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P19206

- BIOB_LYSSH

UniProt

P19206 - BIOB_LYSSH

Protein

Biotin synthase

Gene

bioB

Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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 bindingi64 – 641Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi68 – 681Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi71 – 711Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi108 – 1081Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi140 – 1401Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi200 – 2001Iron-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

    UniPathwayiUPA00078; UER00162.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
    Gene namesi
    Name:bioBUniRule annotation
    OrganismiLysinibacillus sphaericus (Bacillus sphaericus)
    Taxonomic identifieri1421 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 332332Biotin synthasePRO_0000185545Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP19206.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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.

    P19206-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNWLQLADEV IAGKVISDDE ALAILNSDDD DILKLMDGAF AIRKHYYGKK    50
    VKLNMIMNAK SGYCPEDCGY CSQSSKSTAP IEKYPFITKE EILAGAKRAF 100
    ENKIGTYCIV ASGRGPTRKD VNVVSEAVEE IKAKYGLKVC ACLGLLKEEQ 150
    AQQLKEAGVD RYNHNLNTSE RHHSYITTTH TYEDRVNTVE VVKKHGISPC 200
    SGAIIGMKET KMDVVEIARA LHQLDADSIP VNFLHAIDGT KLEGTQDLNP 250
    RYCLKVLALF RYMNPSKEIR ISGGREVNLG FLQPFGLYAA NSIFVGDYLT 300
    TEGQEANSDY RMLEDLGFEI ELTQKQEEAF CS 332
    Length:332
    Mass (Da):37,015
    Last modified:November 1, 1990 - v1
    Checksum:iB5FF14F5CA9903EF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27867 Genomic DNA. Translation: AAA22268.1.
    M29292 Genomic DNA. Translation: AAB02327.1.
    PIRiJS0274.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27867 Genomic DNA. Translation: AAA22268.1 .
    M29292 Genomic DNA. Translation: AAB02327.1 .
    PIRi JS0274.

    3D structure databases

    ProteinModelPortali P19206.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .

    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. "Cloning of the biotin synthetase gene from Bacillus sphaericus and expression in Escherichia coli and Bacilli."
      Ohsawa I., Speck D., Kisou T., Hayakawa K., Zinsius M., Gloeckler R., Lemoine Y., Kamogawa K.
      Gene 80:39-48(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: T-178-367.
    2. "Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin."
      Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M., Villeval D., Kisou T., Kamogawa K., Lemoine Y.
      Gene 87:63-70(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiBIOB_LYSSH
    AccessioniPrimary (citable) accession number: P19206
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 89 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

    Direct protein sequencing

    Documents

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

    External Data

    Dasty 3