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Q477A1

- BIOB_CUPPJ

UniProt

Q477A1 - BIOB_CUPPJ

Protein

Biotin synthase

Gene

bioB

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (13 Sep 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 bindingi78 – 781Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi82 – 821Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi85 – 851Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi122 – 1221Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi153 – 1531Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi213 – 2131Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi285 – 2851Iron-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

    BioCyciCPIN264198:GIW3-150-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:Reut_A0150
    OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134))
    Taxonomic identifieri264198 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000002697: Chromosome 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342Biotin synthasePRO_0000381573Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi264198.Reut_A0150.

    Structurei

    3D structure databases

    ProteinModelPortaliQ477A1.
    SMRiQ477A1. Positions 31-338.
    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.

    Q477A1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNQAAQTVAT ISAEALRQTA RNTHALPEDA RWRVDDVAAL FALPFNDLLF    50
    RAQQVHRENF DANTVQLSTL LSIKTGGCEE DCGYCPQSAH HDAGVKAEKL 100
    MELDEVLEAA RAAKANGATR FCMGAAWRSP KDRHLEPVMD MVREVKAMGL 150
    ETCVTLGMLK AEQAQQLKDA GLDYYNHNLD TSPEFYGKII TTRTYQDRLD 200
    TIGHVRDAGI NVCCGGIVGM GESREARAGL IAQLANMDPY PESVPINNLV 250
    QVEGTPLAGT EALDPFEFVR TIAVARITMP GAMVRLSAGR EAMDEALQAL 300
    CFMAGANSIF YGEKLLTTGN PQADRDRALL ARLDIRAEGY AG 342
    Length:342
    Mass (Da):37,249
    Last modified:September 13, 2005 - v1
    Checksum:i917A19728C5815FC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000090 Genomic DNA. Translation: AAZ59532.1.
    RefSeqiYP_294376.1. NC_007347.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ59532; AAZ59532; Reut_A0150.
    GeneIDi3610716.
    KEGGireu:Reut_A0150.
    PATRICi20225731. VBIRalEut24049_0744.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000090 Genomic DNA. Translation: AAZ59532.1 .
    RefSeqi YP_294376.1. NC_007347.1.

    3D structure databases

    ProteinModelPortali Q477A1.
    SMRi Q477A1. Positions 31-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 264198.Reut_A0150.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAZ59532 ; AAZ59532 ; Reut_A0150 .
    GeneIDi 3610716.
    KEGGi reu:Reut_A0150.
    PATRICi 20225731. VBIRalEut24049_0744.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci CPIN264198:GIW3-150-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 sequence of chromosome 1 of Ralstonia eutropha JMP134."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JMP134 / LMG 1197.

    Entry informationi

    Entry nameiBIOB_CUPPJ
    AccessioniPrimary (citable) accession number: Q477A1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 66 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