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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1650 [new locus tag: SACOL_RS08415 ]
  • pan locus tag?: SAUPAN004180000
  • symbol: nadD
  • pan gene symbol?: nadD
  • synonym:
  • product: nicotinate (nicotinamide) nucleotide adenylyltransferase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1650 [new locus tag: SACOL_RS08415 ]
  • symbol: nadD
  • product: nicotinate (nicotinamide) nucleotide adenylyltransferase
  • replicon: chromosome
  • strand: -
  • coordinates: 1680525..1681094
  • length: 570
  • 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
    ATGAAAAAGATAGTACTTTACGGCGGTCAGTTTAACCCTATCCATACTGCACATATGATA
    GTAGCTAGCGAAGTATTTCATGAATTACAGCCAGATGAATTTTATTTTTTACCTAGTTTT
    ATGTCTCCATTGAAAAAGCACCATGATTTTATAGACGTTCAGCACAGATTAACAATGATA
    CAGATGATTATCGACGAGCTTGGTTTTGGAGATATTTGTGACGATGAAATTAAACGTGGT
    GGTCAAAGTTATACCTATGACACGATCAAGGCATTCAAGGAGCAACACAAAGACAGTGAG
    TTGTACTTTGTTATTGGGACGGATCAGTATAACCAACTAGAGAAATGGTATCAAATTGAA
    TACTTAAAAGAAATGGTTACTTTTGTAGTTGTAAATCGAGACAAAAATAGTCAAAATGTT
    GAAAATGCTATGATTGCAATTCAGATACCTAGGGTAGATATAAGTTCGACAATGATTCGA
    CAAAGAGTTAGTGAAGGGAAATCTATCCAAGTTCTTGTTCCTAAATCCGTTGAAAACTAT
    ATTAAGGGGGAAGGATTATATGAACATTGA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    570

⊟Protein[edit | edit source]

Protein Data Bank: 2H29
Protein Data Bank: 2H2A

⊟General[edit | edit source]

  • locus tag: SACOL1650 [new locus tag: SACOL_RS08415 ]
  • symbol: NadD
  • description: nicotinate (nicotinamide) nucleotide adenylyltransferase
  • length: 189
  • theoretical pI: 5.83156
  • theoretical MW: 22127.2
  • GRAVY: -0.359259

⊟Function[edit | edit source]

  • reaction:
    EC 2.7.7.18?  ExPASy
    Nicotinate-nucleotide adenylyltransferase ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+
  • TIGRFAM:
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pyridine nucleotides nicotinate (nicotinamide) nucleotide adenylyltransferase (TIGR00482; EC 2.7.7.18; HMM-score: 204.4)
    and 5 more
    cytidyltransferase-like domain (TIGR00125; HMM-score: 23.5)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pantothenate and coenzyme A pantetheine-phosphate adenylyltransferase (TIGR01510; EC 2.7.7.3; HMM-score: 20.9)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Pyridine nucleotides nicotinamide-nucleotide adenylyltransferase (TIGR01527; EC 2.7.7.1; HMM-score: 19.4)
    formylmethanofuran dehydrogenase subunit B (TIGR03129; EC 1.2.99.5; HMM-score: 12.3)
    putative glycosyltransferase, TIGR04348 family (TIGR04348; EC 2.4.1.-; HMM-score: 11.2)
  • TheSEED  :
    • Nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18)
    Cofactors, Vitamins, Prosthetic Groups, Pigments NAD and NADP NAD and NADP cofactor biosynthesis global  Nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18)
  • PFAM:
    HUP (CL0039) CTP_transf_like; Cytidylyltransferase-like (PF01467; HMM-score: 105)

⊟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): 0.0041
    • TAT(Tat/SPI): 0.000055
    • LIPO(Sec/SPII): 0.001442
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MKKIVLYGGQFNPIHTAHMIVASEVFHELQPDEFYFLPSFMSPLKKHHDFIDVQHRLTMIQMIIDELGFGDICDDEIKRGGQSYTYDTIKAFKEQHKDSELYFVIGTDQYNQLEKWYQIEYLKEMVTFVVVNRDKNSQNVENAMIAIQIPRVDISSTMIRQRVSEGKSIQVLVPKSVENYIKGEGLYEH

⊟Experimental data[edit | edit source]

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

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 22.54 h [4]

⊟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, 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)
  3. ↑ 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)
  4. ↑ 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]

Seungil Han, Michael D Forman, Pat Loulakis, Michelle H Rosner, Zhi Xie, Hong Wang, Dennis E Danley, Wei Yuan, John Schafer, Zuoyu Xu
Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Staphyloccocus aureus: structural basis for NaAD interaction in functional dimer.
J Mol Biol: 2006, 360(4);814-25
[PubMed:16784754] [WorldCat.org] [DOI] (P p)

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