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Q5FFY2

- BIOB_EHRRG

UniProt

Q5FFY2 - BIOB_EHRRG

Protein

Biotin synthase

Gene

bioB

Organism
Ehrlichia ruminantium (strain Gardel)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Mar 2005)
      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 bindingi55 – 551Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi59 – 591Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi99 – 991Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi130 – 1301Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi190 – 1901Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi262 – 2621Iron-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

    BioCyciERUM302409:GHVW-705-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:ERGA_CDS_06730
    OrganismiEhrlichia ruminantium (strain Gardel)
    Taxonomic identifieri302409 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeEhrlichia
    ProteomesiUP000000533: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 322322Biotin synthasePRO_0000381376Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi302409.ERGA_CDS_06730.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5FFY2.
    SMRiQ5FFY2. Positions 6-316.
    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.

    Q5FFY2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCTSIRHDWQ LPEVLELFNI PFNDLILNAH LIHRKFFNSN EIQIAGLLNI    50
    KTGGCPENCK YCSQSAHYKT QLKKEDLLNI ETIKEAIKKA KVNGIDRFCF 100
    AAAWRQIRDR DIEYICNIIS LIKSENLESC ASLGMVTLEQ AKKLKTAGLD 150
    FYNHNIDTSR DFYYNVTTTR SYDDRLSSLN NISEAEINIC SGGILGLGES 200
    IEDRAKMLLT LANLKKHPKS VPINRLVPIK GTPFENNPKI SNIDFIRTIA 250
    VARILMPESY VRLAAGRESM SHEMQALCLF AGANSLFYGE KLLTTPNADC 300
    NDDKNLLSKL GVKTKQAVFF DS 322
    Length:322
    Mass (Da):36,318
    Last modified:March 1, 2005 - v1
    Checksum:i8E11CAB36A23F150
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR925677 Genomic DNA. Translation: CAI28125.1.
    RefSeqiWP_011255762.1. NC_006831.1.
    YP_196599.1. NC_006831.1.

    Genome annotation databases

    EnsemblBacteriaiCAI28125; CAI28125; ERGA_CDS_06730.
    GeneIDi3268492.
    KEGGierg:ERGA_CDS_06730.
    PATRICi20579130. VBIEhrRum72196_0715.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR925677 Genomic DNA. Translation: CAI28125.1 .
    RefSeqi WP_011255762.1. NC_006831.1.
    YP_196599.1. NC_006831.1.

    3D structure databases

    ProteinModelPortali Q5FFY2.
    SMRi Q5FFY2. Positions 6-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 302409.ERGA_CDS_06730.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAI28125 ; CAI28125 ; ERGA_CDS_06730 .
    GeneIDi 3268492.
    KEGGi erg:ERGA_CDS_06730.
    PATRICi 20579130. VBIEhrRum72196_0715.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci ERUM302409:GHVW-705-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. "Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity."
      Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.
      J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Gardel.

    Entry informationi

    Entry nameiBIOB_EHRRG
    AccessioniPrimary (citable) accession number: Q5FFY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 1, 2005
    Last modified: October 1, 2014
    This is version 73 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