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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0961 [new locus tag: SACOL_RS04925 ]
  • pan locus tag?: SAUPAN003060000
  • symbol: gluD
  • pan gene symbol?: gudB
  • synonym:
  • product: glutamate dehydrogenase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0961 [new locus tag: SACOL_RS04925 ]
  • symbol: gluD
  • product: glutamate dehydrogenase
  • replicon: chromosome
  • strand: +
  • coordinates: 962628..963872
  • length: 1245
  • 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
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    ATGACTGAGAACAATAATTTAGTAACTTCTACTCAAGGAATTATTAAAGAAGCATTGCAT
    AAATTGGGATTTGACGAAGGAATGTACGATTTAATTAAAGAACCTTTAAGAATGTTACAA
    GTGCGTATCCCTGTACGAATGGATGATGGCACAGTAAAAACATTCACAGGTTACCGTGCG
    CAACATAATGATGCTGTTGGACCAACAAAAGGGGGCGTGCGTTTCCACCCAGATGTTGAT
    GAAGAAGAAGTAAAAGCATTATCAATGTGGATGACTTTGAAATGTGGCATTGTAAACTTA
    CCATACGGTGGTGGTAAGGGTGGTATCGTTTGTGATCCACGTCAAATGAGCATTCATGAA
    GTTGAACGTTTATCACGCGGATATGTAAGAGCAATTTCACAATTCGTAGGTCCGAACAAA
    GATATTCCAGCACCAGATGTATTTACAAACTCACAAATTATGGCTTGGATGATGGATGAA
    TATAGTGCATTAGATAAATTTAATTCACCAGGTTTCATCACAGGTAAACCAATTGTATTG
    GGTGGTTCTCATGGACGCGACAGATCAACTGCACTAGGTGTAGTTATTGCAATTGAACAA
    GCTGCAAAACGTCGTAATATGCAAATTGAAGGTGCCAAGGTTGTTATTCAAGGTTTCGGT
    AATGCCGGAAGTTTCTTAGCTAAATTCTTATATGATTTAGGTGCAAAAATTGTAGGTATC
    TCTGATGCTTACGGTGCATTACACGATCCAAATGGCTTAGATATAGATTATTTATTAGAC
    CGTCGTGATAGTTTTGGTACGGTAACAAATTTATTTGAAGAAACAATCTCAAATAAAGAA
    TTGTTTGAATTAGATTGTGACATTTTAGTACCAGCGGCTATTTCAAACCAAATTACAGAA
    GACAATGCACATGATATTAAAGCTAGTATCGTTGTTGAAGCTGCTAATGGACCTACAACA
    CCAGAAGCAACACGTATTTTAACTGAACGTGGTATATTATTAGTTCCAGACGTATTAGCA
    AGTGCTGGTGGTGTAACGGTTTCTTACTTCGAATGGGTACAAAATAATCAAGGTTATTAT
    TGGTCTGAAGAAGAAGTTAATGAAAAGCTACGTGAAAAATTAGAAGCGGCATTTGATACG
    ATTTACGAATTGTCTCAAAACCGAAAAATAGATATGAGACTTGCAGCATATATCATAGGT
    ATTAAACGTACAGCAGAAGCAGCTAGATATCGTGGTTGGGCATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1245

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0961 [new locus tag: SACOL_RS04925 ]
  • symbol: GluD
  • description: glutamate dehydrogenase
  • length: 414
  • theoretical pI: 5.00453
  • theoretical MW: 45759.7
  • GRAVY: -0.21087

⊟Function[edit | edit source]

  • reaction:
    EC 1.4.1.2?  ExPASy
    Glutamate dehydrogenase L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH
  • TIGRFAM:
    Cellular processes Cellular processes Sporulation and germination dipicolinic acid synthetase, A subunit (TIGR02853; HMM-score: 11.9)
  • TheSEED  :
    • Glutamate dehydrogenase (NAD(+)) (EC 1.4.1.2)
    Amino Acids and Derivatives Glutamine, glutamate, aspartate, asparagine; ammonia assimilation Glutamate dehydrogenases  NAD-specific glutamate dehydrogenase (EC 1.4.1.2)
    and 1 more
    Amino Acids and Derivatives Glutamine, glutamate, aspartate, asparagine; ammonia assimilation Glutamine, Glutamate, Aspartate and Asparagine Biosynthesis  NAD-specific glutamate dehydrogenase (EC 1.4.1.2)
  • PFAM:
    NADP_Rossmann (CL0063) ELFV_dehydrog; Glutamate/Leucine/Phenylalanine/Valine dehydrogenase (PF00208; HMM-score: 262.1)
    and 3 more
    AA_dh_N (CL0603) ELFV_dehydrog_N; Glu/Leu/Phe/Val dehydrogenase, dimerisation domain (PF02812; HMM-score: 188.7)
    NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 15.8)
    no clan defined CobS_N; Cobaltochelatase CobS subunit N terminal (PF12556; HMM-score: 11.8)

⊟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: 1
    • Signal peptide possibility: -1
    • N-terminally Anchored Score: -1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.002571
    • TAT(Tat/SPI): 0.000265
    • LIPO(Sec/SPII): 0.000366
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTENNNLVTSTQGIIKEALHKLGFDEGMYDLIKEPLRMLQVRIPVRMDDGTVKTFTGYRAQHNDAVGPTKGGVRFHPDVDEEEVKALSMWMTLKCGIVNLPYGGGKGGIVCDPRQMSIHEVERLSRGYVRAISQFVGPNKDIPAPDVFTNSQIMAWMMDEYSALDKFNSPGFITGKPIVLGGSHGRDRSTALGVVIAIEQAAKRRNMQIEGAKVVIQGFGNAGSFLAKFLYDLGAKIVGISDAYGALHDPNGLDIDYLLDRRDSFGTVTNLFEETISNKELFELDCDILVPAAISNQITEDNAHDIKASIVVEAANGPTTPEATRILTERGILLVPDVLASAGGVTVSYFEWVQNNQGYYWSEEEVNEKLREKLEAAFDTIYELSQNRKIDMRLAAYIIGIKRTAEAARYRGWA

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 218 [5]
  • interaction partners:
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL1263(sucD)succinyl-CoA synthetase subunit alpha  [6] (data from MRSA252)
    SACOL1929ABC transporter ATP-binding protein  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: CcpA regulon
    CcpA(TF)important in Carbon catabolism; RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 45.82 h [7]

⊟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. ↑ 6.0 6.1 6.2 Artem Cherkasov, Michael Hsing, Roya Zoraghi, Leonard J Foster, Raymond H See, Nikolay Stoynov, Jihong Jiang, Sukhbir Kaur, Tian Lian, Linda Jackson, Huansheng Gong, Rick Swayze, Emily Amandoron, Farhad Hormozdiari, Phuong Dao, Cenk Sahinalp, Osvaldo Santos-Filho, Peter Axerio-Cilies, Kendall Byler, William R McMaster, Robert C Brunham, B Brett Finlay, Neil E Reiner
    Mapping the protein interaction network in methicillin-resistant Staphylococcus aureus.
    J Proteome Res: 2011, 10(3);1139-50
    [PubMed:21166474] [WorldCat.org] [DOI] (I p)
  7. ↑ 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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