Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

B0S194

- LUXS_FINM2

UniProt

B0S194 - LUXS_FINM2

Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Finegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi53 – 531IronUniRule annotation
    Metal bindingi57 – 571IronUniRule annotation
    Metal bindingi122 – 1221IronUniRule 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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Autoinducer synthesis, Quorum sensing

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciFMAG334413:GJ6M-767-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:FMG_0716
    OrganismiFinegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus)
    Taxonomic identifieri334413 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiales Family XI. Incertae SedisFinegoldia
    ProteomesiUP000001319: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 156156S-ribosylhomocysteine lyasePRO_1000093308Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi334413.FMG_0716.

    Structurei

    3D structure databases

    ProteinModelPortaliB0S194.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LuxS family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1854.
    HOGENOMiHOG000040372.
    KOiK07173.
    OMAiIANDIEW.
    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.

    B0S194-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKIESFKIN HLKLMPGIYV SRKDYLGNEV LTTFDLRITA PNREPVMNTA    50
    EVHAIEHLGA TFLRNKLENE VIYFGPMGCR TGFYLILVGD KKSEDIVDLI 100
    KELFEFISNY EGEIPGQSAK DCGNYSDMNL SMAKFYSNKY LNVINNIKKE 150
    NLIYPE 156
    Length:156
    Mass (Da):17,927
    Last modified:April 8, 2008 - v1
    Checksum:iBE5D1CA61F0010F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008971 Genomic DNA. Translation: BAG08134.1.
    RefSeqiYP_001692024.1. NC_010376.1.

    Genome annotation databases

    EnsemblBacteriaiBAG08134; BAG08134; FMG_0716.
    GeneIDi6020185.
    KEGGifma:FMG_0716.
    PATRICi21887109. VBIFinMag33027_0921.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP008971 Genomic DNA. Translation: BAG08134.1 .
    RefSeqi YP_001692024.1. NC_010376.1.

    3D structure databases

    ProteinModelPortali B0S194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 334413.FMG_0716.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAG08134 ; BAG08134 ; FMG_0716 .
    GeneIDi 6020185.
    KEGGi fma:FMG_0716.
    PATRICi 21887109. VBIFinMag33027_0921.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci FMAG334413:GJ6M-767-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 Finegoldia magna, an anaerobic opportunistic pathogen."
      Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.
      DNA Res. 15:39-47(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29328.

    Entry informationi

    Entry nameiLUXS_FINM2
    AccessioniPrimary (citable) accession number: B0S194
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 44 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3