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A9R3C8

- BIOB_YERPG

UniProt

A9R3C8 - BIOB_YERPG

Protein

Biotin synthase

Gene

bioB

Organism
Yersinia pestis bv. Antiqua (strain Angola)
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 1 (05 Feb 2008)
      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

    BioCyciYPES349746:GHPB-1428-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:YpAngola_A1425
    OrganismiYersinia pestis bv. Antiqua (strain Angola)
    Taxonomic identifieri349746 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000001204: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345Biotin synthasePRO_0000381724Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi349746.YpAngola_A1425.

    Structurei

    3D structure databases

    ProteinModelPortaliA9R3C8.
    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.

    A9R3C8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATYHHWTVG QALALFDKPL LELLFEAQQV HRQHFDPRQV QVSTLLSIKT    50
    GACPEDCKYC PQSSRYKTGL ESERLMQVEQ VLESAKKAKA AGSTRFCMGA 100
    AWKNPHERDM PYLAKMVEGV KALGMETCMT LGSLSKQQAH RLADAGLDYY 150
    NHNLDTSPEF YGSIITTRSY QERLDTLNEV RDAGIKVCSG GIVGLGETVR 200
    DRAGLLVQLA NLPKPPESVP INMLVKVKGT PLENNAEVDA FEFIRTIAVA 250
    RIMMPSSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPDEDK 300
    DLQLFRKLGL NPQQTATSHG DREQQQALTE QLLHGDTAQF YNAAV 345
    Length:345
    Mass (Da):38,378
    Last modified:February 5, 2008 - v1
    Checksum:i5E947F85B26780A1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX85289.1.
    RefSeqiYP_001605944.1. NC_010159.1.

    Genome annotation databases

    EnsemblBacteriaiABX85289; ABX85289; YpAngola_A1425.
    GeneIDi5799892.
    KEGGiypg:YpAngola_A1425.
    PATRICi18571979. VBIYerPes97331_1779.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000901 Genomic DNA. Translation: ABX85289.1 .
    RefSeqi YP_001605944.1. NC_010159.1.

    3D structure databases

    ProteinModelPortali A9R3C8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 349746.YpAngola_A1425.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX85289 ; ABX85289 ; YpAngola_A1425 .
    GeneIDi 5799892.
    KEGGi ypg:YpAngola_A1425.
    PATRICi 18571979. VBIYerPes97331_1779.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci YPES349746:GHPB-1428-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 sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
      Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
      J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Angola.

    Entry informationi

    Entry nameiBIOB_YERPG
    AccessioniPrimary (citable) accession number: A9R3C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 51 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