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C5A1S7

- RIBL_THEGJ

UniProt

C5A1S7 - RIBL_THEGJ

Protein

FAD synthase

Gene

ribL

Organism
Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 35 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.UniRule annotation

    Catalytic activityi

    ATP + FMN = diphosphate + FAD.UniRule annotation

    Cofactori

    Divalent metal cations.UniRule annotation

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 182ATPUniRule annotation
    Nucleotide bindingi22 – 254ATPUniRule annotation
    Nucleotide bindingi101 – 1044ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. FMN adenylyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. FAD biosynthetic process Source: UniProtKB-HAMAP
    2. FMN metabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciTGAM593117:GHFT-1882-MONOMER.
    UniPathwayiUPA00277; UER00407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FAD synthaseUniRule annotation (EC:2.7.7.2UniRule annotation)
    Alternative name(s):
    FMN adenylyltransferaseUniRule annotation
    Flavin adenine dinucleotide synthaseUniRule annotation
    Gene namesi
    Name:ribLUniRule annotation
    Ordered Locus Names:TGAM_1844
    OrganismiThermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)
    Taxonomic identifieri593117 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus
    ProteomesiUP000001488: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151FAD synthasePRO_0000406283Add
    BLAST

    Proteomic databases

    PaxDbiC5A1S7.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi593117.TGAM_1844.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the archaeal FAD synthase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0615.
    HOGENOMiHOG000284153.
    KOiK14656.
    OMAiIVLGHDQ.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_02115. FAD_synth_arch.
    InterProiIPR004821. Cyt_trans-like.
    IPR024902. FAD_synth_RibL.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF01467. CTP_transf_2. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    C5A1S7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGPSKGRKI RVLVGGVFDI LHVGHVHFLK QAKELGDELV VIVAHDETVR    50
    RNKRRNPINP AEDRAELLRA IRYVDEVYIG SPGGIDFELV RRINPDVIAI 100
    GPDQNFNCEK LKEELKRHGI EAEVIRVPYL YKSDRAKTTK IIRRIVEEFC 150
    E 151
    Length:151
    Mass (Da):17,308
    Last modified:July 28, 2009 - v1
    Checksum:iE68F9F6A2E6E4074
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001398 Genomic DNA. Translation: ACS34346.1.
    RefSeqiWP_015859455.1. NC_012804.1.
    YP_002960210.1. NC_012804.1.

    Genome annotation databases

    EnsemblBacteriaiACS34346; ACS34346; TGAM_1844.
    GeneIDi7987671.
    KEGGitga:TGAM_1844.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001398 Genomic DNA. Translation: ACS34346.1 .
    RefSeqi WP_015859455.1. NC_012804.1.
    YP_002960210.1. NC_012804.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 593117.TGAM_1844.

    Proteomic databases

    PaxDbi C5A1S7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACS34346 ; ACS34346 ; TGAM_1844 .
    GeneIDi 7987671.
    KEGGi tga:TGAM_1844.

    Phylogenomic databases

    eggNOGi COG0615.
    HOGENOMi HOG000284153.
    KOi K14656.
    OMAi IVLGHDQ.

    Enzyme and pathway databases

    UniPathwayi UPA00277 ; UER00407 .
    BioCyci TGAM593117:GHFT-1882-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_02115. FAD_synth_arch.
    InterProi IPR004821. Cyt_trans-like.
    IPR024902. FAD_synth_RibL.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF01467. CTP_transf_2. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea."
      Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M., Anthouard V., Forterre P., Wincker P., Confalonieri F.
      Genome Biol. 10:R70.1-R70.23(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 15229 / JCM 11827 / EJ3.

    Entry informationi

    Entry nameiRIBL_THEGJ
    AccessioniPrimary (citable) accession number: C5A1S7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 35 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