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Q979C2

- RIBL_THEVO

UniProt

Q979C2 - RIBL_THEVO

Protein

FAD synthase

Gene

ribL

Organism
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Oct 2001)
      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.By similarity

    Catalytic activityi

    ATP + FMN = diphosphate + FAD.

    Cofactori

    Divalent metal cations.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei120 – 1201ATP; via amide nitrogen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 102ATP
    Nucleotide bindingi14 – 174ATP
    Nucleotide bindingi91 – 944ATP

    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

    BioCyciTVOL273116:GC31-1257-MONOMER.
    UniPathwayiUPA00277; UER00407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FAD synthase (EC:2.7.7.2)
    Alternative name(s):
    FMN adenylyltransferase
    Flavin adenine dinucleotide synthase
    Gene namesi
    Name:ribL
    Ordered Locus Names:TV1239
    ORF Names:TVG1279046
    OrganismiThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
    Taxonomic identifieri273116 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
    ProteomesiUP000001017: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 142142FAD synthasePRO_0000406287Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi273116.TVN1215.

    Structurei

    Secondary structure

    1
    142
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi15 – 2511
    Beta strandi28 – 358
    Helixi38 – 436
    Helixi52 – 598
    Beta strandi66 – 705
    Helixi76 – 838
    Beta strandi86 – 905
    Helixi95 – 10814
    Beta strandi113 – 1164

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GLVX-ray1.99A/B1-142[»]
    ProteinModelPortaliQ979C2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ979C2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the archaeal FAD synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0615.
    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.

    Q979C2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIRVMATGVF DILHLGHIHY LKESKKLGDE LVVVVARDST ARNNGKIPIF    50
    DENSRLALIS ELKVVDRAIL GHEGDMMKTV IEVKPDIITL GYDQKFDEAE 100
    LQSKINKLGI TVKIVRISKY DGQLNSSSSV RKKIMELIGE RY 142
    Length:142
    Mass (Da):16,009
    Last modified:October 1, 2001 - v1
    Checksum:iB9A106F982D0022E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000011 Genomic DNA. Translation: BAB60381.1.
    RefSeqiNP_111734.1. NC_002689.2.
    WP_010917473.1. NC_002689.2.

    Genome annotation databases

    EnsemblBacteriaiBAB60381; BAB60381; BAB60381.
    GeneIDi1441355.
    KEGGitvo:TVN1215.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000011 Genomic DNA. Translation: BAB60381.1 .
    RefSeqi NP_111734.1. NC_002689.2.
    WP_010917473.1. NC_002689.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GLV X-ray 1.99 A/B 1-142 [» ]
    ProteinModelPortali Q979C2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273116.TVN1215.

    Protocols and materials databases

    DNASUi 1441355.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB60381 ; BAB60381 ; BAB60381 .
    GeneIDi 1441355.
    KEGGi tvo:TVN1215.

    Phylogenomic databases

    eggNOGi COG0615.
    KOi K14656.
    OMAi IVLGHDQ.

    Enzyme and pathway databases

    UniPathwayi UPA00277 ; UER00407 .
    BioCyci TVOL273116:GC31-1257-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q979C2.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.
    2. "The crystal structure of the lipopolysaccharide core biosynthesis protein from Thermoplasma volcanium GSS1."
      Midwest center for structural genomics (MCSG)
      Submitted (MAY-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH AMP.

    Entry informationi

    Entry nameiRIBL_THEVO
    AccessioniPrimary (citable) accession number: Q979C2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 72 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

    3D-structure, Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3