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B1IHH9

- BIOB_CLOBK

UniProt

B1IHH9 - BIOB_CLOBK

Protein

Biotin synthase

Gene

bioB

Organism
Clostridium botulinum (strain Okra / Type B1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      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 bindingi62 – 621Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi106 – 1061Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi138 – 1381Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi198 – 1981Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi268 – 2681Iron-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

    BioCyciCBOT498213:GCNI-2294-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:CLD_2316
    OrganismiClostridium botulinum (strain Okra / Type B1)
    Taxonomic identifieri498213 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000008541: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 318318Biotin synthasePRO_0000381314Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi498213.CLD_2316.

    Structurei

    3D structure databases

    ProteinModelPortaliB1IHH9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239958.
    KOiK01012.
    OMAiTCENTLR.
    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.

    B1IHH9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNIIKYKKK ILNGDLLTKE EVEELLEEDI TDLAATANEI RESLCGNKFD    50
    LCTIINGKSG RCQENCKYCA QSAHFDTDII EYNILNSDRI MNSAISNYNK 100
    GVHRFSVVTS GRALNNNEVD TLCKTYLKLK ETCSIRLCAS HGLLKYEDLK 150
    RLKDSGVTRY HNNLETSRKF FTKICTTHKY DDKIETIKNA KKAGFEICSG 200
    GIIGLGETME DRIDMAFTLR ELSVESVPVN ILNPIKGTPL ENQEILSYEE 250
    IIKTLALFRF ILPTVQIRLA GGRTIISDKG KKALESGVNG AISGDMLTTL 300
    GIETSEDIKM IKNLGFEV 318
    Length:318
    Mass (Da):35,584
    Last modified:April 29, 2008 - v1
    Checksum:i867B09F25FEC2E29
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000939 Genomic DNA. Translation: ACA43727.1.
    RefSeqiYP_001781871.1. NC_010516.1.

    Genome annotation databases

    EnsemblBacteriaiACA43727; ACA43727; CLD_2316.
    GeneIDi6150942.
    KEGGicbb:CLD_2316.
    PATRICi19404910. VBICloBot127283_2359.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000939 Genomic DNA. Translation: ACA43727.1 .
    RefSeqi YP_001781871.1. NC_010516.1.

    3D structure databases

    ProteinModelPortali B1IHH9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 498213.CLD_2316.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACA43727 ; ACA43727 ; CLD_2316 .
    GeneIDi 6150942.
    KEGGi cbb:CLD_2316.
    PATRICi 19404910. VBICloBot127283_2359.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci CBOT498213:GCNI-2294-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. "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
      Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
      PLoS ONE 2:E1271-E1271(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Okra / Type B1.

    Entry informationi

    Entry nameiBIOB_CLOBK
    AccessioniPrimary (citable) accession number: B1IHH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 45 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