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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL1908 [new locus tag: SACOL_RS09825 ]
  • pan locus tag?: SAUPAN004784000
  • symbol: fumC
  • pan gene symbol?: fumC
  • synonym:
  • product: fumarate hydratase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL1908 [new locus tag: SACOL_RS09825 ]
  • symbol: fumC
  • product: fumarate hydratase
  • replicon: chromosome
  • strand: -
  • coordinates: 1963566..1964951
  • length: 1386
  • 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
    ATGTCAGTAAGAATTGAACATGATACTTTTGGAGAAATAGAAGTACCTGCAGATAAATAT
    TGGGGTGCTCAAACAGAAAGAAGTAAACGTAATTTCCCAGTTGGTAAAGAGCGTATGCCA
    ATCGAAGTAGTTTATGGTTTTGCACAACTAAAGCGTGCAGCAGCAATAGCTAATTTTGAT
    TTAGGAAAATTAAGCGAGGCAAAGAAAGATGCCATTGTATACGCATGTGATCAAATTTTA
    TCAGGTGAATTAGATGAACACTTCCCACTAGTTGTATGGCAAACAGGAAGCGGTACACAA
    AGTAATATGAATGTGAACGAAGTAGTAAGTTATGTTGCTAATATGTATTTAAAAGATCAT
    CAAAGTGATGAAAGTATCCACCCAAATGATGATGTAAATAAATCTCAAAGTTCGAATGAT
    ACATTCCCAACTGCTATGCACGTTGCATTATATCAAGAGGTTGAAACAAAATTAGAACCT
    GCATTAAAACTTTTAAGAAATACTTTGAAAGAAAAAGAAGATAAATTTGATTCAATTATT
    AAAATTGGTCGTACACATTTACAAGATGCAACGCCGATCAAACTAGGACAAGAGATTAGT
    GGCTGGCGTTATATGCTTGACCGTTGTGAAACAATGTTATCTGAATCTAAGAAGCACATT
    TTAAATCTTGCCATCGGTGGTACGGCTGTTGGTACTGGTATTAATGCGCATCCTGAATTT
    GGTGATAAAGTGGCACATTATATTTCAGAAAATACGGGTTATCCATTTGTATCTTCTGAA
    AATAAATTCCACGCACTTACAGCGCATGATGAAGTTGTTCAATTGCATGGAACATTGAAG
    GCATTAGCAGGAGACTTAATGAAAATTGCTAATGATGTGAGATGGTTGGCTTCAGGGCCA
    CGAGCTGGTTTGGCAGAAATTTCTATCCCTGAAAATGAACCAGGTTCATCAATTATGCCT
    GGTAAAGTTAATCCTACACAATGTGAAATGTTAACAATGGTTGCAGTCCAAGTAATGGGT
    AATGATACAGTTGTTGGCTTCGCAAGTTCACAAGGTAACTTTGAATTGAATGTTTATAAA
    CCAGTTATTATGCATAATACACTACAATCAATTTATCTTTTAGCTGATGGTATGGAAACA
    TTTAATAACAATTGTGCAGTGGGCATTGAACCAATCGAAGAGAATATTGATAATTATTTA
    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: SACOL1908 [new locus tag: SACOL_RS09825 ]
  • symbol: FumC
  • description: fumarate hydratase
  • length: 461
  • theoretical pI: 4.97681
  • theoretical MW: 51107.5
  • GRAVY: -0.329718

⊟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: 751.7)
    and 4 more
    Metabolism Energy metabolism Amino acids and amines aspartate ammonia-lyase (TIGR00839; EC 4.3.1.1; HMM-score: 469.7)
    Metabolism Purines, pyrimidines, nucleosides, and nucleotides Purine ribonucleotide biosynthesis adenylosuccinate lyase (TIGR00928; EC 4.3.2.2; HMM-score: 88.9)
    Metabolism Energy metabolism Other 3-carboxy-cis,cis-muconate cycloisomerase (TIGR02426; EC 5.5.1.2; HMM-score: 73)
    Metabolism Amino acid biosynthesis Glutamate family argininosuccinate lyase (TIGR00838; EC 4.3.2.1; HMM-score: 60.3)
  • TheSEED  :
    • Fumarate hydratase class II (EC 4.2.1.2)
    Carbohydrates Central carbohydrate metabolism TCA Cycle  Fumarate hydratase class II (EC 4.2.1.2)
  • PFAM:
    no clan defined Lyase_1; Lyase (PF00206; HMM-score: 381)
    and 4 more
    FumaraseC_C; Fumarase C C-terminus (PF10415; HMM-score: 91)
    DNA_primase_lrg (CL0242) DNA_primase_lrg; Eukaryotic and archaeal DNA primase, large subunit (PF04104; HMM-score: 16)
    KNTase_C (CL0291) NTase_sub_bind; Nucleotidyltransferase substrate binding protein like (PF08780; HMM-score: 15.4)
    no clan defined HsbA; Hydrophobic surface binding protein A (PF12296; HMM-score: 14.4)

⊟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: 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): 0.003889
    • TAT(Tat/SPI): 0.000959
    • LIPO(Sec/SPII): 0.000775
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MSVRIEHDTFGEIEVPADKYWGAQTERSKRNFPVGKERMPIEVVYGFAQLKRAAAIANFDLGKLSEAKKDAIVYACDQILSGELDEHFPLVVWQTGSGTQSNMNVNEVVSYVANMYLKDHQSDESIHPNDDVNKSQSSNDTFPTAMHVALYQEVETKLEPALKLLRNTLKEKEDKFDSIIKIGRTHLQDATPIKLGQEISGWRYMLDRCETMLSESKKHILNLAIGGTAVGTGINAHPEFGDKVAHYISENTGYPFVSSENKFHALTAHDEVVQLHGTLKALAGDLMKIANDVRWLASGPRAGLAEISIPENEPGSSIMPGKVNPTQCEMLTMVAVQVMGNDTVVGFASSQGNFELNVYKPVIMHNTLQSIYLLADGMETFNNNCAVGIEPIEENIDNYLNQSLMLVTALNPHIGYEKAAQIAKKAHKEGLTLKESAIQTGYVTEEQFEAWIKPEDMVDPH

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 191 [5]
  • interaction partners:
    SACOL2218(adk)adenylate kinase  [6] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL0634(eutD)phosphotransacetylase  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL1961(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [6] (data from MRSA252)
    SACOL0961(gluD)glutamate dehydrogenase  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL0966(pgi)glucose-6-phosphate isomerase  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [6] (data from MRSA252)
    SACOL2237(rplW)50S ribosomal protein L23  [6] (data from MRSA252)
    SACOL0588(rpoB)DNA-directed RNA polymerase subunit beta  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2104(upp)uracil phosphoribosyltransferase  [6] (data from MRSA252)
    SACOL0426acetyl-CoA acetyltransferase  [6] (data from MRSA252)
    SACOL0721hypothetical protein  [6] (data from MRSA252)
    SACOL0727hypothetical protein  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL1020hypothetical protein  [6] (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. ↑ 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 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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