From AureoWiki
Jump to navigation Jump to search

NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2301 [new locus tag: SACOL_RS12105 ]
  • pan locus tag?: SAUPAN005786000
  • symbol: SACOL2301
  • pan gene symbol?: fdhA
  • synonym:
  • product: formate dehydrogenase subunit alpha

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2301 [new locus tag: SACOL_RS12105 ]
  • symbol: SACOL2301
  • product: formate dehydrogenase subunit alpha
  • replicon: chromosome
  • strand: -
  • coordinates: 2361126..2364080
  • length: 2955
  • 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
    1681
    1741
    1801
    1861
    1921
    1981
    2041
    2101
    2161
    2221
    2281
    2341
    2401
    2461
    2521
    2581
    2641
    2701
    2761
    2821
    2881
    2941
    ATGCAAGAACATTTGGTGGTTACACTTGATGGAAAAGATTATCTTGTAGAACCAGGTACG
    AATTTACTTGAATTTATTAAATCACAAGATACTTTTGTACCTTCAATTTGTTATAACGAG
    TCGATGGGACCAATTCAAACATGTGATACATGTACTGTTGAGATTGACGGTAAAATTGAA
    CGTTCATGTAGTACGGTGATTGATCGTCCAATGACTGTAAATACTGTGAACAATGATGTG
    AAAGATGCTCAAAAAGAAGCGCTTGATCGAATTTTAGAAAAGCATATGCTGTATTGTACA
    GTATGTGATTATAATAATGGTGATTGTGAAATTCATAATACGATGGATGCATGGGGGCTT
    CAGCATCAAACGTATGAATATAAAGAGAAGCCATACGAAAAAGATTACGGCCCATTTTAT
    CGTTATGATCCAAATCAATGTATCTTATGTGGGCGTTGTGTAGAAGCATGTCAAGATATC
    GAAGTGAATGAAACTATTAGAATTGATTGGGATCGTGAACATCCACGTGTTATTTGGGAT
    AATGATGTACCGATTAATGAGTCTTCATGTGTATCTTGTGGTCAATGTGCGACGGTATGT
    CCATGTAATGCCATGATGGAAGTGAATATGGAAGGTAATGCGGGTTATATGACTGATACG
    GAACCTGGTTCATTAGCAGCAATGATTGATTTAACTAAAAAAGCAGAACCTGGTTATGGT
    CCACTATTTGCAATCTCAGATTCAGAAGCAGAAATGCGTAAAGAGCGTATTAAGAAAACT
    AAAACAGTGTGTACTTATTGTGGTGTGGGTTGTTCATTTGAAGTTTGGACTAAAGATAGA
    GAAATTTTAAAAGTACAACCATCACATGATTCTCCAGCAAATAAAATTGCGACTTGTGTT
    AAAGGTAAGTTTTCATGGGGACATATTAATTCAGATCAACGATTAACTAAACCACTAGTA
    AGGAAAAATGGTGAGTTCCATGAAGTAGAATGGGATGAAGCTTTAAACGTCATTGCAGAT
    AATTTTACAGCTATTAAAGAAAAGCATGGCCCAGATGCACTATCATTCATTTCTTCTTCT
    AAAGCGACGAATGAAGAATCGTATTTAATGCAAAAATTAGCAAGACAAGTTATTGGCACA
    AATAACGTTGATAACTGTTCAAGATATTGCCAAGCACCTGCAACAAAAGGCTTATTTAGA
    ACGGTTGGACACGGCGGTGACTCAGGTAGTATTGAAGATTTAGAAAAAGCGGCAATGTCT
    GTATTGATAGGTACTAATACAGCCGAAGCTCATCCAGTTATCGCATCACGCATGAAACGT
    GCACAAAAATTATTTGGTCAAAAAATACATGTATTTGATATTAGAAAACATGAAATGGCA
    GAACGTGCGGATCGTTTTTATCAACCTAAACCAGGTACGGATTTAGCGTGGTTAAGTGCA
    GTGACTAAGTATATTATTGATCATGATTTACACGATAAAGCATTTATTGATGAGTGGGTA
    GATGATTTTGATGAATATTACAAATCATTAGAAACATTTACAATGGCTTTTGCTGAAGAA
    GCAACAGGTATTCCTGAATCAGAATTGATTAAATTTGCTGAAGAATGTGCTAAAGCTGAA
    TCTGTTGTAATTTGTTGGGCAATGGGTATTACACAACAAGACATTGGTAGTGACTCAAGT
    ACAGCGATTTCAAACTTATTATTAGTAACAGGTAATTATCGTCGTCCTGGTACTGGTGCG
    TATCCATTACGTGGACATAATAATGTTCAAGGATGTAGTGATATGGGAAGTATGCCTGAT
    AAGATTACTGGTTATCAAAGTATTGAAGCGGATGATATTCGCGCTAAATTTGAAAAAGAA
    TATGGCGTTAAATTGAATCCAAAAGCTGGTAAAGATAATCATGAAATGGTAGAAGGTATA
    CATGACGGAGAAGTACACTCATTGTACTTATATGGTGAAGATACGGGTATTGTGGATTCA
    AATATTAATTTTGTACAAGCTGCGTTTGAAAAATTAGATTTCATGGTAGTCCAAGATGAA
    TTTTTAACATTCACAGCAACATACGCAGATGTTGTATTGCCAGCAAGTCCTTCACTTGAA
    AAAGACGGTACTTTTACAAATACCGAACGTCGTATTCAACGTTTATACCAAGCATTAGAA
    CCTCTTGGTGATTCAAAACCTGACTGGAAAATTTTCCAAGCAATTGCTAATAGATTAGGA
    TTTGATTGGAATTACAAGCATCCTAGTGAAATTATGGATGAAGTAGCACGCTTAACACCT
    CTATATGCTGGGGTAAGTTATGATCGTTTAGAAGGATTCAATAGTTTACAATGGCCAGTA
    CAACCTGATGGTACTGATGAGCCTATTCTATACTTAGAAGGATTCAATTTTGATAATGGT
    AAAGCAAAATTATTCCCATTATCATTTGATAATTACTTTAAGCAAGATGAAATTTATGAT
    ATTCATGTAAACAATGGTCGATTGTTAGAGCACTTCCATGAAGGTAATATGACTTATCAA
    ACACCAATGATTAAATACAAAGTGCCACGTGCATTTGTTGAAATTTCTCCAGAGCTTGCT
    GAAGATAGAGGCATTCATGAAGGTGCAGAAGTTAAGCTGATTTCTGAAACAGGAGAAGCG
    GTATTACAAGTTCACGTGACAGATCGTGTTAAAGGTAAAGAAATCTATATTCCATTAAAT
    AATGATGCGATGGAAAATGGAGATCTAGGTGCAATTAACTTATTAACTAATAGTGATGTT
    GATCAATACACGGATACACCATCTTATAAACGTACTAGCTGTCGTTTGGAGGTAATTACG
    AAACGTGGTAAGTCACCGTTGAACCCTAATAATTTCCGTGTCAATAAAAAACGTCAACCG
    CAGTACAGTGTTCAAGTACAGAAAAAATGGGAACGTTCAGATTATGTTTTCCCGGGAAAT
    CAGGTGGATAAATAA
    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
    1680
    1740
    1800
    1860
    1920
    1980
    2040
    2100
    2160
    2220
    2280
    2340
    2400
    2460
    2520
    2580
    2640
    2700
    2760
    2820
    2880
    2940
    2955

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2301 [new locus tag: SACOL_RS12105 ]
  • symbol: SACOL2301
  • description: formate dehydrogenase subunit alpha
  • length: 984
  • theoretical pI: 4.75761
  • theoretical MW: 111243
  • GRAVY: -0.523679

⊟Function[edit | edit source]

  • reaction:
    EC 1.17.1.9?  ExPASy
    Formate dehydrogenase Formate + NAD+ = CO2 + NADH
  • TIGRFAM:
    formate dehydrogenase, alpha subunit (TIGR01591; EC 1.2.1.2; HMM-score: 803.3)
    and 39 more
    Metabolism Central intermediary metabolism Nitrogen metabolism periplasmic nitrate reductase, large subunit (TIGR01706; EC 1.7.99.4; HMM-score: 289.5)
    Metabolism Energy metabolism Electron transport periplasmic nitrate reductase, large subunit (TIGR01706; EC 1.7.99.4; HMM-score: 289.5)
    Metabolism Energy metabolism Aerobic periplasmic nitrate reductase, large subunit (TIGR01706; EC 1.7.99.4; HMM-score: 289.5)
    oxidoreductase alpha (molybdopterin) subunit (TIGR01701; HMM-score: 248.8)
    Metabolism Energy metabolism Electron transport NADH dehydrogenase (quinone), G subunit (TIGR01973; EC 1.6.99.5; HMM-score: 246.3)
    Metabolism Energy metabolism Anaerobic formate dehydrogenase-N alpha subunit (TIGR01553; EC 1.1.5.6; HMM-score: 228.2)
    Metabolism Energy metabolism Electron transport formate dehydrogenase-N alpha subunit (TIGR01553; EC 1.1.5.6; HMM-score: 228.2)
    anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family (TIGR02166; HMM-score: 168.7)
    Metabolism Energy metabolism Electron transport arsenite oxidase, large subunit (TIGR02693; EC 1.20.9.1; HMM-score: 143.3)
    DMSO reductase family type II enzyme, molybdopterin subunit (TIGR03479; HMM-score: 126.7)
    molybdopterin guanine dinucleotide-containing S/N-oxide reductases (TIGR00509; HMM-score: 114.7)
    formylmethanofuran dehydrogenase subunit B (TIGR03129; EC 1.2.99.5; HMM-score: 85.3)
    trimethylamine-N-oxide reductase TorA (TIGR02164; EC 1.7.2.3; HMM-score: 59.8)
    Metabolism Energy metabolism Anaerobic nitrate reductase, alpha subunit (TIGR01580; EC 1.7.99.4; HMM-score: 48.8)
    [FeFe] hydrogenase, group A (TIGR02512; EC 1.12.-.-; HMM-score: 48.7)
    glycyl-radical enzyme activating protein (TIGR02494; EC 1.97.1.-; HMM-score: 18.7)
    Metabolism Energy metabolism Electron transport electron transport complex, RnfABCDGE type, C subunit (TIGR01945; HMM-score: 17.7)
    Metabolism Central intermediary metabolism Sulfur metabolism sulfite reductase, subunit C (TIGR02912; EC 1.8.-.-; HMM-score: 16.7)
    Metabolism Energy metabolism Electron transport NADH-quinone oxidoreductase, chain I (TIGR01971; HMM-score: 16.5)
    Metabolism Energy metabolism Electron transport ferredoxin-type protein NapF (TIGR00402; HMM-score: 14.8)
    Unknown function General archaeoflavoprotein, MJ0208 family (TIGR02700; HMM-score: 14.5)
    Metabolism Energy metabolism Electron transport cytochrome c nitrite reductase, Fe-S protein (TIGR03149; EC 1.7.2.2; HMM-score: 13.7)
    [FeFe] hydrogenase, group B1/B3 (TIGR04105; EC 1.12.-.-; HMM-score: 13.2)
    Metabolism Central intermediary metabolism Sulfur metabolism sulfite reductase, dissimilatory-type beta subunit (TIGR02066; EC 1.8.99.3; HMM-score: 12.9)
    Metabolism Central intermediary metabolism Nitrogen fixation ferredoxin III, nif-specific (TIGR02936; HMM-score: 12.8)
    indolepyruvate ferredoxin oxidoreductase, alpha subunit (TIGR03336; EC 1.2.7.8; HMM-score: 10.4)
    2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family (TIGR02179; HMM-score: 9.6)
    Genetic information processing Protein fate Protein modification and repair [benzylsuccinate synthase]-activating enzyme (TIGR04003; EC 1.97.-.-; HMM-score: 8.5)
    Metabolism Energy metabolism Electron transport NADH-plastoquinone oxidoreductase, I subunit (TIGR00403; EC 1.6.5.3; HMM-score: 8.4)
    Metabolism Energy metabolism Amino acids and amines choline TMA-lyase-activating enzyme (TIGR04395; EC 1.97.-.-; HMM-score: 7.6)
    Genetic information processing Protein fate Protein modification and repair glycine radical enzyme activase, YjjW family (TIGR04041; EC 1.97.1.-; HMM-score: 7.2)
    coenzyme F420 hydrogenase, subunit gamma (TIGR03294; EC 1.12.98.1; HMM-score: 6.8)
    Metabolism Energy metabolism TCA cycle succinate dehydrogenase and fumarate reductase iron-sulfur protein (TIGR00384; HMM-score: 5.7)
    Metabolism Energy metabolism Anaerobic succinate dehydrogenase and fumarate reductase iron-sulfur protein (TIGR00384; HMM-score: 5.7)
    Metabolism Energy metabolism Aerobic succinate dehydrogenase and fumarate reductase iron-sulfur protein (TIGR00384; HMM-score: 5.7)
    ferredoxin-type protein, NapH/MauN family (TIGR02163; HMM-score: 5.6)
    Metabolism Energy metabolism Methanogenesis putative methanogenesis marker 16 metalloprotein (TIGR03287; HMM-score: 3.5)
    Metabolism Central intermediary metabolism Sulfur metabolism sulfite reductase, subunit A (TIGR02910; EC 1.8.-.-; HMM-score: 3.3)
    pyruvate:ferredoxin (flavodoxin) oxidoreductase (TIGR02176; EC 1.2.7.1; HMM-score: 2.3)
  • TheSEED  :
    • Formate dehydrogenase related protein
    Respiration Respiration - no subcategory Formate hydrogenase  Formate dehydrogenase related protein
  • PFAM:
    no clan defined Molybdopterin; Molybdopterin oxidoreductase (PF00384; HMM-score: 265.9)
    and 19 more
    4Fe-4S (CL0344) Molybdop_Fe4S4; Molybdopterin oxidoreductase Fe4S4 domain (PF04879; HMM-score: 69.4)
    AcetylDC-like (CL0332) Molydop_binding; Molydopterin dinucleotide binding domain (PF01568; HMM-score: 67.8)
    4Fe-4S (CL0344) Fer4; 4Fe-4S binding domain (PF00037; HMM-score: 37.4)
    no clan defined NADH-G_4Fe-4S_3; NADH-ubiquinone oxidoreductase-G iron-sulfur binding region (PF10588; HMM-score: 36.4)
    Fer2 (CL0486) Fer2_4; 2Fe-2S iron-sulfur cluster binding domain (PF13510; HMM-score: 34.6)
    4Fe-4S (CL0344) Fer4_7; 4Fe-4S dicluster domain (PF12838; HMM-score: 32.7)
    Fer4_21; 4Fe-4S dicluster domain (PF14697; HMM-score: 31.2)
    Fer4_6; 4Fe-4S binding domain (PF12837; HMM-score: 30.7)
    Fer4_10; 4Fe-4S dicluster domain (PF13237; HMM-score: 23.6)
    Fer4_9; 4Fe-4S dicluster domain (PF13187; HMM-score: 22)
    Fer2 (CL0486) Fer2; 2Fe-2S iron-sulfur cluster binding domain (PF00111; HMM-score: 19.2)
    4Fe-4S (CL0344) Fer4_15; 4Fe-4S single cluster domain (PF13459; HMM-score: 19)
    Fer4_8; 4Fe-4S dicluster domain (PF13183; HMM-score: 17.7)
    Fer4_17; 4Fe-4S dicluster domain (PF13534; HMM-score: 16.8)
    Fer4_2; 4Fe-4S binding domain (PF12797; HMM-score: 15.3)
    Fer4_13; 4Fe-4S single cluster domain of Ferredoxin I (PF13370; HMM-score: 14.8)
    C2H2-zf (CL0361) zf-C2HE; C2HE / C2H2 / C2HC zinc-binding finger (PF16278; HMM-score: 14.8)
    4Fe-4S (CL0344) Fer4_16; 4Fe-4S double cluster binding domain (PF13484; HMM-score: 12.4)
    Fer4_22; 4Fe-4S dicluster domain (PF17179; HMM-score: 12.1)

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

  • domains:
  • modifications:
  • cofactors: Mo-bis(molybdopterin guanine dinucleotide), [2Fe-2S] cluster, [4Fe-4S] cluster
  • 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): 0.015111
    • TAT(Tat/SPI): 0.000481
    • LIPO(Sec/SPII): 0.000642
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MQEHLVVTLDGKDYLVEPGTNLLEFIKSQDTFVPSICYNESMGPIQTCDTCTVEIDGKIERSCSTVIDRPMTVNTVNNDVKDAQKEALDRILEKHMLYCTVCDYNNGDCEIHNTMDAWGLQHQTYEYKEKPYEKDYGPFYRYDPNQCILCGRCVEACQDIEVNETIRIDWDREHPRVIWDNDVPINESSCVSCGQCATVCPCNAMMEVNMEGNAGYMTDTEPGSLAAMIDLTKKAEPGYGPLFAISDSEAEMRKERIKKTKTVCTYCGVGCSFEVWTKDREILKVQPSHDSPANKIATCVKGKFSWGHINSDQRLTKPLVRKNGEFHEVEWDEALNVIADNFTAIKEKHGPDALSFISSSKATNEESYLMQKLARQVIGTNNVDNCSRYCQAPATKGLFRTVGHGGDSGSIEDLEKAAMSVLIGTNTAEAHPVIASRMKRAQKLFGQKIHVFDIRKHEMAERADRFYQPKPGTDLAWLSAVTKYIIDHDLHDKAFIDEWVDDFDEYYKSLETFTMAFAEEATGIPESELIKFAEECAKAESVVICWAMGITQQDIGSDSSTAISNLLLVTGNYRRPGTGAYPLRGHNNVQGCSDMGSMPDKITGYQSIEADDIRAKFEKEYGVKLNPKAGKDNHEMVEGIHDGEVHSLYLYGEDTGIVDSNINFVQAAFEKLDFMVVQDEFLTFTATYADVVLPASPSLEKDGTFTNTERRIQRLYQALEPLGDSKPDWKIFQAIANRLGFDWNYKHPSEIMDEVARLTPLYAGVSYDRLEGFNSLQWPVQPDGTDEPILYLEGFNFDNGKAKLFPLSFDNYFKQDEIYDIHVNNGRLLEHFHEGNMTYQTPMIKYKVPRAFVEISPELAEDRGIHEGAEVKLISETGEAVLQVHVTDRVKGKEIYIPLNNDAMENGDLGAINLLTNSDVDQYTDTPSYKRTSCRLEVITKRGKSPLNPNNFRVNKKRQPQYSVQVQKKWERSDYVFPGNQVDK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3]
  • quantitative data / protein copy number per cell: 497 [4]
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator: SigB* (activation) regulon
    SigB*(sigma factor)controlling a large regulon involved in stress/starvation response and adaptation;  [5] [6]   other strains

⊟Transcription pattern[edit | edit source]

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

⊟Protein stability[edit | edit source]

  • half-life: 13.41 h [7]

⊟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, 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)
  3. ↑ 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)
  4. ↑ 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)
  5. ↑ Markus Bischoff, Paul Dunman, Jan Kormanec, Daphne Macapagal, Ellen Murphy, William Mounts, Brigitte Berger-Bächi, Steven Projan
    Microarray-based analysis of the Staphylococcus aureus sigmaB regulon.
    J Bacteriol: 2004, 186(13);4085-99
    [PubMed:15205410] [WorldCat.org] [DOI] (P p)
  6. ↑ Jan Pané-Farré, Beate Jonas, Konrad Förstner, Susanne Engelmann, Michael Hecker
    The sigmaB regulon in Staphylococcus aureus and its regulation.
    Int J Med Microbiol: 2006, 296(4-5);237-58
    [PubMed:16644280] [WorldCat.org] [DOI] (P p)
  7. ↑ 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]

Retrieved from "http://aureowiki.med.uni-greifswald.de/index.php?title=SACOL2301&oldid=99199"