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Q5X592

- BIOB_LEGPA

UniProt

Q5X592 - BIOB_LEGPA

Protein

Biotin synthase

Gene

bioB

Organism
Legionella pneumophila (strain Paris)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      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 bindingi54 – 541Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi61 – 611Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi98 – 981Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi129 – 1291Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi189 – 1891Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi261 – 2611Iron-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

    BioCyciLPNE297246:GCO9-1813-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:lpp1428
    OrganismiLegionella pneumophila (strain Paris)
    Taxonomic identifieri297246 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
    ProteomesiUP000000610: Chromosome

    Organism-specific databases

    LegioListilpp1428.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 315315Biotin synthasePRO_0000381438Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi297246.lpp1428.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5X592.
    SMRiQ5X592. Positions 6-313.
    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.

    Q5X592-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEEKKQWSI SDIEAIYQQP FNDLLYQAHT IHRTYHDPNS LQFATLLSIK    50
    TGACPEDCGY CSQSGHYKTH VEKEKLMSVE EVLQCAKEAK EGGAKRFCMG 100
    AAWRCPPDKA IPQLKEMIEG VKSLGLETCM TLGMLTKEQA SHLKEAGLDY 150
    YNHNIDTSPS YYDKVVTTRK FSDRLDTLNN VRSAGINVCC GGILGLGETR 200
    EDRIEFLLTL ANMETPPESV PINRLIPVEG TPLAQAERVE GIELVRTIAT 250
    ARILMPKSAI RLTAGRTEMS DELQALCYFA GANSVFIGDK LLTEDNPQRF 300
    KDKTLFNKLG LTEMV 315
    Length:315
    Mass (Da):35,177
    Last modified:November 23, 2004 - v1
    Checksum:i5A48E1A8F2153AB0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628336 Genomic DNA. Translation: CAH12579.1.
    RefSeqiYP_123752.1. NC_006368.1.

    Genome annotation databases

    EnsemblBacteriaiCAH12579; CAH12579; lpp1428.
    GeneIDi3117229.
    KEGGilpp:lpp1428.
    PATRICi22323235. VBILegPne27771_1676.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR628336 Genomic DNA. Translation: CAH12579.1 .
    RefSeqi YP_123752.1. NC_006368.1.

    3D structure databases

    ProteinModelPortali Q5X592.
    SMRi Q5X592. Positions 6-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 297246.lpp1428.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAH12579 ; CAH12579 ; lpp1428 .
    GeneIDi 3117229.
    KEGGi lpp:lpp1428.
    PATRICi 22323235. VBILegPne27771_1676.

    Organism-specific databases

    LegioListi lpp1428.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci LPNE297246:GCO9-1813-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. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
      Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
      Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Paris.

    Entry informationi

    Entry nameiBIOB_LEGPA
    AccessioniPrimary (citable) accession number: Q5X592
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 72 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