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NCBI: 02-MAR-2017

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus N315
  • locus tag: SA_RS09430 [old locus tag: SA1669 ]
  • pan locus tag?: SAUPAN004784000
  • symbol: SA_RS09430
  • pan gene symbol?: fumC
  • synonym:
  • product: class II fumarate hydratase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SA_RS09430 [old locus tag: SA1669 ]
  • symbol: SA_RS09430
  • product: class II fumarate hydratase
  • replicon: chromosome
  • strand: -
  • coordinates: 1905519..1906904
  • length: 1386
  • essential: no DEG other strains

⊟Accession numbers[edit | edit source]

  • Location: NC_002745 (1905519..1906904) NCBI
  • BioCyc: SA_RS09430 BioCyc
  • MicrobesOnline: see SA1669

⊟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
    ATGTCAGTAAGAATTGAACATGATACTTTTGGAGAAATAGAAGTACCTGCAGATAAATAT
    TGGGGTGCTCAAACAGAAAGAAGTAAACGCAATTTCCCAGTTGGTAAAGAGCGTATGCCA
    ATCGAAGTAGTTTATGGTTTTGCACAACTAAAGCGTGCAGCAGCATTAGCTAATTTTGAT
    TTAGGAAAATTAAGCGAGGCAAAGAAAGATGCCATTGTATACGCATGTGATCAAATTTTA
    TCAGGTGAATTAGATGAACACTTCCCACTAGTTGTATGGCAAACAGGAAGCGGTACACAA
    AGTAATATGAATGTGAACGAAGTAGTAAGTTATGTTGCTAATATGTATTTAAAAGATCAT
    CAAATTGATGAAAGTATCCACCCAAATGATGATGTAAATGAATCACAAAGTTCGAATGAT
    ACATTCCCAACTGCTATGCACGTTGCATTATATCAAGAGGTTGAAACAAAATTAGAACCT
    GCATTAAAACTTTTAAGAAATACTTTGAAAGAAAAAGAAGACAAATTTGAATCAATTATT
    AAAATTGGTCGTACACATTTACAAGATGCAACGCCGATCAAACTAGGACAAGAGATTAGT
    GGCTGGCGTTATATGCTTGACCGTTGCGAAATAATGTTATCTGAATCTAAGAAGCACATT
    TTAAATCTTGCCATCGGTGGTACGGCTGTTGGTACTGGTATTAATGCGCATCCTGAATTT
    GGTGATAAGGTGGCACATTATATTTCAGAAAATACGGGTTATCCATTTGTATCTTCTGAA
    AATAAATTCCACGCACTTACAGCGCATGATGAAGTTGTTCAATTGCACGGAACATTGAAG
    GCATTAGCTGGAGATTTAATGAAAATTGCTAATGATGTGAGATGGTTGGCTTCAGGTCCA
    CGAGCTGGTTTGGCAGAAATTTCCATCCCTGAAAATGAACCAGGTTCATCAATTATGCCT
    GGTAAAGTTAATCCTACACAATGTGAAATGTTAACAATGGTTGCAGTCCAAGTAATGGGT
    AATGATACAGTTGTTGGCTTCGCAAGTTCACAAGGTAACTTTGAATTGAATGTTTATAAA
    CCAGTTATTATGCATAATACACTACAATCAATTTACCTTTTAGCTGATGGTATGGAAACA
    TTTAATAACAATTGTGCAGTGGGCATTGAGCCAATCGAAGAGAATATTGATAATTATTTA
    AATCAATCATTAATGTTAGTTACTGCATTAAATCCACATATTGGTTATGAAAAAGCAGCT
    CAAATTGCTAAGAAAGCCCATAAAGAAGGTTTAACTTTAAAAGAATCTGCAATTCAAACT
    GGATATGTTACAGAAGAACAATTTGAAGCATGGATTAAACCAGAAGATATGGTAGATCCT
    CATTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1386

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SA_RS09430 [old locus tag: SA1669 ]
  • symbol: SA_RS09430
  • description: class II fumarate hydratase
  • length: 461
  • theoretical pI: 4.862
  • theoretical MW: 51160.7
  • GRAVY: -0.307592

⊟Function[edit | edit source]

  • reaction:
    EC 4.2.1.2?  ExPASy
    Fumarate hydratase (S)-malate = fumarate + H2O
  • TIGRFAM:
    Metabolism Energy metabolism TCA cycle fumarate hydratase, class II (TIGR00979; EC 4.2.1.2; HMM-score: 745.8)
    and 4 more
    Metabolism Energy metabolism Amino acids and amines aspartate ammonia-lyase (TIGR00839; EC 4.3.1.1; HMM-score: 467.7)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis adenylosuccinate lyase (TIGR00928; EC 4.3.2.2; HMM-score: 87.9)
    Metabolism Energy metabolism Other 3-carboxy-cis,cis-muconate cycloisomerase (TIGR02426; EC 5.5.1.2; HMM-score: 71.5)
    Metabolism Amino acid biosynthesis Glutamate family argininosuccinate lyase (TIGR00838; EC 4.3.2.1; HMM-score: 59.3)
  • TheSEED: see SA1669
  • PFAM:
    no clan defined Lyase_1; Lyase (PF00206; HMM-score: 376.7)
    and 3 more
    FumaraseC_C; Fumarase C C-terminus (PF10415; HMM-score: 91.5)
    KNTase_C (CL0291) NTase_sub_bind; Nucleotidyltransferase substrate binding protein like (PF08780; HMM-score: 15.5)
    no clan defined HsbA; Hydrophobic surface binding protein A (PF12296; HMM-score: 12.7)

⊟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:
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.003911
    • TAT(Tat/SPI): 0.000952
    • LIPO(Sec/SPII): 0.000795
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSVRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAALANFDLGKLSEAKKDAIVYACDQILSGELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQIDESIHPNDDVNESQSSNDTFPTAMHVALYQEVETKLEPALKLLRNTLKEKEDKFESIIKIGRTHLQDATPIKLGQEISGWRYMLDRCEIMLSESKKHILNLAIGGTAVGTGINAHPEFGDKVAHYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLNQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDPH

⊟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:
    SA_RS09855(gatA)glutamyl-tRNA(Gln) amidotransferase subunit A  [1] (data from MRSA252)
    SA_RS01960acetyl-CoA acyltransferase  [1] (data from MRSA252)
    SA_RS0291550S ribosomal protein L10  [1] (data from MRSA252)
    SA_RS02930DNA-directed RNA polymerase subunit beta  [1] (data from MRSA252)
    SA_RS02955elongation factor G  [1] (data from MRSA252)
    SA_RS03155phosphate acetyltransferase  [1] (data from MRSA252)
    SA_RS03545hypothetical protein  [1] (data from MRSA252)
    SA_RS03575transcriptional regulator  [1] (data from MRSA252)
    SA_RS04140aldehyde dehydrogenase  [1] (data from MRSA252)
    SA_RS04575NADH dehydrogenase  [1] (data from MRSA252)
    SA_RS04660NAD-specific glutamate dehydrogenase  [1] (data from MRSA252)
    SA_RS04680glucose-6-phosphate isomerase  [1] (data from MRSA252)
    SA_RS04935hypothetical protein  [1] (data from MRSA252)
    SA_RS05350pyruvate dehydrogenase E1 component subunit alpha  [1] (data from MRSA252)
    SA_RS0622530S ribosomal protein S2  [1] (data from MRSA252)
    SA_RS07955molecular chaperone DnaK  [1] (data from MRSA252)
    SA_RS08545isocitrate dehydrogenase (NADP(+))  [1] (data from MRSA252)
    SA_RS11010uracil phosphoribosyltransferase  [1] (data from MRSA252)
    SA_RS1163050S ribosomal protein L17  [1] (data from MRSA252)
    SA_RS11660adenylate kinase  [1] (data from MRSA252)
    SA_RS1167050S ribosomal protein L15  [1] (data from MRSA252)
    SA_RS1168030S ribosomal protein S5  [1] (data from MRSA252)
    SA_RS1175550S ribosomal protein L23  [1] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟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 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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