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B9J289

- LUXS_BACCQ

UniProt

B9J289 - LUXS_BACCQ

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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Bacillus cereus (strain Q1)
Status
Reviewed - 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

Binds 1 iron ion 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

Enzyme and pathway databases

BioCyciBCER361100:GJ7M-4594-MONOMER.

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:BCQ_4606
OrganismiBacillus cereus (strain Q1)
Taxonomic identifieri361100 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000000441: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157S-ribosylhomocysteine lyasePRO_1000118534Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi361100.BCQ_4606.

Structurei

3D structure databases

ProteinModelPortaliB9J289.
SMRiB9J289. Positions 4-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiRDHLNSD.
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.

B9J289-1 [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:March 24, 2009 - v1
Checksum:i5D2BB8F36D754793
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000227 Genomic DNA. Translation: ACM15032.1.
RefSeqiYP_002532321.1. NC_011969.1.

Genome annotation databases

EnsemblBacteriaiACM15032; ACM15032; BCQ_4606.
GeneIDi7376637.
KEGGibcq:BCQ_4606.
PATRICi18917007. VBIBacCer120424_4668.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000227 Genomic DNA. Translation: ACM15032.1 .
RefSeqi YP_002532321.1. NC_011969.1.

3D structure databases

ProteinModelPortali B9J289.
SMRi B9J289. Positions 4-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 361100.BCQ_4606.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACM15032 ; ACM15032 ; BCQ_4606 .
GeneIDi 7376637.
KEGGi bcq:BCQ_4606.
PATRICi 18917007. VBIBacCer120424_4668.

Phylogenomic databases

eggNOGi COG1854.
HOGENOMi HOG000040372.
KOi K07173.
OMAi RDHLNSD.
OrthoDBi EOG68WRBM.

Enzyme and pathway databases

BioCyci BCER361100:GJ7M-4594-MONOMER.

Family and domain databases

Gene3Di 3.30.1360.80. 1 hit.
HAMAPi MF_00091. LuxS.
InterProi IPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view ]
Pfami PF02664. LuxS. 1 hit.
[Graphical view ]
PIRSFi PIRSF006160. AI2. 1 hit.
PRINTSi PR01487. LUXSPROTEIN.
ProDomi PD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF63411. SSF63411. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
    Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
    J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Q1.

Entry informationi

Entry nameiLUXS_BACCQ
AccessioniPrimary (citable) accession number: B9J289
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: October 1, 2014
This is version 35 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