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Q051U2

- BIOB_LEPBL

UniProt

Q051U2 - BIOB_LEPBL

Protein

Biotin synthase

Gene

bioB

Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain L550)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (14 Nov 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.UniRule annotation

    Catalytic activityi

    Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

    Cofactori

    Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation
    Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi74 – 741Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi77 – 771Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi114 – 1141Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi146 – 1461Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi206 – 2061Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi276 – 2761Iron-sulfur 2 (2Fe-2S)UniRule annotation

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    3. biotin synthase activity Source: UniProtKB-HAMAP
    4. iron ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. biotin biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Biotin biosynthesis

    Keywords - Ligandi

    2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciLBOR355276:GHUQ-1402-MONOMER.
    UniPathwayiUPA00078; UER00162.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
    Gene namesi
    Name:bioBUniRule annotation
    Ordered Locus Names:LBL_1414
    OrganismiLeptospira borgpetersenii serovar Hardjo-bovis (strain L550)
    Taxonomic identifieri355276 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000000655: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 358358Biotin synthasePRO_0000381444Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi355276.LBL_1414.

    Structurei

    3D structure databases

    ProteinModelPortaliQ051U2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the radical SAM superfamily. Biotin synthase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239958.
    KOiK01012.
    OMAiCKEDCIF.
    OrthoDBiEOG622PMP.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01694. BioB.
    InterProiIPR013785. Aldolase_TIM.
    IPR010722. BATS_dom.
    IPR002684. Biotin_synth/BioAB.
    IPR024177. Biotin_synthase.
    IPR006638. Elp3/MiaB/NifB.
    IPR007197. rSAM.
    [Graphical view]
    PfamiPF06968. BATS. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001619. Biotin_synth. 1 hit.
    SMARTiSM00876. BATS. 1 hit.
    SM00729. Elp3. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00433. bioB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q051U2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEKMYATLK TAEKIFSEIS SVITKQEGLE ILNGSIPLTT CLDKAFQERN    50
    RYFYNKVRIH ILDNIKNGYC PEDCGYCAQR KNANSGIKEY PMKSEAEIYE 100
    DAVQAKKNGA YRFCMVTSGT GPNRLTTERL ASTIRRITNE LGMKVCLSAG 150
    LLDEEKAQVL KSAGLDRYNH NLNTSENHYP EICDTHTYAQ RTQTLDSVSK 200
    AGIGMCSGVI VGMGESFQDI VDMAFELKSF RVISIPVNFF IPVKGHAIKN 250
    PGILTPELCV RILCLFRLVN PDSEIRIAAG REGHLRSLSA MALFAANSLF 300
    SSGYLNVKGS EIIETVTMIR DAGFVPELVD GGILPEESGT EMLYSEKNFP 350
    ELYKFKKS 358
    Length:358
    Mass (Da):39,844
    Last modified:November 14, 2006 - v1
    Checksum:i77B9930EF3CF4746
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000348 Genomic DNA. Translation: ABJ78903.1.
    RefSeqiWP_011670109.1. NC_008508.1.
    YP_797836.1. NC_008508.1.

    Genome annotation databases

    EnsemblBacteriaiABJ78903; ABJ78903; LBL_1414.
    GeneIDi4407278.
    KEGGilbl:LBL_1414.
    PATRICi22366650. VBILepBor75619_1784.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000348 Genomic DNA. Translation: ABJ78903.1 .
    RefSeqi WP_011670109.1. NC_008508.1.
    YP_797836.1. NC_008508.1.

    3D structure databases

    ProteinModelPortali Q051U2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 355276.LBL_1414.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ78903 ; ABJ78903 ; LBL_1414 .
    GeneIDi 4407278.
    KEGGi lbl:LBL_1414.
    PATRICi 22366650. VBILepBor75619_1784.

    Phylogenomic databases

    eggNOGi COG0502.
    HOGENOMi HOG000239958.
    KOi K01012.
    OMAi CKEDCIF.
    OrthoDBi EOG622PMP.

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci LBOR355276:GHUQ-1402-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01694. BioB.
    InterProi IPR013785. Aldolase_TIM.
    IPR010722. BATS_dom.
    IPR002684. Biotin_synth/BioAB.
    IPR024177. Biotin_synthase.
    IPR006638. Elp3/MiaB/NifB.
    IPR007197. rSAM.
    [Graphical view ]
    Pfami PF06968. BATS. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001619. Biotin_synth. 1 hit.
    SMARTi SM00876. BATS. 1 hit.
    SM00729. Elp3. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00433. bioB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: L550.

    Entry informationi

    Entry nameiBIOB_LEPBL
    AccessioniPrimary (citable) accession number: Q051U2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: November 14, 2006
    Last modified: October 1, 2014
    This is version 55 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3