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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • 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 source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • 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 source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 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 source | edit]

General[edit source | edit]

  • 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 source | edit]

  • reaction:
    EC 6.3.5.3?  ExPASy
    Phosphoribosylformylglycinamidine synthaseATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
    EC 3.5.1.2?  ExPASy
    GlutaminaseL-glutamine + H2O = L-glutamate + NH3
  • TIGRFAM:
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPurine ribonucleotide biosynthesisphosphoribosylformylglycinamidine synthase I (TIGR01737; EC 6.3.5.3; HMM-score: 325.8)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPurine ribonucleotide biosynthesisphosphoribosylformylglycinamidine synthase (TIGR01857; EC 6.3.5.3; HMM-score: 83.2)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPurine ribonucleotide biosynthesisphosphoribosylformylglycinamidine synthase (TIGR01735; EC 6.3.5.3; HMM-score: 76.2)
    Genetic information processingProtein fateDegradation of proteins, peptides, and glycopeptidesintracellular protease, PfpI family (TIGR01382; HMM-score: 25.8)
    MetabolismAmino acid biosynthesisHistidine familyimidazole glycerol phosphate synthase, glutamine amidotransferase subunit (TIGR01855; EC 2.4.2.-; HMM-score: 25.4)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersPyridoxinepyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2 (TIGR03800; EC 2.6.-.-; HMM-score: 21.8)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPyrimidine ribonucleotide biosynthesisCTP synthase (TIGR00337; EC 6.3.4.2; HMM-score: 17.2)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersHeme, porphyrin, and cobalamincobyric acid synthase CobQ (TIGR00313; EC 6.3.5.10; HMM-score: 17.1)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPurine ribonucleotide biosynthesisGMP synthase (glutamine-hydrolyzing), N-terminal domain (TIGR00888; EC 6.3.5.2; HMM-score: 16.2)
    MetabolismPurines, pyrimidines, nucleosides, and nucleotidesPyrimidine ribonucleotide biosynthesiscarbamoyl-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:  
    Nucleosides and NucleotidesPurinesDe 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)
    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 & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:

Localization[edit source | edit]

  • 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
    • Ymax: 0.187
    • Ymax_pos: 21
    • Cmax: 0.156
    • Cmax_pos: 21
    • Smax: 0.291
    • Smax_pos: 12
    • Smean: 0.202
    • D: 0.193
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MKFAVLVFPGSNCDRDMFNAAIKSGVEAEYVDYRETSLSGFDGVLIPGGFSFGDYLRSGAMASVAPIISEVKRLAAEGKPVLGVCNGFQILTEIGLLPGALLHNDSHLFISRNEELEIVNNQTAFTNLYEQGEKVIYPVAHGEGHYYCTDEIYQQLKANNQIILKYVNNPNGSYDDIAGIVNEKGNVCGMMPHPERALETLLGTDSGVKLFEAMVKSWREQHV

Experimental data[edit source | edit]

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

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: 18.71 h [6]

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  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 source | edit]