Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
    Nucleic Acids Res. 32:977-988(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10987.

Entry informationi

Entry nameiLUXS_BACC1
AccessioniPrimary (citable) accession number: Q72YS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 14, 2005
Last sequence update: July 4, 2004
Last modified: March 31, 2015
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.