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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL2362 [new locus tag: SACOL_RS12405 ]
  • pan locus tag?: SAUPAN005877000
  • symbol: mqo1
  • pan gene symbol?: mqo
  • synonym:
  • product: malate:quinone oxidoreductase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL2362 [new locus tag: SACOL_RS12405 ]
  • symbol: mqo1
  • product: malate:quinone oxidoreductase
  • replicon: chromosome
  • strand: -
  • coordinates: 2420487..2421965
  • length: 1479
  • 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
    ATGACAACACAACATAGCAAAACAGATGTCATCTTAATTGGTGGCGGTATTATGAGTGCA
    ACATTAGGAACATTACTTAAAGAATTATCACCTGAGAAAAATATTAAAGTGTTTGAAAAA
    TTAGCACAACCTGGCGAAGAGAGTTCAAATGTATGGAATAATGCCGGTACAGGGCATTCA
    GCACTTTGCGAGTTGAACTATACAAAAGAAGGTAAGGATGGCACAGTTGATTGTAGTAAA
    GCAATTAAGATAAATGAGCAGTACCAAATTTCAAAACAGTTTTGGGCATATTTAGTTAAA
    ACAGGACAATTAGATAACCCAGATCGCTTTATTCAAGCGGTGCCACACATGAGTTTTGTC
    ATTGGCGAAGATAATGTAGCTTTTATAAAAAGTCGTGTTGCAACGTTAAAGAAAAGTATT
    TTATTCGAAAAAATGAAATTATCGCAAGATGAAGAAGAAATGAAATCTTGGGTACCGTTA
    ATGATTGAAGGTCGTAAGTCTGATGAACCAATTGCTTTAACTTATGATGAAACTGGTACA
    GATGTTAACTTTGGTGCGTTAACTGCAAAGTTATTTGATAATTTAGAGCAACGTGGTGTG
    GGAATTCAATATAAGCAGAATGTATTAGACATCAAGAAACAGAAATCTGGGGTATGGCTA
    GTTAAAGTTAAAGATTTAGAAACTAATGAAACGACAACATATGAATCTGATTTTGTATTT
    ATTGGTGCTGGCGGTGCGAGTTTACCATTACTCCAAAAGACTGGGATTAAACAATCAAAA
    CATATTGGTGGTTTCCCGGTAAGTGGATTATTCCTGCGCTGTACAAATCAAGAAGTGATT
    GATCGTCATCATGCTAAAGTGTACGGAAAAGCAGCAGTGGGTGCGCCACCAATGTCAGTG
    CCGCACTTAGATACACGTTTTGTAGACGGCAAGCGTTCATTGTTATTTGGTCCATTTGCA
    GGTTTCTCACCTAAATTTTTAAAAACAGGTTCACATATGGATTTAATTAAATCGGTTAAA
    CCAAATAATATCGTGACGATGTTATCTGCAGGTATCAAAGAAATGAGTCTTACGAAGTAT
    TTAGTGTCACAATTGATGTTATCTAATGATGAGCGTATGGATGATTTAAGAGTCTTTTTC
    CCAAATGCTAAAAATGAAGATTGGGAAGTGATTACAGCAGGGCAACGTGTCCAAGTAATC
    AAGGATACTGAGGATTCTAAAGGTAACTTACAATTTGGTACTGAAGTTATTACGTCAGAT
    GATGGCACATTAGCTGCATTACTTGGTGCATCACCTGGTGCGTCAACAGCTGTAGATATT
    ATGTTTGATGTTTTACAGAGATGCTATCGTGATGAATTCAAAGGATGGGAACCAAAGATT
    AAAGAAATGGTGCCGTCATTTGGTTATCGCTTAACAGATCATGAGGATTTATATCATAAA
    ATTAATGAAGAAGTAACTAAGTATTTACAAGTTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1479

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL2362 [new locus tag: SACOL_RS12405 ]
  • symbol: Mqo1
  • description: malate:quinone oxidoreductase
  • length: 492
  • theoretical pI: 6.68621
  • theoretical MW: 54813.4
  • GRAVY: -0.321748

⊟Function[edit | edit source]

  • reaction:
    EC 1.1.5.4?  ExPASy
    Malate dehydrogenase (quinone) (S)-malate + a quinone = oxaloacetate + reduced quinone
  • TIGRFAM:
    Metabolism Energy metabolism TCA cycle malate dehydrogenase (acceptor) (TIGR01320; EC 1.1.5.4; HMM-score: 709.8)
    and 4 more
    Genetic information processing Protein synthesis tRNA and rRNA base modification tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain (TIGR03197; HMM-score: 17.7)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other C-3',4' desaturase CrtD (TIGR02733; EC 1.3.99.-; HMM-score: 16.4)
    Unknown function Enzymes of unknown specificity flavoprotein, HI0933 family (TIGR00275; HMM-score: 15)
    Metabolism Energy metabolism Electron transport thioredoxin-disulfide reductase (TIGR01292; EC 1.8.1.9; HMM-score: 12.4)
  • TheSEED  :
    • Malate:quinone oxidoreductase (EC 1.1.5.4)
    Carbohydrates Central carbohydrate metabolism TCA Cycle  Malate:quinone oxidoreductase (EC 1.1.5.4)
  • PFAM:
    NADP_Rossmann (CL0063) Mqo; Malate:quinone oxidoreductase (Mqo) (PF06039; HMM-score: 769.3)
    and 5 more
    DAO; FAD dependent oxidoreductase (PF01266; HMM-score: 36.9)
    Pyr_redox_2; Pyridine nucleotide-disulphide oxidoreductase (PF07992; HMM-score: 16.8)
    HI0933_like; HI0933-like protein (PF03486; HMM-score: 16.2)
    FAD_binding_3; FAD binding domain (PF01494; HMM-score: 12.6)
    FAD_binding_2; FAD binding domain (PF00890; HMM-score: 10.6)

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

  • domains:
  • modifications:
  • cofactors: FAD
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cellwall
    • Cytoplasmic Score: 0.01
    • Cytoplasmic Membrane Score: 0.53
    • Cellwall Score: 8.75
    • Extracellular Score: 0.7
    • 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): 0.129481
    • TAT(Tat/SPI): 0.018532
    • LIPO(Sec/SPII): 0.030927
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTTQHSKTDVILIGGGIMSATLGTLLKELSPEKNIKVFEKLAQPGEESSNVWNNAGTGHSALCELNYTKEGKDGTVDCSKAIKINEQYQISKQFWAYLVKTGQLDNPDRFIQAVPHMSFVIGEDNVAFIKSRVATLKKSILFEKMKLSQDEEEMKSWVPLMIEGRKSDEPIALTYDETGTDVNFGALTAKLFDNLEQRGVGIQYKQNVLDIKKQKSGVWLVKVKDLETNETTTYESDFVFIGAGGASLPLLQKTGIKQSKHIGGFPVSGLFLRCTNQEVIDRHHAKVYGKAAVGAPPMSVPHLDTRFVDGKRSLLFGPFAGFSPKFLKTGSHMDLIKSVKPNNIVTMLSAGIKEMSLTKYLVSQLMLSNDERMDDLRVFFPNAKNEDWEVITAGQRVQVIKDTEDSKGNLQFGTEVITSDDGTLAALLGASPGASTAVDIMFDVLQRCYRDEFKGWEPKIKEMVPSFGYRLTDHEDLYHKINEEVTKYLQVK

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 40 [5]
  • interaction partners:
    SACOL1385(acnA)aconitate hydratase  [6] (data from MRSA252)
    SACOL0452(ahpC)alkyl hydroperoxide reductase subunit C  [6] (data from MRSA252)
    SACOL0557(cysK)cysteine synthase  [6] (data from MRSA252)
    SACOL0842(eno)phosphopyruvate hydratase  [6] (data from MRSA252)
    SACOL1329(femC)glutamine synthetase  [6] (data from MRSA252)
    SACOL1782(fhs)formate--tetrahydrofolate ligase  [6] (data from MRSA252)
    SACOL1199(ftsZ)cell division protein FtsZ  [6] (data from MRSA252)
    SACOL0593(fusA)elongation factor G  [6] (data from MRSA252)
    SACOL0838(gapA1)glyceraldehyde 3-phosphate dehydrogenase  [6] (data from MRSA252)
    SACOL2145(glmS)glucosamine--fructose-6-phosphate aminotransferase  [6] (data from MRSA252)
    SACOL1513(hup)DNA-binding protein HU  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [6] (data from MRSA252)
    SACOL1102(pdhA)pyruvate dehydrogenase complex E1 component subunit alpha  [6] (data from MRSA252)
    SACOL1103(pdhB)pyruvate dehydrogenase complex E1 component subunit beta  [6] (data from MRSA252)
    SACOL1104(pdhC)branched-chain alpha-keto acid dehydrogenase E2  [6] (data from MRSA252)
    SACOL1105(pdhD)dihydrolipoamide dehydrogenase  [6] (data from MRSA252)
    SACOL2128(pdp)pyrimidine-nucleoside phosphorylase  [6] (data from MRSA252)
    SACOL0204(pflB)formate acetyltransferase  [6] (data from MRSA252)
    SACOL0839(pgk)phosphoglycerate kinase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL2224(rplF)50S ribosomal protein L6  [6] (data from MRSA252)
    SACOL0015(rplI)50S ribosomal protein L9  [6] (data from MRSA252)
    SACOL0585(rplJ)50S ribosomal protein L10  [6] (data from MRSA252)
    SACOL0583(rplK)50S ribosomal protein L11  [6] (data from MRSA252)
    SACOL2212(rplQ)50S ribosomal protein L17  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL2233(rpsC)30S ribosomal protein S3  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2225(rpsH)30S ribosomal protein S8  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL2230(rpsQ)30S ribosomal protein S17  [6] (data from MRSA252)
    SACOL1449(sucA)2-oxoglutarate dehydrogenase E1 component  [6] (data from MRSA252)
    SACOL0840(tpiA)triosephosphate isomerase  [6] (data from MRSA252)
    SACOL1155(trxA)thioredoxin  [6] (data from MRSA252)
    SACOL1276(tsf)elongation factor Ts  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0731LysR family transcriptional regulator  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)
    SACOL2173alkaline shock protein 23  [6] (data from MRSA252)
    SACOL25691-pyrroline-5-carboxylate dehydrogenase  [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 6.24 6.25 6.26 6.27 6.28 6.29 6.30 6.31 6.32 6.33 6.34 6.35 6.36 6.37 6.38 6.39 6.40 6.41 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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