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A7H632

- BIOB_CAMJD

UniProt

A7H632 - BIOB_CAMJD

Protein

Biotin synthase

Gene

bioB

Organism
Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (11 Sep 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 bindingi16 – 161Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi20 – 201Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi23 – 231Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi60 – 601Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi95 – 951Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi153 – 1531Iron-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

    BioCyciCJEJ360109:GJDG-1999-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:JJD26997_2057
    OrganismiCampylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97)
    Taxonomic identifieri360109 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
    ProteomesiUP000002302: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 278278Biotin synthasePRO_0000381285Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi360109.JJD26997_2057.

    Structurei

    3D structure databases

    ProteinModelPortaliA7H632.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239958.
    KOiK01012.
    OMAiTSEATYG.
    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.

    A7H632-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQIMLCAISN IASGNCSEDC KYCTQSAHVR TDIQKYRRKE LSQIVLEAKM    50
    AKKNEALGFC LVTAGLGLDD EKLEYVCEAA KAVQKEVPNL LLIACNGMAS 100
    VEQLKELKKA GIFSYNHNLE TSKEFFPQIC TTHTWESRFQ TNLNAKEAGL 150
    MLCCGGIYGM GESEENRLSF RKSLQELQPF STPINFFIAN ENLKLQTPRL 200
    SADEALKIVR DTKEALPQSV VMVAGGREVV LQERQYEIFQ AGAGAIVIGD 250
    YLTTKGEEPS QDIIKLKEMG FTFASECH 278
    Length:278
    Mass (Da):30,957
    Last modified:September 11, 2007 - v1
    Checksum:i7A88500208F9BF2B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000768 Genomic DNA. Translation: ABS44048.1.
    RefSeqiWP_011990970.1. NC_009707.1.
    YP_001398962.1. NC_009707.1.

    Genome annotation databases

    EnsemblBacteriaiABS44048; ABS44048; JJD26997_2057.
    GeneIDi5389132.
    KEGGicjd:JJD26997_2057.
    PATRICi20049802. VBICamJej122183_2034.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000768 Genomic DNA. Translation: ABS44048.1 .
    RefSeqi WP_011990970.1. NC_009707.1.
    YP_001398962.1. NC_009707.1.

    3D structure databases

    ProteinModelPortali A7H632.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 360109.JJD26997_2057.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABS44048 ; ABS44048 ; JJD26997_2057 .
    GeneIDi 5389132.
    KEGGi cjd:JJD26997_2057.
    PATRICi 20049802. VBICamJej122183_2034.

    Phylogenomic databases

    eggNOGi COG0502.
    HOGENOMi HOG000239958.
    KOi K01012.
    OMAi TSEATYG.
    OrthoDBi EOG622PMP.

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci CJEJ360109:GJDG-1999-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 Campylobacter jejuni subsp doylei 269.97 isolated from human blood."
      Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
      Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-1458 / RM4099 / 269.97.

    Entry informationi

    Entry nameiBIOB_CAMJD
    AccessioniPrimary (citable) accession number: A7H632
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 49 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