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A5D4Y6

- BIOB_PELTS

UniProt

A5D4Y6 - BIOB_PELTS

Protein

Biotin synthase

Gene

bioB

Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (12 Jun 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 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 bindingi139 – 1391Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi199 – 1991Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi269 – 2691Iron-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

    BioCyciPTHE370438:GCGQ-539-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:PTH_0521
    OrganismiPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
    Taxonomic identifieri370438 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum
    ProteomesiUP000006556: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 321321Biotin synthasePRO_0000381523Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi370438.PTH_0521.

    Structurei

    3D structure databases

    ProteinModelPortaliA5D4Y6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0502.
    HOGENOMiHOG000239958.
    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.

    A5D4Y6-1 [UniParc]FASTAAdd to Basket

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    MFNELVKKIK SGLEITFEEA LALGGLDEDR LNELFLAALQ VNRHFHGNRV    50
    DLCSIVNARS GRCSEDCAFC AQSGHYRTEA PVYPLLSKEE ILERAREMEL 100
    RGARRFALVT SGRGISESDF EKVLDIYQML KEKTGLGLCA SLGIIGYDKA 150
    VRLKEAGVGM YHHNLETCRS YFPHICTTHS FDERVETVKA AKEAGLEVCS 200
    GGIIGLGESW RHRVEMAFHL KELGVASVPI NILTPVKGTP LWGRPLLEPV 250
    EVLRTAAMFR LVLPGALIRL CGGREAALRD LQPLALLAGV NALMVGNYLT 300
    TSGRRVEDDL QMVADLKLSV M 321
    Length:321
    Mass (Da):35,453
    Last modified:June 12, 2007 - v1
    Checksum:iF280BD8D6C62A033
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009389 Genomic DNA. Translation: BAF58702.1.
    RefSeqiYP_001211071.1. NC_009454.1.

    Genome annotation databases

    EnsemblBacteriaiBAF58702; BAF58702; PTH_0521.
    GeneIDi5138818.
    KEGGipth:PTH_0521.
    PATRICi22907920. VBIPelThe8413_0582.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP009389 Genomic DNA. Translation: BAF58702.1 .
    RefSeqi YP_001211071.1. NC_009454.1.

    3D structure databases

    ProteinModelPortali A5D4Y6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 370438.PTH_0521.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAF58702 ; BAF58702 ; PTH_0521 .
    GeneIDi 5138818.
    KEGGi pth:PTH_0521.
    PATRICi 22907920. VBIPelThe8413_0582.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci PTHE370438:GCGQ-539-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. "The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
      Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
      Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 13744 / JCM 10971 / SI.

    Entry informationi

    Entry nameiBIOB_PELTS
    AccessioniPrimary (citable) accession number: A5D4Y6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 52 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, Reference proteome

    Documents

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

    External Data

    Dasty 3