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NCBI: 03-AUG-2016
⊟Summary[edit | edit source]
- organism: Staphylococcus aureus NCTC8325
- locus tag: SAOUHSC_00832
- pan locus tag?: SAUPAN002817000
- symbol: SAOUHSC_00832
- pan gene symbol?: aroD
- synonym:
- product: 3-dehydroquinase
⊟Genome View[edit | edit source]
⊟Gene[edit | edit source]
⊟General[edit | edit source]
- type: CDS
- locus tag: SAOUHSC_00832
- symbol: SAOUHSC_00832
- product: 3-dehydroquinase
- replicon: chromosome
- strand: +
- coordinates: 807550..808266
- length: 717
- essential: no DEG other strains
⊟Accession numbers[edit | edit source]
- Gene ID: 3918944 NCBI
- RefSeq: YP_499386 NCBI
- BioCyc: G1I0R-776 BioCyc
- MicrobesOnline: 1289297 MicrobesOnline
⊟Phenotype[edit | edit source]
Share your knowledge and add information here. [edit]
⊟DNA sequence[edit | edit source]
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661ATGACACATGTGGAAGTAGTAGCGACTATCGCGCCACAATTATCTATCGAAGAAACTTTA
ATTCAAAAAATTAATCATCGTATTGATGCAATAGACGTATTAGAATTACGAATTGATCAA
ATTGAAAATGTCACAGTTGATCAAGTGGCAGAAATGATTACAAAGCTGAAGGTTATGCAA
GATTCATTCAAATTATTAGTTACGTATCGTACAAAGTTACAAGGTGGCTATGGGCAATTT
ACAAATGACTCGTATCTTAATTTAATATCAGACTTAGCAAATATCAATGGCATAGATATG
ATTGATATAGAATGGCAAGCAGATATTGACATTGAAAAACATCAACGAATCATTACACAT
TTGCAACAGTATAATAAAGAGGTGGTTATATCACATCATAATTTCGAAAGTACGCCTCCA
TTAGATGAATTGCAATTTATATTTTTTAAAATGCAAAAATTCAACCCAGAATACGTTAAA
TTAGCAGTAATGCCACATAATAAAAATGATGTGTTAAATTTATTGCAGGCAATGTCTACA
TTTTCAGATACTATGGACTGCAAAGTTGTTGGTATTTCAATGTCTAAACTTGGACTAATA
AGTAGAACGGCTCAAGGCGTTTTTGGTGGTGCGTTGACTTATGGTTGTATCGGAGTACCA
CAAGCTCCAGGACAGATTGATGTTACTGATTTAAAAGCACAAGTGACTTTATACTAA60
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⊟Protein[edit | edit source]
⊟General[edit | edit source]
- locus tag: SAOUHSC_00832
- symbol: SAOUHSC_00832
- description: 3-dehydroquinase
- length: 238
- theoretical pI: 4.90902
- theoretical MW: 26868.8
- GRAVY: -0.0155462
⊟Function[edit | edit source]
- reaction: EC 4.2.1.10? ExPASy3-dehydroquinate dehydratase 3-dehydroquinate = 3-dehydroshikimate + H2O
- TIGRFAM: Amino acid biosynthesis Aromatic amino acid family 3-dehydroquinate dehydratase, type I (TIGR01093; EC 4.2.1.10; HMM-score: 173.2)
- TheSEED :
- 3-dehydroquinate dehydratase I (EC 4.2.1.10)
Amino Acids and Derivatives Aromatic amino acids and derivatives Chorismate Synthesis 3-dehydroquinate dehydratase I (EC 4.2.1.10)and 2 more - PFAM: TIM_barrel (CL0036) DHquinase_I; Type I 3-dehydroquinase (PF01487; HMM-score: 165)and 1 moreno clan defined Borrelia_lipo_2; Borrelia burgdorferi BBR25 lipoprotein (PF06238; HMM-score: 10.4)
⊟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): 0.001965
- TAT(Tat/SPI): 0.000074
- LIPO(Sec/SPII): 0.00016
- predicted transmembrane helices (TMHMM): 0
⊟Accession numbers[edit | edit source]
⊟Protein sequence[edit | edit source]
- MTHVEVVATIAPQLSIEETLIQKINHRIDAIDVLELRIDQIENVTVDQVAEMITKLKVMQDSFKLLVTYRTKLQGGYGQFTNDSYLNLISDLANINGIDMIDIEWQADIDIEKHQRIITHLQQYNKEVVISHHNFESTPPLDELQFIFFKMQKFNPEYVKLAVMPHNKNDVLNLLQAMSTFSDTMDCKVVGISMSKLGLISRTAQGVFGGALTYGCIGVPQAPGQIDVTDLKAQVTLY
⊟Experimental data[edit | edit source]
- experimentally validated: PeptideAtlas [1] [2]
- protein localization: data available for COL
- quantitative data / protein copy number per cell:
- interaction partners:
SAOUHSC_01471 (asnC) asparaginyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_01683 (dnaK) molecular chaperone DnaK [3] (data from MRSA252) SAOUHSC_00799 (eno) phosphopyruvate hydratase [3] (data from MRSA252) SAOUHSC_00574 (eutD) phosphotransacetylase [3] (data from MRSA252) SAOUHSC_02117 (gatA) aspartyl/glutamyl-tRNA amidotransferase subunit A [3] (data from MRSA252) SAOUHSC_02255 (groES) co-chaperonin GroES [3] (data from MRSA252) SAOUHSC_00375 (guaA) GMP synthase [3] (data from MRSA252) SAOUHSC_01246 (infB) translation initiation factor IF-2 [3] (data from MRSA252) SAOUHSC_00493 (lysS) lysyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_01243 (nusA) transcription elongation factor NusA [3] (data from MRSA252) SAOUHSC_00900 (pgi) glucose-6-phosphate isomerase [3] (data from MRSA252) SAOUHSC_00796 (pgk) phosphoglycerate kinase [3] (data from MRSA252) SAOUHSC_00519 (rplA) 50S ribosomal protein L1 [3] (data from MRSA252) SAOUHSC_02509 (rplB) 50S ribosomal protein L2 [3] (data from MRSA252) SAOUHSC_02512 (rplC) 50S ribosomal protein L3 [3] (data from MRSA252) SAOUHSC_02511 (rplD) 50S ribosomal protein L4 [3] (data from MRSA252) SAOUHSC_02500 (rplE) 50S ribosomal protein L5 [3] (data from MRSA252) SAOUHSC_02496 (rplF) 50S ribosomal protein L6 [3] (data from MRSA252) SAOUHSC_00017 (rplI) 50S ribosomal protein L9 [3] (data from MRSA252) SAOUHSC_00520 (rplJ) 50S ribosomal protein L10 [3] (data from MRSA252) SAOUHSC_00518 (rplK) 50S ribosomal protein L11 [3] (data from MRSA252) SAOUHSC_00521 (rplL) 50S ribosomal protein L7/L12 [3] (data from MRSA252) SAOUHSC_02478 (rplM) 50S ribosomal protein L13 [3] (data from MRSA252) SAOUHSC_02492 (rplO) 50S ribosomal protein L15 [3] (data from MRSA252) SAOUHSC_02484 (rplQ) 50S ribosomal protein L17 [3] (data from MRSA252) SAOUHSC_02495 (rplR) 50S ribosomal protein L18 [3] (data from MRSA252) SAOUHSC_01211 (rplS) 50S ribosomal protein L19 [3] (data from MRSA252) SAOUHSC_01784 (rplT) 50S ribosomal protein L20 [3] (data from MRSA252) SAOUHSC_01757 (rplU) 50S ribosomal protein L21 [3] (data from MRSA252) SAOUHSC_02507 (rplV) 50S ribosomal protein L22 [3] (data from MRSA252) SAOUHSC_02510 (rplW) 50S ribosomal protein L23 [3] (data from MRSA252) SAOUHSC_01493 (rpsA) 30S ribosomal protein S1 [3] (data from MRSA252) SAOUHSC_01232 (rpsB) 30S ribosomal protein S2 [3] (data from MRSA252) SAOUHSC_02506 (rpsC) 30S ribosomal protein S3 [3] (data from MRSA252) SAOUHSC_01829 (rpsD) 30S ribosomal protein S4 [3] (data from MRSA252) SAOUHSC_02494 (rpsE) 30S ribosomal protein S5 [3] (data from MRSA252) SAOUHSC_02477 (rpsI) 30S ribosomal protein S9 [3] (data from MRSA252) SAOUHSC_01208 (rpsP) 30S ribosomal protein S16 [3] (data from MRSA252) SAOUHSC_02508 (rpsS) 30S ribosomal protein S19 [3] (data from MRSA252) SAOUHSC_01418 (sucA) 2-oxoglutarate dehydrogenase E1 component [3] (data from MRSA252) SAOUHSC_01788 (thrS) threonyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_01779 (tig) trigger factor [3] (data from MRSA252) SAOUHSC_00797 (tpiA) triosephosphate isomerase [3] (data from MRSA252) SAOUHSC_01822 (tpx) 2-Cys peroxiredoxin [3] (data from MRSA252) SAOUHSC_01234 (tsf) elongation factor Ts [3] (data from MRSA252) SAOUHSC_02353 (upp) uracil phosphoribosyltransferase [3] (data from MRSA252) SAOUHSC_00069 protein A [3] (data from MRSA252) SAOUHSC_00187 formate acetyltransferase [3] (data from MRSA252) SAOUHSC_00206 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_00365 alkyl hydroperoxide reductase subunit C [3] (data from MRSA252) SAOUHSC_00444 hypothetical protein [3] (data from MRSA252) SAOUHSC_00474 50S ribosomal protein L25/general stress protein Ctc [3] (data from MRSA252) SAOUHSC_00488 hypothetical protein [3] (data from MRSA252) SAOUHSC_00499 pyridoxal biosynthesis lyase PdxS [3] (data from MRSA252) SAOUHSC_00525 DNA-directed RNA polymerase subunit beta' [3] (data from MRSA252) SAOUHSC_00529 elongation factor G [3] (data from MRSA252) SAOUHSC_00530 elongation factor Tu [3] (data from MRSA252) SAOUHSC_00562 phosphomethylpyrimidine kinase [3] (data from MRSA252) SAOUHSC_00608 alcohol dehydrogenase [3] (data from MRSA252) SAOUHSC_00669 hypothetical protein [3] (data from MRSA252) SAOUHSC_00679 hypothetical protein [3] (data from MRSA252) SAOUHSC_00694 hypothetical protein [3] (data from MRSA252) SAOUHSC_00742 ribonucleotide-diphosphate reductase subunit alpha [3] (data from MRSA252) SAOUHSC_00767 hypothetical protein [3] (data from MRSA252) SAOUHSC_00795 glyceraldehyde-3-phosphate dehydrogenase [3] (data from MRSA252) SAOUHSC_00835 hypothetical protein [3] (data from MRSA252) SAOUHSC_00878 hypothetical protein [3] (data from MRSA252) SAOUHSC_00895 glutamate dehydrogenase [3] (data from MRSA252) SAOUHSC_00906 hypothetical protein [3] (data from MRSA252) SAOUHSC_00921 3-oxoacyl- synthase [3] (data from MRSA252) SAOUHSC_00937 oligoendopeptidase F [3] (data from MRSA252) SAOUHSC_01040 pyruvate dehydrogenase complex, E1 component subunit alpha [3] (data from MRSA252) SAOUHSC_01041 pyruvate dehydrogenase complex, E1 component subunit beta [3] (data from MRSA252) SAOUHSC_01042 branched-chain alpha-keto acid dehydrogenase subunit E2 [3] (data from MRSA252) SAOUHSC_01043 dihydrolipoamide dehydrogenase [3] (data from MRSA252) SAOUHSC_01058 GTP-binding protein TypA [3] (data from MRSA252) SAOUHSC_01100 thioredoxin [3] (data from MRSA252) SAOUHSC_01150 cell division protein FtsZ [3] (data from MRSA252) SAOUHSC_01347 aconitate hydratase [3] (data from MRSA252) SAOUHSC_01416 dihydrolipoamide succinyltransferase [3] (data from MRSA252) SAOUHSC_01451 threonine dehydratase [3] (data from MRSA252) SAOUHSC_01490 DNA-binding protein HU [3] (data from MRSA252) SAOUHSC_01605 6-phosphogluconate dehydrogenase [3] (data from MRSA252) SAOUHSC_01666 glycyl-tRNA synthetase [3] (data from MRSA252) SAOUHSC_01794 glyceraldehyde 3-phosphate dehydrogenase 2 [3] (data from MRSA252) SAOUHSC_01801 isocitrate dehydrogenase [3] (data from MRSA252) SAOUHSC_01806 pyruvate kinase [3] (data from MRSA252) SAOUHSC_01820 acetate kinase [3] (data from MRSA252) SAOUHSC_01867 D-alanine aminotransferase [3] (data from MRSA252) SAOUHSC_01868 dipeptidase PepV [3] (data from MRSA252) SAOUHSC_01901 putative translaldolase [3] (data from MRSA252) SAOUHSC_02108 ferritin [3] (data from MRSA252) SAOUHSC_02140 manganese-dependent inorganic pyrophosphatase [3] (data from MRSA252) SAOUHSC_02363 aldehyde dehydrogenase [3] (data from MRSA252) SAOUHSC_02365 UDP-N-acetylglucosamine 1-carboxyvinyltransferase [3] (data from MRSA252) SAOUHSC_02399 glucosamine--fructose-6-phosphate aminotransferase [3] (data from MRSA252) SAOUHSC_02441 alkaline shock protein 23 [3] (data from MRSA252) SAOUHSC_02485 DNA-directed RNA polymerase subunit alpha [3] (data from MRSA252) SAOUHSC_02486 30S ribosomal protein S11 [3] (data from MRSA252) SAOUHSC_02577 D-isomer specific 2-hydroxyacid dehydrogenase NAD binding domain-containing protein [3] (data from MRSA252) SAOUHSC_02869 1-pyrroline-5-carboxylate dehydrogenase [3] (data from MRSA252) SAOUHSC_02922 L-lactate dehydrogenase [3] (data from MRSA252) SAOUHSC_02926 fructose-1,6-bisphosphate aldolase [3] (data from MRSA252) SAOUHSC_02927 malate:quinone oxidoreductase [3] (data from MRSA252) SAOUHSC_02965 carbamate kinase [3] (data from MRSA252) SAOUHSC_02968 ornithine carbamoyltransferase [3] (data from MRSA252) SAOUHSC_02969 arginine deiminase [3] (data from MRSA252)
⊟Expression & Regulation[edit | edit source]
⊟Operon[edit | edit source]
⊟Regulation[edit | edit source]
- regulator:
⊟Transcription pattern[edit | edit source]
- S.aureus Expression Data Browser: [4] Multi-gene expression profiles
⊟Protein synthesis (provided by Aureolib)[edit | edit source]
- Aureolib: no data available
⊟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]
- ↑ Maren Depke, Stephan Michalik, Alexander Rabe, Kristin Surmann, Lars Brinkmann, Nico Jehmlich, Jörg Bernhardt, Michael Hecker, Bernd Wollscheid, Zhi Sun, Robert L Moritz, Uwe Völker, Frank Schmidt
A peptide resource for the analysis of Staphylococcus aureus in host-pathogen interaction studies.
Proteomics: 2015, 15(21);3648-61
[PubMed:26224020] [WorldCat.org] [DOI] (I p) - ↑ Stephan Michalik, Maren Depke, Annette Murr, Manuela Gesell Salazar, Ulrike Kusebauch, Zhi Sun, Tanja C Meyer, Kristin Surmann, Henrike Pförtner, Petra Hildebrandt, Stefan Weiss, Laura Marcela Palma Medina, Melanie Gutjahr, Elke Hammer, Dörte Becher, Thomas Pribyl, Sven Hammerschmidt, Eric W Deutsch, Samuel L Bader, Michael Hecker, Robert L Moritz, Ulrike Mäder, Uwe Völker, Frank Schmidt
A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions.
Sci Rep: 2017, 7(1);9718
[PubMed:28887440] [WorldCat.org] [DOI] (I e) - ↑ 3.000 3.001 3.002 3.003 3.004 3.005 3.006 3.007 3.008 3.009 3.010 3.011 3.012 3.013 3.014 3.015 3.016 3.017 3.018 3.019 3.020 3.021 3.022 3.023 3.024 3.025 3.026 3.027 3.028 3.029 3.030 3.031 3.032 3.033 3.034 3.035 3.036 3.037 3.038 3.039 3.040 3.041 3.042 3.043 3.044 3.045 3.046 3.047 3.048 3.049 3.050 3.051 3.052 3.053 3.054 3.055 3.056 3.057 3.058 3.059 3.060 3.061 3.062 3.063 3.064 3.065 3.066 3.067 3.068 3.069 3.070 3.071 3.072 3.073 3.074 3.075 3.076 3.077 3.078 3.079 3.080 3.081 3.082 3.083 3.084 3.085 3.086 3.087 3.088 3.089 3.090 3.091 3.092 3.093 3.094 3.095 3.096 3.097 3.098 3.099 3.100 3.101 3.102 3.103 3.104 3.105 3.106 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) - ↑ 4.0 4.1 Ulrike Mäder, Pierre Nicolas, Maren Depke, Jan Pané-Farré, Michel Debarbouille, Magdalena M van der Kooi-Pol, Cyprien Guérin, Sandra Dérozier, Aurelia Hiron, Hanne Jarmer, Aurélie Leduc, Stephan Michalik, Ewoud Reilman, Marc Schaffer, Frank Schmidt, Philippe Bessières, Philippe Noirot, Michael Hecker, Tarek Msadek, Uwe Völker, Jan Maarten van Dijl
Staphylococcus aureus Transcriptome Architecture: From Laboratory to Infection-Mimicking Conditions.
PLoS Genet: 2016, 12(4);e1005962
[PubMed:27035918] [WorldCat.org] [DOI] (I e)