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A1V817

- BIOB_BURMS

UniProt

A1V817 - BIOB_BURMS

Protein

Biotin synthase

Gene

bioB

Organism
Burkholderia mallei (strain SAVP1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      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

    BioCyciBMAL320388:GHFL-3076-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:BMASAVP1_A3077
    OrganismiBurkholderia mallei (strain SAVP1)
    Taxonomic identifieri320388 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
    ProteomesiUP000006708: Chromosome I

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 336336Biotin synthasePRO_0000381268Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi320388.BMASAVP1_A3077.

    Structurei

    3D structure databases

    ProteinModelPortaliA1V817.
    SMRiA1V817. 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.
    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.

    A1V817-1 [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:February 6, 2007 - v1
    Checksum:iEA07331837FB0837
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000526 Genomic DNA. Translation: ABM52397.1.
    RefSeqiYP_994370.1. NC_008785.1.

    Genome annotation databases

    EnsemblBacteriaiABM52397; ABM52397; BMASAVP1_A3077.
    GeneIDi4679631.
    KEGGibmv:BMASAVP1_A3077.
    PATRICi19158837. VBIBurMal134057_4657.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000526 Genomic DNA. Translation: ABM52397.1 .
    RefSeqi YP_994370.1. NC_008785.1.

    3D structure databases

    ProteinModelPortali A1V817.
    SMRi A1V817. Positions 21-330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 320388.BMASAVP1_A3077.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM52397 ; ABM52397 ; BMASAVP1_A3077 .
    GeneIDi 4679631.
    KEGGi bmv:BMASAVP1_A3077.
    PATRICi 19158837. VBIBurMal134057_4657.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci BMAL320388:GHFL-3076-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 (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SAVP1.

    Entry informationi

    Entry nameiBIOB_BURMS
    AccessioniPrimary (citable) accession number: A1V817
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 52 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