Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q3AX82

- BIOB_SYNS9

UniProt

Q3AX82 - BIOB_SYNS9

Protein

Biotin synthase

Gene

bioB

Organism
Synechococcus sp. (strain CC9902)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (22 Nov 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi55 – 551Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi59 – 591Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi100 – 1001Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi132 – 1321Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi192 – 1921Iron-sulfur 2 (2Fe-2S)UniRule annotation
    Metal bindingi264 – 2641Iron-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

    BioCyciSSP316279:GJCI-1408-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:Syncc9902_1394
    OrganismiSynechococcus sp. (strain CC9902)
    Taxonomic identifieri316279 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
    ProteomesiUP000002712: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 333333Biotin synthasePRO_0000381681Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi316279.Syncc9902_1394.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3AX82.
    SMRiQ3AX82. Positions 6-315.
    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.

    Q3AX82-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTITTRHDWT TEEIQTLLEL PLMDLLWQAQ TVHRDANPGY RVQLASLLSV    50
    KTGGCEEDCS YCSQSIHNSS DVSGFEAQMR VEPVLERARA AKEAGADRFC 100
    MGWAWREIRD GAQFEAMLEM VRGVRGMGME ACVTAGMLTD DQAGRLAEAG 150
    LTAYNHNLDT SPEHYEKIIS TRTYEDRLET LQRVRKAGVT LCSGGIIGMG 200
    ETLRDRASML QVLASMNPHP ESVPVNGLVA VEGTPLEEQQ PFEPLELVRM 250
    VATARILMPH ARVRLSAGRE QLSREAQILC LQAGADSIFY GDLLLTTGNP 300
    DVEADRRLLA DAGVQANWQE NASSLAIKAP AST 333
    Length:333
    Mass (Da):36,588
    Last modified:November 22, 2005 - v1
    Checksum:i9AAC8D447CA7B5BF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000097 Genomic DNA. Translation: ABB26358.1.
    RefSeqiWP_011360181.1. NC_007513.1.
    YP_377402.1. NC_007513.1.

    Genome annotation databases

    EnsemblBacteriaiABB26358; ABB26358; Syncc9902_1394.
    GeneIDi3742525.
    KEGGisye:Syncc9902_1394.
    PATRICi23800171. VBISynSp76179_1545.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000097 Genomic DNA. Translation: ABB26358.1 .
    RefSeqi WP_011360181.1. NC_007513.1.
    YP_377402.1. NC_007513.1.

    3D structure databases

    ProteinModelPortali Q3AX82.
    SMRi Q3AX82. Positions 6-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 316279.Syncc9902_1394.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABB26358 ; ABB26358 ; Syncc9902_1394 .
    GeneIDi 3742525.
    KEGGi sye:Syncc9902_1394.
    PATRICi 23800171. VBISynSp76179_1545.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00078 ; UER00162 .
    BioCyci SSP316279:GJCI-1408-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 Synechococcus sp. CC9902."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CC9902.

    Entry informationi

    Entry nameiBIOB_SYNS9
    AccessioniPrimary (citable) accession number: Q3AX82
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 67 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