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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1072 [new locus tag: SACOL_RS05470 ]
  • pan locus tag?: SAUPAN003276000
  • symbol: folD
  • pan gene symbol?: folD
  • synonym:
  • product: bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1072 [new locus tag: SACOL_RS05470 ]
  • symbol: folD
  • product: bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase
  • replicon: chromosome
  • strand: -
  • coordinates: 1081861..1082721
  • length: 861
  • 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
    ATGGTTGCTAAAATTTTAGATGGTAAACAAATTGCCAAAGACTACAGACAGGGGTTACAA
    GATCAAGTTGAAGCGCTAAAAGAAAAGGGTTTTACACCTAAATTATCCGTTATATTAGTT
    GGTAATGATGGCGCTAGTCAAAGTTATGTTAGATCAAAAAAGAAAGCAGCTGAAAAAATT
    GGTATGATTTCAGAAATCGTACATTTGGAAGAAACAGCTACTGAAGAAGAAGTATTAAAC
    GAACTAAATAGACTAAATAATGATGATTCTGTAAGTGGTATTTTGGTACAAGTACCATTA
    CCAAAACAAGTTAGCGAACAGAAAATATTAGAAGCAATCAATCCTGAAAAAGATGTGGAC
    GGTTTTCATCCAATAAATATAGGGAAATTATATATCGATGAACAAACTTTTGTACCTTGC
    ACACCGCTCGGCATCATGGAAATATTAAAACATGCTGATATTGATTTAGAAGGTAAAAAT
    GCAGTTGTAATTGGACGAAGTCATATTGTCGGACAACCAGTTTCTAAGTTACTACTTCAA
    AAAAATGCATCAGTAACAATCTTACATTCTCGTTCAAAAGATATGGCATCATATTTAAAA
    GATGCTGATGTCATTGTCAGTGCAGTTGGTAAGCCTGGTTTAGTAACAAAAGATGTGGTC
    AAAGAAGGAGCAGTAATTATCGATGTTGGCAATACGCCAGATGAAAATGGCAAATTAAAA
    GGTGACGTTGATTATGATGCGGTTAAAGAAATTGCTGGAGCTATTACACCAGTTCCTGGT
    GGCGTTGGTCCATTAACAATTACTATGGTATTAAATAATACTTTGCTTGCAGAAAAAATG
    CGTCGAGGTATTGATTCGTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    861

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL1072 [new locus tag: SACOL_RS05470 ]
  • symbol: FolD
  • description: bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase
  • length: 286
  • theoretical pI: 5.24534
  • theoretical MW: 30843.3
  • GRAVY: -0.127972

⊟Function[edit | edit source]

  • reaction:
    EC 1.5.1.5?  ExPASy
    Methylenetetrahydrofolate dehydrogenase (NADP+) 5,10-methylenetetrahydrofolate + NADP+ = 5,10-methenyltetrahydrofolate + NADPH
    EC 3.5.4.9?  ExPASy
    Methenyltetrahydrofolate cyclohydrolase 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate
  • TIGRFAM:
    Unknown function General putative RNA-binding protein, YhbY family (TIGR00253; HMM-score: 11.1)
  • TheSEED  :
    • Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)
    • Methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5)
    Carbohydrates One-carbon Metabolism One-carbon metabolism by tetrahydropterines  Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)
    and 4 more
    Carbohydrates One-carbon Metabolism One-carbon metabolism by tetrahydropterines  Methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5)
    Carbohydrates One-carbon Metabolism Serine-glyoxylate cycle  Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)
    Carbohydrates One-carbon Metabolism Serine-glyoxylate cycle  Methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5)
    Cofactors, Vitamins, Prosthetic Groups, Pigments Folate and pterines Folate Biosynthesis  Methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5)
  • PFAM:
    NADP_Rossmann (CL0063) THF_DHG_CYH_C; Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain (PF02882; HMM-score: 222.8)
    and 3 more
    AA_dh_N (CL0603) THF_DHG_CYH; Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain (PF00763; HMM-score: 139.6)
    NADP_Rossmann (CL0063) AlaDh_PNT_C; Alanine dehydrogenase/PNT, C-terminal domain (PF01262; HMM-score: 17)
    Shikimate_DH; Shikimate / quinate 5-dehydrogenase (PF01488; HMM-score: 13.7)

⊟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): 0.003408
    • TAT(Tat/SPI): 0.000272
    • LIPO(Sec/SPII): 0.000481
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEGKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPGLVTKDVVKEGAVIIDVGNTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMRRGIDS

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 886 [5]
  • interaction partners:
    SACOL0154(aldA1)aldehyde dehydrogenase  [6] (data from MRSA252)
    SACOL2657(arcA)arginine deiminase  [6] (data from MRSA252)
    SACOL2654(arcC2)carbamate kinase  [6] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL2117(fbaA)fructose-bisphosphate aldolase  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1837(metK)S-adenosylmethionine synthetase  [6] (data from MRSA252)
    SACOL0792(nrdE)ribonucleotide-diphosphate reductase subunit alpha  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0586(rplL)50S ribosomal protein L7/L12  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL2234(rplV)50S ribosomal protein L22  [6] (data from MRSA252)
    SACOL0589(rpoC)DNA-directed RNA polymerase subunit beta'  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL2235(rpsS)30S ribosomal protein S19  [6] (data from MRSA252)
    SACOL1448(sucB)dihydrolipoamide succinyltransferase  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0435GTP-dependent nucleic acid-binding protein EngD  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)
    SACOL2004leukocidin subunit precursor  [6] (data from MRSA252)
    SACOL2006Aerolysin/leukocidin family protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • data available for N315

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: no data available

⊟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. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 6.18 6.19 6.20 6.21 6.22 6.23 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 6.36 6.37 6.38 6.39 6.40 6.41 6.42 6.43 6.44 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)

⊟Relevant publications[edit | edit source]

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