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A9HRF2

- BIOB_GLUDA

UniProt

A9HRF2 - BIOB_GLUDA

Protein

Biotin synthase

Gene

bioB

Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 2 (01 Sep 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 bindingi51 – 511Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi55 – 551Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi96 – 961Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi127 – 1271Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi187 – 1871Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi259 – 2591Iron-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

    BioCyciGDIA272568:GJPS-3000-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:GDI2953, Gdia_3396
    OrganismiGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
    Taxonomic identifieri272568 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter
    ProteomesiUP000000736: Chromosome, UP000001176: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 316316Biotin synthasePRO_0000381409Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272568.GDI_2953.

    Structurei

    3D structure databases

    ProteinModelPortaliA9HRF2.
    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.

    A9HRF2-1 [UniParc]FASTAAdd to Basket

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    MRTDWTRDEI AALIALPFPE LMFRAQSVHR ARFDPTEIQI STLLSIKTGG    50
    CPEDCAYCPQ SAKHEDGGVK ASRLMAVEAV LKEARAARDA GAARFCMGAA 100
    WRSPKDHDLE TVCAMVEGVK SLGMETCVTL GMLDDRQAHR LREAGLDYYN 150
    HNLDTSPEHY GSIISTRTYQ ERLDTLAHVR DAGINVCCGG IVGMGENDDD 200
    RAGLIASLAS LPRHPESVPI NLLVRVAGTP LAGADPVDPI DFVRIIAAAR 250
    IAMPASRVRL AAGREDMTDE AQTLCFLAGA NSIFYGEKLL TTPNPEASRD 300
    ARLLARLGMH TSLAQA 316
    Length:316
    Mass (Da):34,213
    Last modified:September 1, 2009 - v2
    Checksum:i56B554525102199E
    GO

    Sequence cautioni

    The sequence ACI53122.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAP56896.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM889285 Genomic DNA. Translation: CAP56896.1. Different initiation.
    CP001189 Genomic DNA. Translation: ACI53122.1. Different initiation.
    RefSeqiYP_001603186.1. NC_010125.1.
    YP_002277737.1. NC_011365.1.

    Genome annotation databases

    EnsemblBacteriaiACI53122; ACI53122; Gdia_3396.
    CAP56896; CAP56896; GDI2953.
    GeneIDi5791775.
    6976842.
    KEGGigdi:GDI_2953.
    gdj:Gdia_3396.
    PATRICi22055230. VBIGluDia203729_3377.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM889285 Genomic DNA. Translation: CAP56896.1 . Different initiation.
    CP001189 Genomic DNA. Translation: ACI53122.1 . Different initiation.
    RefSeqi YP_001603186.1. NC_010125.1.
    YP_002277737.1. NC_011365.1.

    3D structure databases

    ProteinModelPortali A9HRF2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272568.GDI_2953.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI53122 ; ACI53122 ; Gdia_3396 .
    CAP56896 ; CAP56896 ; GDI2953 .
    GeneIDi 5791775.
    6976842.
    KEGGi gdi:GDI_2953.
    gdj:Gdia_3396.
    PATRICi 22055230. VBIGluDia203729_3377.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci GDIA272568:GJPS-3000-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. "Complete genome sequence of the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5."
      Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A., Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.
      , Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O., Baldani J.I., Ferreira P.C.
      BMC Genomics 10:450-450(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49037 / DSM 5601 / PAl5.
    2. "Two genome sequences of the same bacterial strain, Gluconacetobacter diazotrophicus PAl 5, suggest a new standard in genome sequence submission."
      Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.
      Stand. Genomic Sci. 2:309-317(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49037 / DSM 5601 / PAl5.

    Entry informationi

    Entry nameiBIOB_GLUDA
    AccessioniPrimary (citable) accession number: A9HRF2
    Secondary accession number(s): B5ZM22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 1, 2009
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 47 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3