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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1077 [new locus tag: SACOL_RS05495 ]
  • pan locus tag?: SAUPAN003281000
  • symbol: purQ
  • pan gene symbol?: purQ
  • synonym:
  • product: phosphoribosylformylglycinamidine synthase I

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1077 [new locus tag: SACOL_RS05495 ]
  • symbol: purQ
  • product: phosphoribosylformylglycinamidine synthase I
  • replicon: chromosome
  • strand: +
  • coordinates: 1085488..1086159
  • length: 672
  • 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
    481
    541
    601
    661
    ATGAAATTTGCGGTTCTTGTTTTTCCAGGTTCGAATTGTGATAGAGACATGTTTAATGCT
    GCTATTAAAAGTGGTGTTGAAGCGGAATATGTAGATTATAGAGAAACATCACTAAGTGGA
    TTTGATGGCGTACTTATTCCTGGTGGATTTTCATTCGGGGATTACTTAAGATCTGGGGCA
    ATGGCTAGTGTAGCGCCGATTATTTCGGAAGTTAAACGTCTTGCAGCTGAAGGTAAGCCA
    GTATTAGGTGTTTGTAATGGGTTTCAAATTTTAACTGAAATAGGCTTATTACCTGGTGCA
    TTATTGCATAACGATTCACATTTATTTATTAGTAGAAATGAAGAGTTAGAAATAGTGAAT
    AATCAAACGGCATTTACAAATCTTTATGAACAAGGTGAAAAAGTTATATATCCTGTAGCT
    CACGGTGAAGGTCATTATTATTGTACTGATGAAATATATCAACAATTAAAAGCTAACAAT
    CAAATTATTCTGAAATATGTGAATAATCCGAACGGTTCATATGATGATATTGCAGGAATT
    GTTAACGAAAAAGGCAATGTATGTGGCATGATGCCACATCCTGAAAGAGCTTTAGAAACG
    TTGTTAGGTACTGATAGTGGTGTGAAATTATTTGAAGCGATGGTAAAAAGTTGGAGGGAA
    CAACATGTCTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    672

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1077 [new locus tag: SACOL_RS05495 ]
  • symbol: PurQ
  • description: phosphoribosylformylglycinamidine synthase I
  • length: 223
  • theoretical pI: 4.69597
  • theoretical MW: 24526.7
  • GRAVY: -0.108969

⊟Function[edit | edit source]

  • reaction:
    EC 3.5.1.2?  ExPASy
    Glutaminase L-glutamine + H2O = L-glutamate + NH3
    EC 6.3.5.3?  ExPASy
    Phosphoribosylformylglycinamidine synthase ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
  • TIGRFAM:
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylformylglycinamidine synthase I (TIGR01737; EC 6.3.5.3; HMM-score: 325.8)
    and 10 more
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylformylglycinamidine synthase (TIGR01857; EC 6.3.5.3; HMM-score: 83.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis phosphoribosylformylglycinamidine synthase (TIGR01735; EC 6.3.5.3; HMM-score: 76.2)
    Genetic information processing Protein fate Degradation of proteins, peptides, and glycopeptides intracellular protease, PfpI family (TIGR01382; HMM-score: 25.8)
    Metabolism Amino acid biosynthesis Histidine family imidazole glycerol phosphate synthase, glutamine amidotransferase subunit (TIGR01855; EC 2.4.2.-; HMM-score: 25.4)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pyridoxine pyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2 (TIGR03800; EC 2.6.-.-; HMM-score: 21.8)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis CTP synthase (TIGR00337; EC 6.3.4.2; HMM-score: 17.2)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin cobyric acid synthase CobQ (TIGR00313; EC 6.3.5.10; HMM-score: 17.1)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis GMP synthase (glutamine-hydrolyzing), N-terminal domain (TIGR00888; EC 6.3.5.2; HMM-score: 16.2)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Pyrimidine ribonucleotide biosynthesis carbamoyl-phosphate synthase, small subunit (TIGR01368; EC 6.3.5.5; HMM-score: 13.2)
    aminodeoxychorismate synthase (TIGR01823; EC 2.6.1.85; HMM-score: 10.2)
  • TheSEED  :
    • Phosphoribosylformylglycinamidine synthase, glutamine amidotransferase subunit (EC 6.3.5.3)
    Nucleosides and Nucleotides Purines De Novo Purine Biosynthesis  Phosphoribosylformylglycinamidine synthase, glutamine amidotransferase subunit (EC 6.3.5.3)
  • PFAM:
    Glutaminase_I (CL0014) GATase_5; CobB/CobQ-like glutamine amidotransferase domain (PF13507; HMM-score: 155.3)
    and 5 more
    GATase; Glutamine amidotransferase class-I (PF00117; HMM-score: 32.7)
    GATase_3; CobB/CobQ-like glutamine amidotransferase domain (PF07685; HMM-score: 30)
    DJ-1_PfpI; DJ-1/PfpI family (PF01965; HMM-score: 29)
    Peptidase_C26; Peptidase C26 (PF07722; HMM-score: 16.4)
    SNO; SNO glutamine amidotransferase family (PF01174; HMM-score: 13.9)

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

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

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic
    • Cytoplasmic Score: 9.97
    • Cytoplasmic Membrane Score: 0
    • Cellwall Score: 0.01
    • Extracellular Score: 0.02
    • Internal Helices: 0
  • LocateP: Intracellular
    • Prediction by SwissProt Classification: Cytoplasmic
    • Pathway Prediction: No pathway
    • Intracellular possibility: 0.83
    • Signal peptide possibility: -0.5
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.045141
    • TAT(Tat/SPI): 0.000764
    • LIPO(Sec/SPII): 0.006095
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKFAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRETSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEGKPVLGVCNGFQILTEIGLLPGALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQLKANNQIILKYVNNPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDSGVKLFEAMVKSWREQHV

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1277 [5]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • data available for N315

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 18.71 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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