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NCBI: 26-AUG-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA0915 [new locus tag: SA_RS05190 ]
  • 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: SA0915 [new locus tag: SA_RS05190 ]
  • symbol: folD
  • product: bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase
  • replicon: chromosome
  • strand: -
  • coordinates: 1040543..1041403
  • length: 861
  • essential: no DEG 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
    GGATTTCATCCAATAAATATAGGGAAATTATATATCGATGAACAAACTTTTGTACCTTGC
    ACACCGCTCGGCATCATGGAAATATTAAAACATGCTGATATTGATTTAGAAGCTAAAAAT
    GCAGTTGTAATTGGACGAAGTCATATTGTCGGACAACCAGTTTCTAAGTTACTACTTCAA
    AAAAATGCATCAGTAACAATCTTACATTCTCGTTCAAAAGATATGGCATCATATTTAAAA
    GATGCTGATGTCATTGTCAGTGCAGTTGGTAAGCCTAGTTTAGTAACAAAAGATGTGGTC
    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: SA0915 [new locus tag: SA_RS05190 ]
  • symbol: FolD
  • description: bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase
  • length: 286
  • theoretical pI: 5.24534
  • theoretical MW: 30887.4
  • GRAVY: -0.121678

⊟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:
  • 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: 219.8)
    and 4 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: 14.8)
    Phosphatase (CL0031) PTS_IIB; PTS system, Lactose/Cellobiose specific IIB subunit (PF02302; HMM-score: 13.8)

⊟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]

  • MVAKILDGKQIAKDYRQGLQDQVEALKEKGFTPKLSVILVGNDGASQSYVRSKKKAAEKIGMISEIVHLEETATEEEVLNELNRLNNDDSVSGILVQVPLPKQVSEQKILEAINPEKDVDGFHPINIGKLYIDEQTFVPCTPLGIMEILKHADIDLEAKNAVVIGRSHIVGQPVSKLLLQKNASVTILHSRSKDMASYLKDADVIVSAVGKPSLVTKDVVKEGAVIIDVGNTPDENGKLKGDVDYDAVKEIAGAITPVPGGVGPLTITMVLNNTLLAEKMRRGIDS

⊟Experimental data[edit | edit source]

  • experimentally validated: data available for COL, NCTC8325
  • protein localization: data available for COL
  • quantitative data / protein copy number per cell: data available for COL
  • interaction partners:
    SA0162(aldA)hypothetical protein  [1] (data from MRSA252)
    SA2428(arcA)arginine deiminase  [1] (data from MRSA252)
    SA2425(arcC)carbamate kinase  [1] (data from MRSA252)
    SA1984(asp23)alkaline shock protein 23  [1] (data from MRSA252)
    SA1517(citC)isocitrate dehydrogenase  [1] (data from MRSA252)
    SA1409(dnaK)molecular chaperone DnaK  [1] (data from MRSA252)
    SA1927(fbaA)fructose-bisphosphate aldolase  [1] (data from MRSA252)
    SA0505(fus)elongation factor G  [1] (data from MRSA252)
    SA1305(hu)DNA-binding protein II  [1] (data from MRSA252)
    SA1608(metK)S-adenosylmethionine synthetase  [1] (data from MRSA252)
    SA0686(nrdE)ribonucleotide-diphosphate reductase subunit alpha  [1] (data from MRSA252)
    SA1244(odhB)dihydrolipoamide succinyltransferase  [1] (data from MRSA252)
    SA0943-1(pdhA)pyruvate dehydrogenase E1 component subunit alpha  [1] (data from MRSA252)
    SA0944(pdhB)pyruvate dehydrogenase E1 component subunit beta  [1] (data from MRSA252)
    SA0945(pdhC)branched-chain alpha-keto acid dehydrogenase E2 subunit  [1] (data from MRSA252)
    SA0946(pdhD)dihydrolipoamide dehydrogenase  [1] (data from MRSA252)
    SA1938(pdp)pyrimidine-nucleoside phosphorylase  [1] (data from MRSA252)
    SA0218(pflB)formate acetyltransferase  [1] (data from MRSA252)
    SA1520(pykA)pyruvate kinase  [1] (data from MRSA252)
    SA0496(rplA)50S ribosomal protein L1  [1] (data from MRSA252)
    SA2044(rplB)50S ribosomal protein L2  [1] (data from MRSA252)
    SA2035(rplE)50S ribosomal protein L5  [1] (data from MRSA252)
    SA2033(rplF)50S ribosomal protein L6  [1] (data from MRSA252)
    SA0497(rplJ)50S ribosomal protein L10  [1] (data from MRSA252)
    SA0498(rplL)50S ribosomal protein L7/L12  [1] (data from MRSA252)
    SA2029(rplO)50S ribosomal protein L15  [1] (data from MRSA252)
    SA1084(rplS)50S ribosomal protein L19  [1] (data from MRSA252)
    SA1473(rplU)50S ribosomal protein L21  [1] (data from MRSA252)
    SA2042(rplV)50S ribosomal protein L22  [1] (data from MRSA252)
    SA0501(rpoC)DNA-directed RNA polymerase subunit beta'  [1] (data from MRSA252)
    SA1099(rpsB)30S ribosomal protein S2  [1] (data from MRSA252)
    SA2041(rpsC)30S ribosomal protein S3  [1] (data from MRSA252)
    SAS052(rpsD)30S ribosomal protein S4  [1] (data from MRSA252)
    SA2031(rpsE)30S ribosomal protein S5  [1] (data from MRSA252)
    SA2016(rpsI)30S ribosomal protein S9  [1] (data from MRSA252)
    SA2024(rpsK)30S ribosomal protein S11  [1] (data from MRSA252)
    SA2043(rpsS)30S ribosomal protein S19  [1] (data from MRSA252)
    SA0506(tuf)elongation factor Tu  [1] (data from MRSA252)
    SA0351GTP-dependent nucleic acid-binding protein EngD  [1] (data from MRSA252)
    SA0627hypothetical protein  [1] (data from MRSA252)
    SA0802hypothetical protein  [1] (data from MRSA252)
    SA0829hypothetical protein  [1] (data from MRSA252)
    SA1532hypothetical protein  [1] (data from MRSA252)
    SA1812hypothetical protein  [1] (data from MRSA252)
    SA1813hypothetical protein  [1] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: PurR (repression) regulon
    PurR(TF)important in Purine metabolism; RegPrecise 

⊟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. ↑ 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 1.13 1.14 1.15 1.16 1.17 1.18 1.19 1.20 1.21 1.22 1.23 1.24 1.25 1.26 1.27 1.28 1.29 1.30 1.31 1.32 1.33 1.34 1.35 1.36 1.37 1.38 1.39 1.40 1.41 1.42 1.43 1.44 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]

Alexander Scherl, Patrice François, Manuela Bento, Jacques M Deshusses, Yvan Charbonnier, Véronique Converset, Antoine Huyghe, Nadia Walter, Christine Hoogland, Ron D Appel, Jean-Charles Sanchez, Catherine G Zimmermann-Ivol, Garry L Corthals, Denis F Hochstrasser, Jacques Schrenzel
Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth.
J Microbiol Methods: 2005, 60(2);247-57
[PubMed:15590099] [WorldCat.org] [DOI] (P p)

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