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B7HAY7

- BIOB_BACC4

UniProt

B7HAY7 - BIOB_BACC4

Protein

Biotin synthase

Gene

bioB

Organism
Bacillus cereus (strain B4264)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (10 Feb 2009)
      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

    BioCyciBCER405532:GI1K-4186-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:BCB4264_A4225
    OrganismiBacillus cereus (strain B4264)
    Taxonomic identifieri405532 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000007096: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 332332Biotin synthasePRO_0000381221Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi405532.BCB4264_A4225.

    Structurei

    3D structure databases

    ProteinModelPortaliB7HAY7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239958.
    KOiK01012.
    OMAiRIMMPAS.
    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.

    B7HAY7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKQVQTKRDW KKLAYDVVEE KMITKEDAIA ILEADDTEVL EIMNAAYIIR    50
    HHHFGKKVKL NMIINTKSGL CPEDCGYCSQ SIISEAPIDK YAWLTQEKIV 100
    EGAHEAIRRK AGTYCIVASG RRPTDKEVNH VIGAVKEIRE TTDLKICCCL 150
    GFLNEDQAGL LAEAGVHRYN HNLNTHANNY DSICSTHTYD DRVDTVQKAK 200
    QAGISPCSGA IFGMGETIEE RAEIAFELQR IDADSIPCNF LVAVKGTPLE 250
    GQKELTPVDC LKVLAMMRFV NPTKEIRISG GREINLRSVQ PIGLFAANSI 300
    FVGDYLTTAG QEPTADWGMI ADLGFEIEEC AL 332
    Length:332
    Mass (Da):36,841
    Last modified:February 10, 2009 - v1
    Checksum:iCB98AF00F74FC7B2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001176 Genomic DNA. Translation: ACK62962.1.
    RefSeqiYP_002368919.1. NC_011725.1.

    Genome annotation databases

    EnsemblBacteriaiACK62962; ACK62962; BCB4264_A4225.
    GeneIDi7096255.
    KEGGibcb:BCB4264_A4225.
    PATRICi18880343. VBIBacCer117876_4078.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001176 Genomic DNA. Translation: ACK62962.1 .
    RefSeqi YP_002368919.1. NC_011725.1.

    3D structure databases

    ProteinModelPortali B7HAY7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405532.BCB4264_A4225.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACK62962 ; ACK62962 ; BCB4264_A4225 .
    GeneIDi 7096255.
    KEGGi bcb:BCB4264_A4225.
    PATRICi 18880343. VBIBacCer117876_4078.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci BCER405532:GI1K-4186-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. "Genome sequence of Bacillus cereus B4264."
      Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
      Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: B4264.

    Entry informationi

    Entry nameiBIOB_BACC4
    AccessioniPrimary (citable) accession number: B7HAY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 40 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