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Q0I355

- BIOB_HISS1

UniProt

Q0I355 - BIOB_HISS1

Protein

Biotin synthase

Gene

bioB

Organism
Histophilus somni (strain 129Pt) (Haemophilus somnus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (03 Oct 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 bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi110 – 1101Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi141 – 1411Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi201 – 2011Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi273 – 2731Iron-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

    BioCyciHSOM205914:GJ7V-1044-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:HS_1010
    OrganismiHistophilus somni (strain 129Pt) (Haemophilus somnus)
    Taxonomic identifieri205914 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
    ProteomesiUP000001970: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 331331Biotin synthasePRO_0000381418Add
    BLAST

    Proteomic databases

    PRIDEiQ0I355.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi205914.HS_1010.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0I355.
    SMRiQ0I355. Positions 19-326.
    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.

    Q0I355-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTIITINIPS LTPHPCVEYW SVCKVEALFE TPFLELVYQA AQVHRKHFNP    50
    QTIQLSTLMS IKTGGCPEDC SYCPQSARYH TGVQNQQLLC VEEIVEKAKI 100
    AKSRGAGRFC MGAAWRGPKP KDIEKITEII KAVKDLGLET CGTFGLLQDG 150
    MAEELKEAGL DYYNHNIDTA PEHYKEIIGT RDFDDRLNTL GKVRKAGLKV 200
    CCGGIVGMNE TRKERAGLIA SLANLDPQPE SVPINQLVKV EGTPLADAQE 250
    LDWTEFVRTI AVARITMPKS YVRLSAGRQG MSEEMQAMCF MAGANSIFYG 300
    DKLLVTVNPE EDGDQLLMAK LDLKPETQEN K 331
    Length:331
    Mass (Da):36,715
    Last modified:October 3, 2006 - v1
    Checksum:i299A6FF3A1763BC5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000436 Genomic DNA. Translation: ABI25285.1.
    RefSeqiWP_011609164.1. NC_008309.1.
    YP_719221.1. NC_008309.1.

    Genome annotation databases

    EnsemblBacteriaiABI25285; ABI25285; HS_1010.
    GeneIDi4240503.
    KEGGihso:HS_1010.
    PATRICi20282045. VBIHaeSom53361_1059.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000436 Genomic DNA. Translation: ABI25285.1 .
    RefSeqi WP_011609164.1. NC_008309.1.
    YP_719221.1. NC_008309.1.

    3D structure databases

    ProteinModelPortali Q0I355.
    SMRi Q0I355. Positions 19-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 205914.HS_1010.

    Proteomic databases

    PRIDEi Q0I355.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABI25285 ; ABI25285 ; HS_1010 .
    GeneIDi 4240503.
    KEGGi hso:HS_1010.
    PATRICi 20282045. VBIHaeSom53361_1059.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci HSOM205914:GJ7V-1044-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 Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
      Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
      J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 129Pt.

    Entry informationi

    Entry nameiBIOB_HISS1
    AccessioniPrimary (citable) accession number: Q0I355
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 61 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