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Q9RRU8

- LUXS_DEIRA

UniProt

Q9RRU8 - LUXS_DEIRA

Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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).

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi57 – 571Iron
    Metal bindingi61 – 611Iron
    Metal bindingi125 – 1251Iron

    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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Autoinducer synthesis, Quorum sensing

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciDRAD243230:GH46-2436-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:DR_2387
    OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
    Taxonomic identifieri243230 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
    ProteomesiUP000002524: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 158158S-ribosylhomocysteine lyasePRO_0000172218Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi243230.DR_2387.

    Structurei

    Secondary structure

    1
    158
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113
    Turni14 – 163
    Beta strandi19 – 2911
    Beta strandi35 – 428
    Helixi53 – 7018
    Beta strandi74 – 796
    Beta strandi83 – 9311
    Helixi96 – 11116
    Turni122 – 1243
    Turni126 – 1294
    Helixi133 – 14614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1INNX-ray1.80A/B1-158[»]
    1J6VX-ray2.10A1-158[»]
    1VGXX-ray1.90A/B1-158[»]
    1VH2X-ray2.00A1-158[»]
    1VJEX-ray1.64A/B1-158[»]
    ProteinModelPortaliQ9RRU8.
    SMRiQ9RRU8. Positions 7-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9RRU8.

    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.

    Q9RRU8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPDMANVESF DLDHTKVKAP YVRLAGVKTT PKGDQISKYD LRFLQPNQGA    50
    IDPAAIHTLE HLLAGYMRDH LEGVVDVSPM GCRTGMYMAV IGEPDEQGVM 100
    KAFEAALKDT AGHDQPIPGV SELECGNYRD HDLAAARQHA RDVLDQGLKV 150
    QETILLER 158
    Length:158
    Mass (Da):17,395
    Last modified:May 1, 2000 - v1
    Checksum:i174CC86C50FB714F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF11932.1.
    PIRiD75280.
    RefSeqiNP_296108.1. NC_001263.1.
    WP_010889013.1. NC_001263.1.

    Genome annotation databases

    EnsemblBacteriaiAAF11932; AAF11932; DR_2387.
    GeneIDi1797935.
    KEGGidra:DR_2387.
    PATRICi21632492. VBIDeiRad64572_2623.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000513 Genomic DNA. Translation: AAF11932.1 .
    PIRi D75280.
    RefSeqi NP_296108.1. NC_001263.1.
    WP_010889013.1. NC_001263.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1INN X-ray 1.80 A/B 1-158 [» ]
    1J6V X-ray 2.10 A 1-158 [» ]
    1VGX X-ray 1.90 A/B 1-158 [» ]
    1VH2 X-ray 2.00 A 1-158 [» ]
    1VJE X-ray 1.64 A/B 1-158 [» ]
    ProteinModelPortali Q9RRU8.
    SMRi Q9RRU8. Positions 7-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243230.DR_2387.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF11932 ; AAF11932 ; DR_2387 .
    GeneIDi 1797935.
    KEGGi dra:DR_2387.
    PATRICi 21632492. VBIDeiRad64572_2623.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DRAD243230:GH46-2436-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9RRU8.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
    2. "A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs."
      Lewis H.A., Furlong E.B., Laubert B., Eroshkina G.A., Batiyenko Y., Adams J.M., Bergseid M.G., Marsh C.D., Peat T.S., Sanderson W.E., Sauder J.M., Buchanan S.G.
      Structure 9:527-537(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

    Entry informationi

    Entry nameiLUXS_DEIRA
    AccessioniPrimary (citable) accession number: Q9RRU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 91 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3