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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • 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 source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • 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 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
    ATGAAAAAGATAGTACTTTACGGCGGTCAGTTTAACCCTATCCATACTGCACATATGATA
    GTAGCTAGCGAAGTATTTCATGAATTACAGCCAGATGAATTTTATTTTTTACCTAGTTTT
    ATGTCTCCATTGAAAAAGCACCATGATTTTATAGACGTTCAGCACAGATTAACAATGATA
    CAGATGATTATCGACGAGCTTGGTTTTGGAGATATTTGTGACGATGAAATTAAACGTGGT
    GGTCAAAGTTATACCTATGACACGATCAAGGCATTCAAGGAGCAACACAAAGACAGTGAG
    TTGTACTTTGTTATTGGGACGGATCAGTATAACCAACTAGAGAAATGGTATCAAATTGAA
    TACTTAAAAGAAATGGTTACTTTTGTAGTTGTAAATCGAGACAAAAATAGTCAAAATGTT
    GAAAATGCTATGATTGCAATTCAGATACCTAGGGTAGATATAAGTTCGACAATGATTCGA
    CAAAGAGTTAGTGAAGGGAAATCTATCCAAGTTCTTGTTCCTAAATCCGTTGAAAACTAT
    ATTAAGGGGGAAGGATTATATGAACATTGA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    570

Protein[edit source | edit]

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

General[edit source | edit]

  • 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 source | edit]

  • reaction:
    EC 2.7.7.18?  ExPASy
    Nicotinate-nucleotide adenylyltransferaseATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD+
  • TIGRFAM:
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersPyridine nucleotidesnicotinate (nicotinamide) nucleotide adenylyltransferase (TIGR00482; EC 2.7.7.18; HMM-score: 204.4)
    cytidyltransferase-like domain (TIGR00125; HMM-score: 23.5)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersPantothenate and coenzyme Apantetheine-phosphate adenylyltransferase (TIGR01510; EC 2.7.7.3; HMM-score: 20.9)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersPyridine nucleotidesnicotinamide-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:  
    Cofactors, Vitamins, Prosthetic Groups, PigmentsNAD and NADPNAD 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 & interactions[edit source | edit]

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

Localization[edit source | edit]

  • 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
    • Ymax: 0.153
    • Ymax_pos: 23
    • Cmax: 0.147
    • Cmax_pos: 23
    • Smax: 0.227
    • Smax_pos: 18
    • Smean: 0.136
    • D: 0.146
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MKKIVLYGGQFNPIHTAHMIVASEVFHELQPDEFYFLPSFMSPLKKHHDFIDVQHRLTMIQMIIDELGFGDICDDEIKRGGQSYTYDTIKAFKEQHKDSELYFVIGTDQYNQLEKWYQIEYLKEMVTFVVVNRDKNSQNVENAMIAIQIPRVDISSTMIRQRVSEGKSIQVLVPKSVENYIKGEGLYEH

Experimental data[edit source | edit]

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: 22.54 h [4]

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, 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 source | edit]

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)