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NCBI: 10-JUN-2013

Summary[edit source | edit]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0838 [new locus tag: SACOL_RS04310 ]
  • pan locus tag?: SAUPAN002706000
  • symbol: gapA1
  • pan gene symbol?: gapA
  • synonym:
  • product: glyceraldehyde 3-phosphate dehydrogenase

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SACOL0838 [new locus tag: SACOL_RS04310 ]
  • symbol: gapA1
  • product: glyceraldehyde 3-phosphate dehydrogenase
  • replicon: chromosome
  • strand: +
  • coordinates: 864842..865852
  • length: 1011
  • 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
    721
    781
    841
    901
    961
    ATGGCAGTAAAAGTAGCAATTAATGGTTTTGGTAGAATTGGTCGTTTAGCATTCAGAAGA
    ATTCAAGAAGTAGAAGGTCTTGAAGTTGTAGCAGTAAACGACTTAACAGATGACGACATG
    TTAGCGCATTTATTAAAATATGACACTATGCAAGGTCGTTTCACAGGTGAAGTAGAGGTA
    GTTGATGGTGGTTTCCGCGTAAATGGTAAAGAAGTTAAATCATTCAGTGAACCAGATGCA
    AGCAAATTACCTTGGAAAGACTTAAATATCGATGTAGTATTAGAATGTACTGGTTTCTAC
    ACTGATAAAGATAAAGCACAAGCTCATATTGAAGCAGGCGCTAAAAAAGTATTAATCTCA
    GCACCAGCTACTGGTGACTTAAAAACAATCGTATTCAACACTAACCACCAAGAGTTAGAC
    GGTTCTGAAACAGTTGTTTCAGGTGCTTCATGTACTACAAACTCATTAGCACCAGTTGCT
    AAAGTTTTAAACGATGACTTTGGTTTAGTTGAAGGTTTAATGACTACAATTCACGCTTAC
    ACAGGTGATCAAAATACACAAGACGCACCTCACAGAAAAGGTGACAAACGTCGTGCTCGT
    GCAGCGGCAGAAAACATCATCCCTAACTCAACAGGTGCTGCTAAAGCTATCGGTAAAGTT
    ATTCCTGAAATCGATGGTAAATTAGATGGTGGTGCACAACGTGTTCCTGTAGCTACAGGT
    TCATTAACTGAATTAACAGTAGTATTAGAAAAACAAGACGTAACAGTTGAACAAGTTAAC
    GAAGCTATGAAAAATGCTTCAAACGAATCATTCGGTTACACTGAAGACGAAATCGTTTCT
    TCAGACGTTGTAGGTATGACTTACGGTTCATTATTCGACGCTACACAAACTCGTGTAATG
    TCAGTTGGCGACCGTCAATTAGTTAAAGTTGCAGCTTGGTATGATAACGAAATGTCATAT
    ACTGCACAATTAGTTCGTACATTAGCATACTTAGCTGAACTTTCTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1011

Protein[edit source | edit]

General[edit source | edit]

  • locus tag: SACOL0838 [new locus tag: SACOL_RS04310 ]
  • symbol: GapA1
  • description: glyceraldehyde 3-phosphate dehydrogenase
  • length: 336
  • theoretical pI: 4.64965
  • theoretical MW: 36280.6
  • GRAVY: -0.218155

Function[edit source | edit]

  • reaction:
    EC 1.2.1.12?  ExPASy
    Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH
  • TIGRFAM:
    MetabolismEnergy metabolismGlycolysis/gluconeogenesisglyceraldehyde-3-phosphate dehydrogenase, type I (TIGR01534; EC 1.2.1.-; HMM-score: 435.2)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersPyridoxineerythrose-4-phosphate dehydrogenase (TIGR01532; EC 1.2.1.72; HMM-score: 283.8)
    MetabolismAmino acid biosynthesisAspartate familyaspartate-semialdehyde dehydrogenase (TIGR01296; EC 1.2.1.11; HMM-score: 14.4)
    MetabolismAmino acid biosynthesisAspartate familyaspartate-semialdehyde dehydrogenase (TIGR00978; EC 1.2.1.11; HMM-score: 13.4)
  • TheSEED:  
    CarbohydratesCentral carbohydrate metabolismGlycolysis and Gluconeogenesis NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) 
    Cofactors, Vitamins, Prosthetic Groups, PigmentsPyridoxinePyridoxin (Vitamin B6) Biosynthesis NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) 
    Stress ResponseOxidative stressGlutaredoxins NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) 
    Oxidative stressRedox-dependent regulation of nucleus processes NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) 
  • PFAM:
    GADPH_aa-bio_dh (CL0139) Gp_dh_C; Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain (PF02800; HMM-score: 204)
    NADP_Rossmann (CL0063) Gp_dh_N; Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain (PF00044; HMM-score: 124.2)
    DapB_N; Dihydrodipicolinate reductase, N-terminus (PF01113; HMM-score: 18.2)
    GADPH_aa-bio_dh (CL0139) Semialdhyde_dhC; Semialdehyde dehydrogenase, dimerisation domain (PF02774; HMM-score: 15.7)
    NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 12.4)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors:
  • effectors:
  • protein partners:
    SACOL0833(clpP)ATP-dependent Clp protease proteolytic subunit  [1] (data from MRSA252)
    SACOL2130(deoD)purine nucleoside phosphorylase  [1] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [1] (data from MRSA252)
    SACOL1245(fabG1)3-oxoacyl-ACP reductase  [1] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [1] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [1] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [1] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [1] (data from MRSA252)
    SACOL1011(ppnK)inorganic polyphosphate/ATP-NAD kinase  [1] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [1] (data from MRSA252)
    SACOL1831(tal)translaldolase  [1] (data from MRSA252)
    SACOL02123-hydroxyacyl-CoA dehydrogenase  [1] (data from MRSA252)
    SACOL2163hypothetical protein  [1] (data from MRSA252)

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: 1
    • Signal Peptide Possibility: -1
    • N-terminally Anchored Score: 1
    • Predicted Cleavage Site: No CleavageSite
  • SignalP: no predicted signal peptide
    • Ymax: 0.124
    • Ymax_pos: 27
    • Cmax: 0.117
    • Cmax_pos: 27
    • Smax: 0.165
    • Smax_pos: 19
    • Smean: 0.117
    • D: 0.121
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MAVKVAINGFGRIGRLAFRRIQEVEGLEVVAVNDLTDDDMLAHLLKYDTMQGRFTGEVEVVDGGFRVNGKEVKSFSEPDASKLPWKDLNIDVVLECTGFYTDKDKAQAHIEAGAKKVLISAPATGDLKTIVFNTNHQELDGSETVVSGASCTTNSLAPVAKVLNDDFGLVEGLMTTIHAYTGDQNTQDAPHRKGDKRRARAAAENIIPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATGSLTELTVVLEKQDVTVEQVNEAMKNASNESFGYTEDEIVSSDVVGMTYGSLFDATQTRVMSVGDRQLVKVAAWYDNEMSYTAQLVRTLAYLAELSK

Experimental data[edit source | edit]

  • experimentally validated: PeptideAtlas
    experimental localization: Cytoplasmic [2] [3] [4] [5] [6]
    quantitative data / protein copy number per cell: 16129 [7]

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator: GapR
    GapR (TF) important in Glycolysis

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: 22.69 h [8]

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. 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 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)
  2. 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)
  3. 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)
  4. Annette Dreisbach, Kristina Hempel, Girbe Buist, Michael Hecker, Dörte Becher, Jan Maarten van Dijl
    Profiling the surfacome of Staphylococcus aureus.
    Proteomics: 2010, 10(17);3082-96
    [PubMed:20662103] [WorldCat.org] [DOI] (I p)
  5. 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)
  6. 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)
  7. 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)
  8. 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]