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Q14HR4

- BIOB_FRAT1

UniProt

Q14HR4 - BIOB_FRAT1

Protein

Biotin synthase

Gene

bioB

Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (22 Aug 2006)
      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 bindingi46 – 461Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi50 – 501Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi53 – 531Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi90 – 901Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi121 – 1211Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi181 – 1811Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi256 – 2561Iron-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

    BioCyciFTUL393115:GJUT-955-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:FTF0937c
    OrganismiFrancisella tularensis subsp. tularensis (strain FSC 198)
    Taxonomic identifieri393115 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
    ProteomesiUP000001821: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Biotin synthasePRO_0000381391Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi393115.FTF0937c.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14HR4.
    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.

    Q14HR4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLQQIKEIY SRPLTELILQ ALEIHNKNFG NDIELCSLKS IKTGTCPEDC    50
    KYCPQSGHYN TSIEKHKLLD KDSILAEAKN AKDAGSKRFC MGAAWKHIPK 100
    KDFDQVAEII TEVKNLGLET CVTLGSINAD EATKLKQAGL DYYNHNLDTS 150
    REFYPEIITT RKFEERIETI RNVANADINV CCGGILGMGE SLDDRFNLLL 200
    ELLQLPAAPK SIPINTLIPI KGTPLGDKYT NAQIDSFELV RFIATTRILF 250
    PQARLRLSAG RENMSLETQT LCFLAGINSI FYGNKLLTEN NATVNSDNFL 300
    LAKLGLKSNA ELC 313
    Length:313
    Mass (Da):34,895
    Last modified:August 22, 2006 - v1
    Checksum:iE964798853D01157
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM286280 Genomic DNA. Translation: CAL08953.1.
    RefSeqiYP_667062.1. NC_008245.1.

    Genome annotation databases

    EnsemblBacteriaiCAL08953; CAL08953; FTF0937c.
    GeneIDi4199704.
    KEGGiftf:FTF0937c.
    PATRICi17960811. VBIFraTul133500_1070.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM286280 Genomic DNA. Translation: CAL08953.1 .
    RefSeqi YP_667062.1. NC_008245.1.

    3D structure databases

    ProteinModelPortali Q14HR4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 393115.FTF0937c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL08953 ; CAL08953 ; FTF0937c .
    GeneIDi 4199704.
    KEGGi ftf:FTF0937c.
    PATRICi 17960811. VBIFraTul133500_1070.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci FTUL393115:GJUT-955-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 sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
      Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
      PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: FSC 198.

    Entry informationi

    Entry nameiBIOB_FRAT1
    AccessioniPrimary (citable) accession number: Q14HR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: August 22, 2006
    Last modified: October 1, 2014
    This is version 59 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