Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q577P8

- BIOB_BRUAB

UniProt

Q577P8 - BIOB_BRUAB

Protein

Biotin synthase

Gene

bioB

Organism
Brucella abortus biovar 1 (strain 9-941)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 2 (28 Jul 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi63 – 631Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi67 – 671Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi107 – 1071Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi138 – 1381Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi198 – 1981Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi270 – 2701Iron-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

    BioCyciBABO262698:GJC2-2947-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:BruAb2_0730
    OrganismiBrucella abortus biovar 1 (strain 9-941)
    Taxonomic identifieri262698 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000000540: Chromosome II

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 328328Biotin synthasePRO_0000381249Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi262698.BruAb2_0730.

    Structurei

    3D structure databases

    ProteinModelPortaliQ577P8.
    SMRiQ577P8. Positions 15-322.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239957.
    KOiK01012.
    OMAiCATEDEA.
    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.

    Q577P8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPDRGGENGA SCSVGRWSAE EARAIYNLPF NDLLFRAHGL HRENFDPNRI    50
    QLSKLLNIKT GGCPEDCGYC SQSASAENGL KASKLMEIET VLEEARKAKA 100
    AGATRYCMGA AWRSPKDRDM PALTHMIESV KAMGLETCMT LGMLDSDKAE 150
    KLADAGLDYY NHNIDTSERF YPAVITTRSF EDRLDTLANV RNAGIKVCSG 200
    GILGLGEEAE DRIDMLVTLA NLPEPPESVP INMLIPMPGT RLAKAAPVDP 250
    LEFVRVVALA RILMPKSHVR LTAGRTAMSD EMQALCFFAG ANSLFMGDTL 300
    LTAANPGDDR DSSLLRRLGI QAETEQPA 328
    Length:328
    Mass (Da):35,653
    Last modified:July 28, 2009 - v2
    Checksum:iB3936726D01DAB70
    GO

    Sequence cautioni

    The sequence AAX76136.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017224 Genomic DNA. Translation: AAX76136.1. Different initiation.
    RefSeqiYP_223497.1. NC_006933.1.

    Genome annotation databases

    EnsemblBacteriaiAAX76136; AAX76136; BruAb2_0730.
    GeneIDi3342165.
    KEGGibmb:BruAb2_0730.
    PATRICi17827742. VBIBruAbo15061_3043.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017224 Genomic DNA. Translation: AAX76136.1 . Different initiation.
    RefSeqi YP_223497.1. NC_006933.1.

    3D structure databases

    ProteinModelPortali Q577P8.
    SMRi Q577P8. Positions 15-322.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 262698.BruAb2_0730.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAX76136 ; AAX76136 ; BruAb2_0730 .
    GeneIDi 3342165.
    KEGGi bmb:BruAb2_0730.
    PATRICi 17827742. VBIBruAbo15061_3043.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci BABO262698:GJC2-2947-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. "Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
      Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
      J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 9-941.

    Entry informationi

    Entry nameiBIOB_BRUAB
    AccessioniPrimary (citable) accession number: Q577P8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 63 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. Brucella abortus strain 9-941
      Brucella abortus (strain 9-941): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3