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B4S0P9

- BIOB_ALTMD

UniProt

B4S0P9 - BIOB_ALTMD

Protein

Biotin synthase

Gene

bioB

Organism
Alteromonas macleodii (strain DSM 17117 / Deep ecotype)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (23 Sep 2008)
      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 bindingi139 – 1391Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi199 – 1991Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi271 – 2711Iron-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

    BioCyciAMAC314275:GHA7-1469-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:MADE_1007255
    OrganismiAlteromonas macleodii (strain DSM 17117 / Deep ecotype)
    Taxonomic identifieri314275 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas
    ProteomesiUP000001870: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 374374Biotin synthasePRO_0000381194Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi314275.MADE_02211.

    Structurei

    3D structure databases

    ProteinModelPortaliB4S0P9.
    SMRiB4S0P9. Positions 15-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0502.
    KOiK01012.
    OMAiRIMMPAS.

    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.

    B4S0P9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLAYAPTAQ TITIRNDWTK AEVEALFAMP FNDLLFNAQV VHRQHFNPNE    50
    VQVSTLLSIK TGACPEDCKY CPQSARYDTG LEKERLLEIE KVIQRAKEAK 100
    QVGSTRFCMG AAWRNPRDRD MPYILKMVEE VKSLGLETCM TLGMLTRDQA 150
    VALKQAGLDY YNHNLDTSPE YYGDIITTRT YEDRLNTLEN VRAAGMNVCS 200
    GGIVGMGETV SDRASMLVQL ANLPEQPQSV PINMLVKVKG TPLDSVEDLD 250
    YFEFIRTIAV ARIMMPKSHV RLSAGREAMN EQMQAMCFMA GANSIFYGCK 300
    LLTTSNPDTH EDVMLFKKLG INTERTRDYS DEAHQQVLEE EIAQQQEQAE 350
    GSNDLFIDAT KPKVAAKQQH ATEA 374
    Length:374
    Mass (Da):41,999
    Last modified:September 23, 2008 - v1
    Checksum:i949F05B2DF1C24D2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001103 Genomic DNA. Translation: AEA97593.1.
    RefSeqiWP_012517935.1. NC_011138.3.
    YP_004426591.1. NC_011138.3.

    Genome annotation databases

    EnsemblBacteriaiAEA97593; AEA97593; MADE_1007255.
    GeneIDi10556793.
    KEGGiamc:MADE_1007255.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001103 Genomic DNA. Translation: AEA97593.1 .
    RefSeqi WP_012517935.1. NC_011138.3.
    YP_004426591.1. NC_011138.3.

    3D structure databases

    ProteinModelPortali B4S0P9.
    SMRi B4S0P9. Positions 15-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 314275.MADE_02211.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AEA97593 ; AEA97593 ; MADE_1007255 .
    GeneIDi 10556793.
    KEGGi amc:MADE_1007255.

    Phylogenomic databases

    eggNOGi COG0502.
    KOi K01012.
    OMAi RIMMPAS.

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci AMAC314275:GHA7-1469-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 genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
      Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
      ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 17117 / Deep ecotype.

    Entry informationi

    Entry nameiBIOB_ALTMD
    AccessioniPrimary (citable) accession number: B4S0P9
    Secondary accession number(s): F2G6Q6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 48 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