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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1817 [new locus tag: SACOL_RS09315 ]
  • pan locus tag?: SAUPAN004455000
  • symbol: ribH
  • pan gene symbol?: ribH
  • synonym:
  • product: 6,7-dimethyl-8-ribityllumazine synthase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1817 [new locus tag: SACOL_RS09315 ]
  • symbol: ribH
  • product: 6,7-dimethyl-8-ribityllumazine synthase
  • replicon: chromosome
  • strand: -
  • coordinates: 1872609..1873073
  • length: 465
  • essential: unknown other strains

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    ATGAATTTTGAAGGTAAATTAATTGGAAAAGATTTGAAAGTTGCAATCGTAGTTAGTCGA
    TTTAATGATTTTATCACTGGAAGATTACTTGAAGGTGCAAAAGATACTTTGATTCGACAT
    GATGTTAATGAAGACAATATTGATGTAGCATTTGTGCCAGGTGCGTTTGAAATTCCTTTA
    GTAGCTAAAAAATTAGCCTCATCAGGAAATTATGATGCAGTAATTACATTAGGATGCGTA
    ATTCGCGGTGCTACGTCTCATTATGATTATGTTTGTAATGAAGTCGCGAAAGGTGTTTCT
    AAAGTGAATGATCAAACTAATGTACCAGTCATATTTGGTATTTTAACGACTGAAAGTATT
    GAACAAGCTGTGGAAAGAGCAGGTACGAAAGCTGGCAATAAAGGTGCTGAAGCAGCAGTA
    AGTGCAATTGAAATGGCTAATTTATTAAAATCTATAAAAGCATAG
    60
    120
    180
    240
    300
    360
    420
    465

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1817 [new locus tag: SACOL_RS09315 ]
  • symbol: RibH
  • description: 6,7-dimethyl-8-ribityllumazine synthase
  • length: 154
  • theoretical pI: 5.78192
  • theoretical MW: 16395.7
  • GRAVY: 0.127273

⊟Function[edit | edit source]

  • reaction:
    EC 2.5.1.9?  ExPASy
    Riboflavin synthase 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
    EC 2.5.1.78?  ExPASy
    6,7-dimethyl-8-ribityllumazine synthase 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
  • TIGRFAM:
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Riboflavin, FMN, and FAD 6,7-dimethyl-8-ribityllumazine synthase (TIGR00114; EC 2.5.1.78; HMM-score: 198)
    and 2 more
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Riboflavin, FMN, and FAD riboflavin synthase (TIGR01506; EC 2.5.1.9; HMM-score: 21.6)
    Metabolism Amino acid biosynthesis Aromatic amino acid family 3-dehydroquinate dehydratase, type II (TIGR01088; EC 4.2.1.10; HMM-score: 12.5)
  • TheSEED  :
    • 6,7-dimethyl-8-ribityllumazine synthase (EC 2.5.1.78)
  • PFAM:
    no clan defined DMRL_synthase; 6,7-dimethyl-8-ribityllumazine synthase (PF00885; HMM-score: 202.7)
    and 1 more
    TIM_barrel (CL0036) Trp_syntA; Tryptophan synthase alpha chain (PF00290; HMM-score: 13.8)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 7.5
    • Cytoplasmic Membrane Score: 1.15
    • Cellwall Score: 0.62
    • Extracellular Score: 0.73
    • Internal Helices: 0
  • LocateP: Intracellular
    • Prediction by SwissProt Classification: Cytoplasmic
    • Pathway Prediction: No pathway
    • Intracellular possibility: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.002429
    • TAT(Tat/SPI): 0.000207
    • LIPO(Sec/SPII): 0.000354
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MNFEGKLIGKDLKVAIVVSRFNDFITGRLLEGAKDTLIRHDVNEDNIDVAFVPGAFEIPLVAKKLASSGNYDAVITLGCVIRGATSHYDYVCNEVAKGVSKVNDQTNVPVIFGILTTESIEQAVERAGTKAGNKGAEAAVSAIEMANLLKSIKA

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 911 [5]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: FMN-box (transcription termination) regulon
    FMN-box(RNA)important in Riboflavin biosynthesis; transcription unit transferred from N315 data RegPrecise 

⊟Transcription pattern[edit | edit source]

⊟Protein synthesis (provided by Aureolib)[edit | edit source]

⊟Protein stability[edit | edit source]

  • half-life: 16.23 h [6]

⊟Biological Material[edit | edit source]

⊟Mutants[edit | edit source]

⊟Expression vector[edit | edit source]

⊟lacZ fusion[edit | edit source]

⊟GFP fusion[edit | edit source]

⊟two-hybrid system[edit | edit source]

⊟FLAG-tag construct[edit | edit source]

⊟Antibody[edit | edit source]

⊟Other Information[edit | edit source]

You are kindly invited to share additional interesting facts.

⊟Literature[edit | edit source]

⊟References[edit | edit source]

  1. ↑ Dörte Becher, Kristina Hempel, Susanne Sievers, Daniela Zühlke, Jan Pané-Farré, Andreas Otto, Stephan Fuchs, Dirk Albrecht, Jörg Bernhardt, Susanne Engelmann, Uwe Völker, Jan Maarten van Dijl, Michael Hecker
    A proteomic view of an important human pathogen--towards the quantification of the entire Staphylococcus aureus proteome.
    PLoS One: 2009, 4(12);e8176
    [PubMed:19997597] [WorldCat.org] [DOI] (I e)
  2. ↑ Kristina Hempel, Jan Pané-Farré, Andreas Otto, Susanne Sievers, Michael Hecker, Dörte Becher
    Quantitative cell surface proteome profiling for SigB-dependent protein expression in the human pathogen Staphylococcus aureus via biotinylation approach.
    J Proteome Res: 2010, 9(3);1579-90
    [PubMed:20108986] [WorldCat.org] [DOI] (I p)
  3. ↑ Kristina Hempel, Florian-Alexander Herbst, Martin Moche, Michael Hecker, Dörte Becher
    Quantitative proteomic view on secreted, cell surface-associated, and cytoplasmic proteins of the methicillin-resistant human pathogen Staphylococcus aureus under iron-limited conditions.
    J Proteome Res: 2011, 10(4);1657-66
    [PubMed:21323324] [WorldCat.org] [DOI] (I p)
  4. ↑ Andreas Otto, Jan Maarten van Dijl, Michael Hecker, Dörte Becher
    The Staphylococcus aureus proteome.
    Int J Med Microbiol: 2014, 304(2);110-20
    [PubMed:24439828] [WorldCat.org] [DOI] (I p)
  5. ↑ Daniela Zühlke, Kirsten Dörries, Jörg Bernhardt, Sandra Maaß, Jan Muntel, Volkmar Liebscher, Jan Pané-Farré, Katharina Riedel, Michael Lalk, Uwe Völker, Susanne Engelmann, Dörte Becher, Stephan Fuchs, Michael Hecker
    Costs of life - Dynamics of the protein inventory of Staphylococcus aureus during anaerobiosis.
    Sci Rep: 2016, 6;28172
    [PubMed:27344979] [WorldCat.org] [DOI] (I e)
  6. ↑ Stephan Michalik, Jörg Bernhardt, Andreas Otto, Martin Moche, Dörte Becher, Hanna Meyer, Michael Lalk, Claudia Schurmann, Rabea Schlüter, Holger Kock, Ulf Gerth, Michael Hecker
    Life and death of proteins: a case study of glucose-starved Staphylococcus aureus.
    Mol Cell Proteomics: 2012, 11(9);558-70
    [PubMed:22556279] [WorldCat.org] [DOI] (I p)

⊟Relevant publications[edit | edit source]

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