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Q731I2

- BIOB_BACC1

UniProt

Q731I2 - BIOB_BACC1

Protein

Biotin synthase

Gene

bioB

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 bindingi71 – 711Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi75 – 751Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi78 – 781Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi115 – 1151Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi147 – 1471Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi207 – 2071Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi277 – 2771Iron-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

    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:BCE_4184
    OrganismiBacillus cereus (strain ATCC 10987)
    Taxonomic identifieri222523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000002527: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 332332Biotin synthasePRO_0000381219Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi222523.BCE_4184.

    Structurei

    3D structure databases

    ProteinModelPortaliQ731I2.
    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.

    Q731I2-1 [UniParc]FASTAAdd to Basket

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    MKQVQTKRDW KKLAYDVVEE KVITKEDAIA ILEADDTEIL EIMNAAYIIR    50
    HHHFGKKVKL NMIINTKSGL CPEDCGYCSQ SIISEAPIDK YAWLTQEKIV 100
    EGAHEAIRRK AGTYCIVASG RRPTDKEVNH VIGAVKEIRE TTDLKICCCL 150
    GFLNEDQAGR LAEAGVHRYN HNLNTHVNNY ESICSTHTYD DRVDTVQKAK 200
    QAGISPCSGA IFGMGETIEE RAEIAFELQR IDADSIPCNF LVAVKGTPLE 250
    GQKELTPVEC LKVLAMMRFV NPTKEIRISG GREINLRSVQ PIGLFAANSI 300
    FVGDYLTTAG QEPTADWGMI EDLGFEIEEC AL 332
    Length:332
    Mass (Da):36,980
    Last modified:July 5, 2004 - v1
    Checksum:i4357805DB937F2A4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS43085.1.
    RefSeqiNP_980477.1. NC_003909.8.

    Genome annotation databases

    EnsemblBacteriaiAAS43085; AAS43085; BCE_4184.
    GeneIDi2748937.
    KEGGibca:BCE_4184.
    PATRICi18857017. VBIBacCer118379_4007.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS43085.1 .
    RefSeqi NP_980477.1. NC_003909.8.

    3D structure databases

    ProteinModelPortali Q731I2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 222523.BCE_4184.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS43085 ; AAS43085 ; BCE_4184 .
    GeneIDi 2748937.
    KEGGi bca:BCE_4184.
    PATRICi 18857017. VBIBacCer118379_4007.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .

    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. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
      Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
      Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10987.

    Entry informationi

    Entry nameiBIOB_BACC1
    AccessioniPrimary (citable) accession number: Q731I2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 78 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