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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1321 [new locus tag: SACOL_RS06730 ]
  • pan locus tag?: SAUPAN003613000
  • symbol: glpD
  • pan gene symbol?: glpD
  • synonym:
  • product: aerobic glycerol-3-phosphate dehydrogenase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1321 [new locus tag: SACOL_RS06730 ]
  • symbol: glpD
  • product: aerobic glycerol-3-phosphate dehydrogenase
  • replicon: chromosome
  • strand: +
  • coordinates: 1338709..1340382
  • length: 1674
  • 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
    1261
    1321
    1381
    1441
    1501
    1561
    1621
    ATGGCATTGTCTACTTTTAAGAGAGAACATATTAAAAAGAATTTAAGAAATGATGAATAT
    GATTTAGTAATTATTGGTGGCGGTATTACAGGTGCAGGTATTGCACTAGACGCGAGTGAA
    AGAGGAATGAAAGTTGCATTAGTTGAAATGCAAGACTTTGCACAAGGAACAAGCTCAAGA
    TCTACAAAATTAGTCCATGGTGGTTTGCGTTACTTAAAACAATTCCAAATTGGAGTAGTT
    GCCGAAACTGGTAAAGAACGTGCGATTGTTTATGAAAATGGGCCTCATGTTACGACTCCA
    GAGTGGATGCTTTTACCAATGCATAAAGGTGGAACATTTGGTAAATTCTCAACATCAATT
    GGTTTAGGAATGTATGATCGTTTAGCAGGTGTTAAGAAGTCTGAACGTAAAAAAATGTTA
    TCTAAAAAAGAAACTTTAGCTAAAGAACCATTAGTTAAAAAAGAAGGTCTAAAAGGCGGC
    GGTTACTATGTTGAATATCGTACTGACGATGCGCGTTTAACTATTGAAGTTATGAAGCGT
    GCTGCTGAAAAAGGCGCAGAAATTATCAACTATACTAAATCTGAACACTTCACTTATGAT
    AAAAATCAACAAGTAAATGGTGTTAAAGTTATAGATAAATTAACTAATGAAAATTATACA
    ATTAAGGCTAAAAAAGTGGTTAATGCAGCAGGTCCATGGGTTGATGATGTTAGAAGTGGT
    GATTATGCACGCAATAATAAAAAATTACGTTTAACTAAAGGTGTACATGTTGTTATTGAT
    CAATCAAAATTCCCATTAGGTCAAGCAGTATACTTTGATACTGAAAAAGATGGAAGAATG
    ATTTTTGCAATTCCACGTGAAGGAAAAGCGTATGTAGGTACTACAGATACATTCTATGAC
    AATATCAAATCTTCACCATTAACTACACAAGAAGACAGAGACTATTTAATCGATGCGATT
    AATTACATGTTCCCTAGTGTTAATGTTACAGATGAAGATATTGAATCAACATGGGCAGGA
    ATTAGACCATTAATTTACGAAGAAGGCAAAGACCCTTCTGAAATCTCTCGTAAGGATGAA
    ATTTGGGAAGGTAAATCAGGTTTATTAACTATTGCAGGTGGTAAATTAACAGGCTATCGT
    CACATGGCTCAAGACATTGTTGATTTAGTATCTAAACGCTTGAAAAAAGACTACGGTTTA
    ACATTTAGTCCATGTAATACAAAAGGTCTGGCAATTTCAGGTGGCGATGTAGGTGGTAGC
    AAGAACTTTGATGCGTTTGTAGAGCAAAAAGTAGATGTAGCTAAAGGATTCGGCATTGAT
    GAAGATGTTGCAAGACGTTTAGCATCTAAATATGGTTCAAATGTTGATGAATTGTTCAAC
    ATTGCGCAAACATCTCAATACCATGATAGCAAGTTACCATTAGAAATTTATGTAGAACTT
    GTTTATAGTATTCAACAAGAAATGGTATACAAACCTAACGATTTCTTAGTTCGTCGTTCT
    GGTAAAATGTATTTCAATATTAAAGATGTATTAGATTATAAAGATGCTGTCATCGATATT
    ATGGCAGATATGCTTGATTACTCTCCAGCTCAAATTGAAGCATATACTGAAGAAGTTGAG
    CAAGCAATTAAAGAAGCGCAACATGGAAATAATCAACCAGCAGTTAAAGAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1560
    1620
    1674

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1321 [new locus tag: SACOL_RS06730 ]
  • symbol: GlpD
  • description: aerobic glycerol-3-phosphate dehydrogenase
  • length: 557
  • theoretical pI: 7.03905
  • theoretical MW: 62387.5
  • GRAVY: -0.490844

⊟Function[edit | edit source]

  • reaction:
    EC 1.1.5.3?  ExPASy
    Glycerol-3-phosphate dehydrogenase sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
  • TIGRFAM:
    Metabolism Energy metabolism Anaerobic glycerol-3-phosphate dehydrogenase, anaerobic, A subunit (TIGR03377; EC 1.1.5.3; HMM-score: 175.5)
    and 26 more
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine glycine oxidase ThiO (TIGR02352; EC 1.4.3.19; HMM-score: 48.2)
    FAD dependent oxidoreductase TIGR03364 (TIGR03364; HMM-score: 33.8)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Chlorophyll and bacteriochlorphyll geranylgeranyl reductase family (TIGR02032; EC 1.3.1.-; HMM-score: 31.8)
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain (TIGR03197; HMM-score: 27.4)
    Metabolism Energy metabolism Electron transport flavocytochrome c (TIGR01813; HMM-score: 23.5)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone 2-polyprenyl-6-methoxyphenol 4-hydroxylase (TIGR01984; EC 1.14.13.-; HMM-score: 22)
    Metabolism Energy metabolism Anaerobic glycerol-3-phosphate dehydrogenase, anaerobic, B subunit (TIGR03378; EC 1.1.5.3; HMM-score: 19.4)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family (TIGR01988; EC 1.14.13.-; HMM-score: 18.9)
    dihydrolipoyl dehydrogenase (TIGR01350; EC 1.8.1.4; HMM-score: 18.3)
    lycopene cyclase family protein (TIGR01790; HMM-score: 18)
    Cellular processes Cellular processes Detoxification alkyl hydroperoxide reductase subunit F (TIGR03140; EC 1.8.1.-; HMM-score: 16.1)
    Cellular processes Cellular processes Adaptations to atypical conditions alkyl hydroperoxide reductase subunit F (TIGR03140; EC 1.8.1.-; HMM-score: 16.1)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other tyrosine decarboxylase MnfA (TIGR03812; EC 4.1.1.25; HMM-score: 14.7)
    Metabolism Energy metabolism Amino acids and amines sarcosine oxidase, alpha subunit family (TIGR01372; HMM-score: 14.6)
    Metabolism Energy metabolism Amino acids and amines sarcosine oxidase, monomeric form (TIGR01377; HMM-score: 14.2)
    squalene-associated FAD-dependent desaturase (TIGR03467; HMM-score: 13.5)
    putative aminophosphonate oxidoreductase (TIGR03329; HMM-score: 13.2)
    Metabolism Energy metabolism Amino acids and amines sarcosine oxidase, beta subunit family (TIGR01373; HMM-score: 12.3)
    Metabolism Energy metabolism TCA cycle succinate dehydrogenase or fumarate reductase, flavoprotein subunit (TIGR01812; HMM-score: 12.2)
    Metabolism Energy metabolism Anaerobic succinate dehydrogenase or fumarate reductase, flavoprotein subunit (TIGR01812; HMM-score: 12.2)
    Metabolism Energy metabolism Aerobic succinate dehydrogenase or fumarate reductase, flavoprotein subunit (TIGR01812; HMM-score: 12.2)
    Metabolism Energy metabolism TCA cycle succinate dehydrogenase, flavoprotein subunit (TIGR01816; HMM-score: 11.9)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Thiamine thiazole biosynthesis enzyme (TIGR00292; HMM-score: 11.6)
    Metabolism Energy metabolism Electron transport thioredoxin-disulfide reductase (TIGR01292; EC 1.8.1.9; HMM-score: 11.3)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other C-3',4' desaturase CrtD (TIGR02733; EC 1.3.99.-; HMM-score: 10.2)
    Cellular processes Cellular processes Detoxification mercury(II) reductase (TIGR02053; EC 1.16.1.1; HMM-score: 9.7)
  • TheSEED  :
    • Aerobic glycerol-3-phosphate dehydrogenase (EC 1.1.5.3)
    Carbohydrates Sugar alcohols Glycerol and Glycerol-3-phosphate Uptake and Utilization  Aerobic glycerol-3-phosphate dehydrogenase (EC 1.1.5.3)
    and 2 more
    Fatty Acids, Lipids, and Isoprenoids Phospholipids Glycerolipid and Glycerophospholipid Metabolism in Bacteria  Aerobic glycerol-3-phosphate dehydrogenase (EC 1.1.5.3)
    Respiration Electron donating reactions Respiratory dehydrogenases 1  Aerobic glycerol-3-phosphate dehydrogenase (EC 1.1.5.3)
  • PFAM:
    NADP_Rossmann (CL0063) DAO; FAD dependent oxidoreductase (PF01266; HMM-score: 193)
    and 11 more
    no clan defined DAO_C; C-terminal domain of alpha-glycerophosphate oxidase (PF16901; HMM-score: 83.7)
    NADP_Rossmann (CL0063) FAD_binding_3; FAD binding domain (PF01494; HMM-score: 29)
    FAD_binding_2; FAD binding domain (PF00890; HMM-score: 27.9)
    Pyr_redox_2; Pyridine nucleotide-disulphide oxidoreductase (PF07992; HMM-score: 23.7)
    Pyr_redox; Pyridine nucleotide-disulphide oxidoreductase (PF00070; HMM-score: 23)
    NAD_binding_8; NAD(P)-binding Rossmann-like domain (PF13450; HMM-score: 17.7)
    Lycopene_cycl; Lycopene cyclase protein (PF05834; HMM-score: 17.1)
    FAD_oxidored; FAD dependent oxidoreductase (PF12831; HMM-score: 16.3)
    GIDA; Glucose inhibited division protein A (PF01134; HMM-score: 16)
    3HCDH_N; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain (PF02737; HMM-score: 12.8)
    HI0933_like; HI0933-like protein (PF03486; HMM-score: 11.1)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors: FAD
  • 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): 0.007739
    • TAT(Tat/SPI): 0.004601
    • LIPO(Sec/SPII): 0.0012
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MALSTFKREHIKKNLRNDEYDLVIIGGGITGAGIALDASERGMKVALVEMQDFAQGTSSRSTKLVHGGLRYLKQFQIGVVAETGKERAIVYENGPHVTTPEWMLLPMHKGGTFGKFSTSIGLGMYDRLAGVKKSERKKMLSKKETLAKEPLVKKEGLKGGGYYVEYRTDDARLTIEVMKRAAEKGAEIINYTKSEHFTYDKNQQVNGVKVIDKLTNENYTIKAKKVVNAAGPWVDDVRSGDYARNNKKLRLTKGVHVVIDQSKFPLGQAVYFDTEKDGRMIFAIPREGKAYVGTTDTFYDNIKSSPLTTQEDRDYLIDAINYMFPSVNVTDEDIESTWAGIRPLIYEEGKDPSEISRKDEIWEGKSGLLTIAGGKLTGYRHMAQDIVDLVSKRLKKDYGLTFSPCNTKGLAISGGDVGGSKNFDAFVEQKVDVAKGFGIDEDVARRLASKYGSNVDELFNIAQTSQYHDSKLPLEIYVELVYSIQQEMVYKPNDFLVRRSGKMYFNIKDVLDYKDAVIDIMADMLDYSPAQIEAYTEEVEQAIKEAQHGNNQPAVKE

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 1239 [5]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: CcpA regulon
    CcpA(TF)important in Carbon catabolism; RegPrecise    transcription unit transferred from N315 data RegPrecise 

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 12.45 h [6]

⊟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. ↑ 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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