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Q8X825

- BIOB_ECO57

UniProt

Q8X825 - BIOB_ECO57

Protein

Biotin synthase

Gene

bioB

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 3 (28 Jul 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 bindingi53 – 531Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi57 – 571Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi60 – 601Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi97 – 971Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi128 – 1281Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi188 – 1881Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi260 – 2601Iron-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

    BioCyciECOL386585:GJFA-852-MONOMER.
    ECOO157:BIOB-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:Z0994, ECs0853
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 346346Biotin synthasePRO_0000381359Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi155864.Z0994.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8X825.
    SMRiQ8X825. Positions 3-315.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239957.
    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.

    Q8X825-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHRPRWTLS QVTELFEKPL LDLLFEAQQV HRQHFDPRQV QVSTLLSIKT    50
    GACPEDCKYC PQSSRYKTGL EAERLMEVEQ VLESARKAKA AGSTRFCMGA 100
    AWKNPHERDM SYLEQMVQGV KAMGLEACMT LGTLSESQAQ RLANAGLDYY 150
    NHNLDTSPEF YGNIITTRTY QERLDTLEKV RDAGIKVCSG GIVGLGETVK 200
    DRAGLLLQLA NLPTPPESVP INMLVKVKGT PLADNDDVDA FDFIRTIAVA 250
    RIMMPTSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPEEDK 300
    DLQLFRKLGL NPQQTAVLAG DNEQQQRLEQ ALMTPDTDEY YNAAAL 346
    Length:346
    Mass (Da):38,638
    Last modified:July 28, 2009 - v3
    Checksum:i28BCA3F4E43B0EC5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG55146.1.
    BA000007 Genomic DNA. Translation: BAB34276.1.
    PIRiE90735.
    F85585.
    RefSeqiNP_286538.1. NC_002655.2.
    NP_308880.1. NC_002695.1.

    Genome annotation databases

    EnsemblBacteriaiAAG55146; AAG55146; Z0994.
    BAB34276; BAB34276; BAB34276.
    GeneIDi917589.
    957992.
    KEGGiece:Z0994.
    ecs:ECs0853.
    PATRICi18350736. VBIEscCol44059_0873.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG55146.1 .
    BA000007 Genomic DNA. Translation: BAB34276.1 .
    PIRi E90735.
    F85585.
    RefSeqi NP_286538.1. NC_002655.2.
    NP_308880.1. NC_002695.1.

    3D structure databases

    ProteinModelPortali Q8X825.
    SMRi Q8X825. Positions 3-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z0994.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG55146 ; AAG55146 ; Z0994 .
    BAB34276 ; BAB34276 ; BAB34276 .
    GeneIDi 917589.
    957992.
    KEGGi ece:Z0994.
    ecs:ECs0853.
    PATRICi 18350736. VBIEscCol44059_0873.

    Phylogenomic databases

    eggNOGi COG0502.
    HOGENOMi HOG000239957.
    KOi K01012.
    OMAi RIMMPAS.
    OrthoDBi EOG622PMP.

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci ECOL386585:GJFA-852-MONOMER.
    ECOO157:BIOB-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: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiBIOB_ECO57
    AccessioniPrimary (citable) accession number: Q8X825
    Secondary accession number(s): Q7AGD7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 83 of the entry and version 3 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