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P45578

- LUXS_ECOLI

UniProt

P45578 - LUXS_ECOLI

Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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).2 Publications

    Catalytic activityi

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

    Cofactori

    Binds 1 iron ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi54 – 541IronBy similarity
    Metal bindingi58 – 581IronBy similarity
    Metal bindingi128 – 1281IronBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell-cell signaling involved in quorum sensing Source: EcoCyc
    2. L-methionine biosynthetic process from S-adenosylmethionine Source: EcoCyc

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Autoinducer synthesis, Quorum sensing

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG12712-MONOMER.
    ECOL316407:JW2662-MONOMER.
    MetaCyc:EG12712-MONOMER.
    BRENDAi4.4.1.21. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-ribosylhomocysteine lyase (EC:4.4.1.21)
    Alternative name(s):
    AI-2 synthesis protein
    Autoinducer-2 production protein LuxS
    Gene namesi
    Name:luxS
    Synonyms:ygaG
    Ordered Locus Names:b2687, JW2662
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12712. luxS.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 171170S-ribosylhomocysteine lyasePRO_0000172220Add
    BLAST

    Proteomic databases

    PaxDbiP45578.
    PRIDEiP45578.

    2D gel databases

    SWISS-2DPAGEP45578.

    Expressioni

    Gene expression databases

    GenevestigatoriP45578.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dnaKP0A6Y81EBI-562313,EBI-542092

    Protein-protein interaction databases

    DIPiDIP-10131N.
    IntActiP45578. 5 interactions.
    STRINGi511145.b2687.

    Structurei

    3D structure databases

    ProteinModelPortaliP45578.
    SMRiP45578. Positions 3-161.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LuxS family.Curated

    Phylogenomic databases

    eggNOGiCOG1854.
    HOGENOMiHOG000040371.
    KOiK07173.
    OMAiRDHLNSD.
    OrthoDBiEOG68WRBM.
    PhylomeDBiP45578.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P45578-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE    50
    RGIHTLEHLF AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV 100
    ADAWKAAMED VLKVQDQNQI PELNVYQCGT YQMHSLQEAQ DIARSILERD 150
    VRINSNEELA LPKEKLQELH I 171
    Length:171
    Mass (Da):19,416
    Last modified:January 23, 2007 - v3
    Checksum:i131F57F1866DA105
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311D → E in AAB40286. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75734.1.
    AP009048 Genomic DNA. Translation: BAA16549.1.
    U83186 Genomic DNA. Translation: AAB40286.1.
    M86657 Genomic DNA. No translation available.
    PIRiH65048.
    RefSeqiNP_417172.1. NC_000913.3.
    YP_490901.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75734; AAC75734; b2687.
    BAA16549; BAA16549; BAA16549.
    GeneIDi12934186.
    947168.
    KEGGiecj:Y75_p2630.
    eco:b2687.
    PATRICi32120768. VBIEscCol129921_2781.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75734.1 .
    AP009048 Genomic DNA. Translation: BAA16549.1 .
    U83186 Genomic DNA. Translation: AAB40286.1 .
    M86657 Genomic DNA. No translation available.
    PIRi H65048.
    RefSeqi NP_417172.1. NC_000913.3.
    YP_490901.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P45578.
    SMRi P45578. Positions 3-161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10131N.
    IntActi P45578. 5 interactions.
    STRINGi 511145.b2687.

    Chemistry

    BindingDBi P45578.
    ChEMBLi CHEMBL3496.

    2D gel databases

    SWISS-2DPAGE P45578.

    Proteomic databases

    PaxDbi P45578.
    PRIDEi P45578.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75734 ; AAC75734 ; b2687 .
    BAA16549 ; BAA16549 ; BAA16549 .
    GeneIDi 12934186.
    947168.
    KEGGi ecj:Y75_p2630.
    eco:b2687.
    PATRICi 32120768. VBIEscCol129921_2781.

    Organism-specific databases

    EchoBASEi EB2573.
    EcoGenei EG12712. luxS.

    Phylogenomic databases

    eggNOGi COG1854.
    HOGENOMi HOG000040371.
    KOi K07173.
    OMAi RDHLNSD.
    OrthoDBi EOG68WRBM.
    PhylomeDBi P45578.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG12712-MONOMER.
    ECOL316407:JW2662-MONOMER.
    MetaCyc:EG12712-MONOMER.
    BRENDAi 4.4.1.21. 2026.

    Miscellaneous databases

    PROi P45578.

    Gene expression databases

    Genevestigatori P45578.

    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. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-76.
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Emr, an Escherichia coli locus for multidrug resistance."
      Lomovskaya O., Lewis K.
      Proc. Natl. Acad. Sci. U.S.A. 89:8938-8942(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-171.
    6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10.
      Strain: K12 / EMG2.
    7. "Detection of new genes in a bacterial genome using Markov models for three gene classes."
      Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.
      Nucleic Acids Res. 23:3554-3562(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    8. "Quorum sensing in Escherichia coli and Salmonella typhimurium."
      Surette M.G., Bassler B.L.
      Proc. Natl. Acad. Sci. U.S.A. 95:7046-7050(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Quorum sensing in Escherichia coli, Salmonella typhimurium, and Vibrio harveyi: a new family of genes responsible for autoinducer production."
      Surette M.G., Miller M.B., Bassler B.L.
      Proc. Natl. Acad. Sci. U.S.A. 96:1639-1644(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiLUXS_ECOLI
    AccessioniPrimary (citable) accession number: P45578
    Secondary accession number(s): P77134, P77805
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    E.coli strain DH5-alpha does not make AI-2; it has a frameshift mutation in the luxS gene that disrupts the protein coding region.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3