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A4SPR7

- BIOB_AERS4

UniProt

A4SPR7 - BIOB_AERS4

Protein

Biotin synthase

Gene

bioB

Organism
Aeromonas salmonicida (strain A449)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (15 May 2007)
      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 bindingi61 – 611Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi65 – 651Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi68 – 681Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi105 – 1051Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi136 – 1361Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi196 – 1961Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi268 – 2681Iron-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

    BioCyciASAL382245:GJJN-2864-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:ASA_2877
    OrganismiAeromonas salmonicida (strain A449)
    Taxonomic identifieri382245 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
    ProteomesiUP000000225: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 362362Biotin synthasePRO_0000381185Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi382245.ASA_2877.

    Structurei

    3D structure databases

    ProteinModelPortaliA4SPR7.
    SMRiA4SPR7. Positions 12-322.
    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.

    A4SPR7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAHTAGGHA LRHDWTLSEV QALFALPFND LLFQAQTIHR AHFDPNEVQV    50
    STLLSIKTGA CPEDCKYCPQ SARYHTGLET ERLMEVEKVL ERAREARANG 100
    SSRFCMGAAW RNPKERDMPY ILRMIEEVRG LGMETCMTLG MLTADQAARL 150
    GAAGLDYYNH NLDTSPEFYG EIISTRTYQD RLDTLEHVRG AGMKVCSGGI 200
    VGMGEQAKDR AGLLMALANL PRHPESVPIN MLVKVKGTPL ENEANLDSFE 250
    FIRTIAVARI MMPASHVRLS AGREKMNEQM QAMCFMAGAN SIFYGCKLLT 300
    TPNPDENSDM QLFKRLGIRP AQRAQKPDQI QEEEILAEVS RQNAPDEMFY 350
    DATRPRAGVA RS 362
    Length:362
    Mass (Da):40,455
    Last modified:May 15, 2007 - v1
    Checksum:i052667FB31533D1B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000644 Genomic DNA. Translation: ABO90889.1.
    RefSeqiWP_005313000.1. NC_009348.1.
    YP_001142637.1. NC_009348.1.

    Genome annotation databases

    EnsemblBacteriaiABO90889; ABO90889; ASA_2877.
    GeneIDi4997734.
    KEGGiasa:ASA_2877.
    PATRICi20792165. VBIAerSal2987_2857.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000644 Genomic DNA. Translation: ABO90889.1 .
    RefSeqi WP_005313000.1. NC_009348.1.
    YP_001142637.1. NC_009348.1.

    3D structure databases

    ProteinModelPortali A4SPR7.
    SMRi A4SPR7. Positions 12-322.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 382245.ASA_2877.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO90889 ; ABO90889 ; ASA_2877 .
    GeneIDi 4997734.
    KEGGi asa:ASA_2877.
    PATRICi 20792165. VBIAerSal2987_2857.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci ASAL382245:GJJN-2864-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. "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
      Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
      BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: A449.

    Entry informationi

    Entry nameiBIOB_AERS4
    AccessioniPrimary (citable) accession number: A4SPR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 55 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