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A2S7R3

- BIOB_BURM9

UniProt

A2S7R3 - BIOB_BURM9

Protein

Biotin synthase

Gene

bioB

Organism
Burkholderia mallei (strain NCTC 10229)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 2 (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 bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi76 – 761Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi113 – 1131Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi144 – 1441Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi204 – 2041Iron-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

    BioCyciBMAL412022:GJI8-2017-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:BMA10229_A2017
    OrganismiBurkholderia mallei (strain NCTC 10229)
    Taxonomic identifieri412022 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000002283: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 336336Biotin synthasePRO_0000381266Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi412022.BMA10229_A2017.

    Structurei

    3D structure databases

    ProteinModelPortaliA2S7R3.
    SMRiA2S7R3. Positions 21-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239957.
    KOiK01012.
    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.

    A2S7R3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEAQTACAT TETPVAAPAA PRWRVADVIA LYELPFNDLL FRAQQTHREH    50
    FDANAIQLST LLSIKTGGCE EDCGYCSQSA HHDTGLKAEK LMEVDAVLAA 100
    ARTAKENGAT RFCMGAAWRN PKDRHIEPIK EMIRGVKDMG LETCVTLGML 150
    EEHQAKALAE AGLDYYNHNL DTSPEFYGQI ISTRTYQDRL DTLERVRDAG 200
    INVCCGGIIG MGESRRERAG LIAQLANMNP YPESVPINNL VAIEGTPLEN 250
    AQALDPFEFV RTIAVARITM PKAMVRLSAG REQLDDAMQA LCFLAGANSM 300
    FYGDVLLTTG NPRAEADRKL LARLGMSASE ASQLSA 336
    Length:336
    Mass (Da):36,668
    Last modified:July 28, 2009 - v2
    Checksum:iEA07331837FB0837
    GO

    Sequence cautioni

    The sequence ABN00616.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000546 Genomic DNA. Translation: ABN00616.1. Different initiation.
    RefSeqiYP_001027982.1. NC_008836.1.

    Genome annotation databases

    EnsemblBacteriaiABN00616; ABN00616; BMA10229_A2017.
    GeneIDi4791516.
    KEGGibml:BMA10229_A2017.
    PATRICi19135010. VBIBurMal46188_4211.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000546 Genomic DNA. Translation: ABN00616.1 . Different initiation.
    RefSeqi YP_001027982.1. NC_008836.1.

    3D structure databases

    ProteinModelPortali A2S7R3.
    SMRi A2S7R3. Positions 21-330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 412022.BMA10229_A2017.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN00616 ; ABN00616 ; BMA10229_A2017 .
    GeneIDi 4791516.
    KEGGi bml:BMA10229_A2017.
    PATRICi 19135010. VBIBurMal46188_4211.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci BMAL412022:GJI8-2017-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. DeShazer D., Woods D.E., Nierman W.C.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 10229.

    Entry informationi

    Entry nameiBIOB_BURM9
    AccessioniPrimary (citable) accession number: A2S7R3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 51 of the entry and version 2 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