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A3M4U4

- BIOB_ACIBT

UniProt

A3M4U4 - BIOB_ACIBT

Protein

Biotin synthase

Gene

bioB

Organism
Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
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 2 (02 Sep 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

    BioCyciABAU400667:GI0Q-1499-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:A1S_1511
    OrganismiAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755)
    Taxonomic identifieri400667 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex
    ProteomesiUP000006737: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Biotin synthasePRO_0000381172Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi400667.A1S_1511.

    Structurei

    3D structure databases

    ProteinModelPortaliA3M4U4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the radical SAM superfamily. Biotin synthase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239957.
    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.

    A3M4U4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLRNDWTRE EIQALYEQPF LDLVFKAQQV HREHFTANTI QVSTLLSIKT    50
    GKCPEDCKYC SQSAHYDSKL EAEKRIAVEK VISEAKAAKD SGSSRFCMGA 100
    AWRNPHERDM PYVLEMVREV KALGMETCMT LGMLNQSQAE RLKDAGLDYY 150
    NHNLDTSREY YSHIISTRTF DDRLNTLDYV RQAGMKVCSG GIVGLGESRE 200
    DRIGLLHELA TLPIHPESVP INMLVPIEGT PLADVEKLDV IEWIRTIAVA 250
    RIIMPHSYIR LSAGRESLSD SDQALAFMAG ANSLFSGDKL LTTPNAGEGK 300
    DQALFNKLGL TAEKPKPTVS DLSVDAMSA 329
    Length:329
    Mass (Da):36,659
    Last modified:September 2, 2008 - v2
    Checksum:iBB5D85217A783FF3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000521 Genomic DNA. Translation: ABO11938.2.

    Genome annotation databases

    EnsemblBacteriaiABO11938; ABO11938; A1S_1511.
    PATRICi20719266. VBIAciBau103176_1541.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000521 Genomic DNA. Translation: ABO11938.2 .

    3D structure databases

    ProteinModelPortali A3M4U4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 400667.A1S_1511.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO11938 ; ABO11938 ; A1S_1511 .
    PATRICi 20719266. VBIAciBau103176_1541.

    Phylogenomic databases

    eggNOGi COG0502.
    HOGENOMi HOG000239957.
    OrthoDBi EOG622PMP.

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci ABAU400667:GI0Q-1499-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. "New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
      Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
      Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17978 / NCDC KC 755.

    Entry informationi

    Entry nameiBIOB_ACIBT
    AccessioniPrimary (citable) accession number: A3M4U4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 55 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

    Documents

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

    External Data

    Dasty 3