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Q8G568

- LUXS_BIFLO

UniProt

Q8G568 - LUXS_BIFLO

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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Bifidobacterium longum (strain NCC 2705)
Status
Reviewed - Annotation score: 3 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 bindingi61 – 611IronUniRule annotation
Metal bindingi65 – 651IronUniRule annotation
Metal bindingi131 – 1311IronUniRule 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

BioCyciBLON206672:GI1E-819-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:BL1152
OrganismiBifidobacterium longum (strain NCC 2705)
Taxonomic identifieri206672 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium
ProteomesiUP000000439: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164S-ribosylhomocysteine lyasePRO_0000297985Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi206672.BL1152.

Structurei

3D structure databases

ProteinModelPortaliQ8G568.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiFIAYEAT.
OrthoDBiEOG68WRBM.
PhylomeDBiQ8G568.

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.

Q8G568-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEETAEKPV VESFQLDHTK VKAPYVRYID TETGPHGDVI SNYDLRLTQP
60 70 80 90 100
NEQAIPTGGL HTIEHTIAVL LRERIPGYID CSPFGCRTGF HLLTWGTHST
110 120 130 140 150
EDVAKALKES LEFIAYKATW DDVPATTEKS CGNYRDHSLF TAKEWAKLIL
160
EEGISSDPFE RKVV
Length:164
Mass (Da):18,451
Last modified:August 21, 2007 - v2
Checksum:iCDC4BD9D1BAA57E5
GO

Sequence cautioni

The sequence AAN24957.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014295 Genomic DNA. Translation: AAN24957.1. Different initiation.
RefSeqiNP_696321.2. NC_004307.2.

Genome annotation databases

EnsemblBacteriaiAAN24957; AAN24957; BL1152.
GeneIDi1022825.
KEGGiblo:BL1152.
PATRICi21118799. VBIBifLon107831_0862.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014295 Genomic DNA. Translation: AAN24957.1 . Different initiation.
RefSeqi NP_696321.2. NC_004307.2.

3D structure databases

ProteinModelPortali Q8G568.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 206672.BL1152.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN24957 ; AAN24957 ; BL1152 .
GeneIDi 1022825.
KEGGi blo:BL1152.
PATRICi 21118799. VBIBifLon107831_0862.

Phylogenomic databases

eggNOGi COG1854.
HOGENOMi HOG000040372.
KOi K07173.
OMAi FIAYEAT.
OrthoDBi EOG68WRBM.
PhylomeDBi Q8G568.

Enzyme and pathway databases

BioCyci BLON206672:GI1E-819-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. "The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
    Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
    Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCC 2705.

Entry informationi

Entry nameiLUXS_BIFLO
AccessioniPrimary (citable) accession number: Q8G568
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: August 21, 2007
Last modified: October 1, 2014
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3