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NCBI: 26-AUG-2013

Summary[edit source | edit]

  • organism: Staphylococcus aureus N315
  • locus tag: SA0944 [new locus tag: SA_RS05355 ]
  • pan locus tag?: SAUPAN003318000
  • symbol: pdhB
  • pan gene symbol?: pdhB
  • synonym:
  • product: pyruvate dehydrogenase E1 component subunit beta

Genome View[edit source | edit]

Gene[edit source | edit]

General[edit source | edit]

  • type: CDS
  • locus tag: SA0944 [new locus tag: SA_RS05355 ]
  • symbol: pdhB
  • product: pyruvate dehydrogenase E1 component subunit beta
  • replicon: chromosome
  • strand: +
  • coordinates: 1071958..1072935
  • length: 978
  • essential: yes [1] DEG other strains

Accession numbers[edit source | edit]

Phenotype[edit source | edit]

  • Share your knowledge and add information here. [edit]

DNA sequence[edit source | edit]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    ATGGCACAAATGACAATGGTTCAAGCGATTAATGATGCGCTTAAAACTGAACTTAAAAAT
    GACCAAGATGTTTTAATTTTTGGTGAAGACGTTGGTGTTAACGGCGGTGTTTTCCGTGTT
    ACTGAAGGACTACAAAAAGAATTTGGTGAAGATAGAGTATTCGATACACCTTTAGCTGAA
    TCAGGTATTGGTGGTTTAGCGATGGGTCTTGCAGTTGAAGGATTCCGTCCGGTTATGGAA
    GTACAATTCTTAGGTTTCGTATTCGAAGTATTTGATGCGATTGCTGGACAAATTGCACGT
    ACTCGTTTCCGTTCAGGCGGTACTAAAACTGCACCTGTAACAATTCGTAGCCCATTTGGT
    GGTGGCGTACACACACCAGAATTACACGCAGATAACTTAGAAGGTATTTTAGCTCAATCT
    CCAGGTCTAAAGGTTGTTATTCCTTCAGGCCCATACGATGCGAAAGGTTTATTAATTTCT
    TCTATTAGAAGTAATGACCCAGTCGTATACTTAGAGCATATGAAATTGTATCGTTCATTC
    CGTGAAGAAGTACCTGAAGAAGAATATACAATTGACATTGGTAAGGCTAATGTGAAAAAA
    GAAGGTAATGACATTTCAATCATCACATACGGTGCAATGGTTCAAGAATCAATGAAAGCT
    GCAGAAGAACTTGAAAAAGATGGTTATTCTGTTGAAGTAATTGACTTACGTACTGTTCAA
    CCAATCGATGTTGACACAATTGTAGCTTCAGTTGAAAAAACTGGTCGTGCAGTTGTAGTT
    CAAGAAGCACAACGTCAAGCTGGTGTTGGTGCAGCAGTTGTAGCTGAATTAAGTGAACGT
    GCAATCCTTTCATTAGAAGCACCTATTGGAAGAGTTGCAGCAGCAGATACAATTTATCCA
    TTCACTCAAGCTGAAAATGTTTGGTTACCAAACAAAAATGACATCATCGAAAAAGCAAAA
    GAAACTTTAGAATTTTAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    978

Protein[edit source | edit]

General[edit source | edit]

  • locus tag: SA0944 [new locus tag: SA_RS05355 ]
  • symbol: PdhB
  • description: pyruvate dehydrogenase E1 component subunit beta
  • length: 325
  • theoretical pI: 4.36436
  • theoretical MW: 35245.8
  • GRAVY: -0.0467692

Function[edit source | edit]

  • reaction:
    EC 1.2.4.1?  ExPASy
    Pyruvate dehydrogenase (acetyl-transferring)Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2
  • TIGRFAM:
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersOther1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersThiamine1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83)
    MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersPyridoxine1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 83)
    2-oxoacid:acceptor oxidoreductase, alpha subunit (TIGR03710; HMM-score: 25.6)
    pyruvate:ferredoxin (flavodoxin) oxidoreductase (TIGR02176; EC 1.2.7.1; HMM-score: 10.5)
  • TheSEED:  
    CarbohydratesCentral carbohydrate metabolismDehydrogenase complexes Pyruvate dehydrogenase E1 component beta subunit (EC 1.2.4.1) 
    Central carbohydrate metabolismPyruvate metabolism II: acetyl-CoA, acetogenesis from pyruvate Pyruvate dehydrogenase E1 component beta subunit (EC 1.2.4.1) 
  • PFAM:
    TKC_like (CL0591) Transketolase_C; Transketolase, C-terminal domain (PF02780; HMM-score: 135.3)
    THDP-binding (CL0254) Transket_pyr; Transketolase, pyrimidine binding domain (PF02779; HMM-score: 130.1)
    TKC_like (CL0591) PFOR_II; Pyruvate:ferredoxin oxidoreductase core domain II (PF17147; HMM-score: 18.3)

Structure, modifications & interactions[edit source | edit]

  • domains:
  • modifications:
  • cofactors: thiamine diphosphate
  • effectors:
  • protein partners:
    SA0033(aadD)kanamycin nucleotidyltransferase  [2] (data from MRSA252)
    SA2428(arcA)arginine deiminase  [2] (data from MRSA252)
    SA1517(citC)isocitrate dehydrogenase  [2] (data from MRSA252)
    SA1498(clpX)ATP-dependent protease ATP-binding subunit ClpX  [2] (data from MRSA252)
    SA1409(dnaK)molecular chaperone DnaK  [2] (data from MRSA252)
    SA1029(ftsZ)cell division protein FtsZ  [2] (data from MRSA252)
    SA0505(fus)elongation factor G  [2] (data from MRSA252)
    SA1510(gapB)glyceraldehyde 3-phosphate dehydrogenase 2  [2] (data from MRSA252)
    SA1716(gatA)aspartyl/glutamyl-tRNA amidotransferase subunit A  [2] (data from MRSA252)
    SA1715(gatB)aspartyl/glutamyl-tRNA amidotransferase subunit B  [2] (data from MRSA252)
    SA1305(hu)DNA-binding protein II  [2] (data from MRSA252)
    SA1902(murA)UDP-N-acetylglucosamine 1-carboxyvinyltransferase  [2] (data from MRSA252)
    SA1244(odhB)dihydrolipoamide succinyltransferase  [2] (data from MRSA252)
    SA0943-1(pdhA)pyruvate dehydrogenase E1 component subunit alpha  [2] (data from MRSA252)
    SA0945(pdhC)branched-chain alpha-keto acid dehydrogenase E2 subunit  [2] (data from MRSA252)
    SA0946(pdhD)dihydrolipoamide dehydrogenase  [2] (data from MRSA252)
    SA0218(pflB)formate acetyltransferase  [2] (data from MRSA252)
    SA1520(pykA)pyruvate kinase  [2] (data from MRSA252)
    SA2341(rocA)1-pyrroline-5-carboxylate dehydrogenase  [2] (data from MRSA252)
    SA0496(rplA)50S ribosomal protein L1  [2] (data from MRSA252)
    SA2044(rplB)50S ribosomal protein L2  [2] (data from MRSA252)
    SA2047(rplC)50S ribosomal protein L3  [2] (data from MRSA252)
    SA2046(rplD)50S ribosomal protein L4  [2] (data from MRSA252)
    SA2035(rplE)50S ribosomal protein L5  [2] (data from MRSA252)
    SA2029(rplO)50S ribosomal protein L15  [2] (data from MRSA252)
    SA1084(rplS)50S ribosomal protein L19  [2] (data from MRSA252)
    SA1502(rplT)50S ribosomal protein L20  [2] (data from MRSA252)
    SA1473(rplU)50S ribosomal protein L21  [2] (data from MRSA252)
    SA2042(rplV)50S ribosomal protein L22  [2] (data from MRSA252)
    SA2045(rplW)50S ribosomal protein L23  [2] (data from MRSA252)
    SA1099(rpsB)30S ribosomal protein S2  [2] (data from MRSA252)
    SA2041(rpsC)30S ribosomal protein S3  [2] (data from MRSA252)
    SAS052(rpsD)30S ribosomal protein S4  [2] (data from MRSA252)
    SA2031(rpsE)30S ribosomal protein S5  [2] (data from MRSA252)
    SA2038(rpsQ)30S ribosomal protein S17  [2] (data from MRSA252)
    SA1245(sucA)2-oxoglutarate dehydrogenase E1  [2] (data from MRSA252)
    SA0506(tuf)elongation factor Tu  [2] (data from MRSA252)
    SA0351GTP-dependent nucleic acid-binding protein EngD  [2] (data from MRSA252)
    SA0802hypothetical protein  [2] (data from MRSA252)
    SA0829hypothetical protein  [2] (data from MRSA252)
    SA1271threonine dehydratase  [2] (data from MRSA252)
    SA1532hypothetical protein  [2] (data from MRSA252)
    SA1924hypothetical protein  [2] (data from MRSA252)
    SA2327pyruvate oxidase  [2] (data from MRSA252)

Localization[edit source | edit]

  • 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
    • Ymax: 0.109
    • Ymax_pos: 16
    • Cmax: 0.127
    • Cmax_pos: 10
    • Smax: 0.167
    • Smax_pos: 9
    • Smean: 0.11
    • D: 0.109
  • predicted transmembrane helices (TMHMM): 0

Accession numbers[edit source | edit]

Protein sequence[edit source | edit]

  • MAQMTMVQAINDALKTELKNDQDVLIFGEDVGVNGGVFRVTEGLQKEFGEDRVFDTPLAESGIGGLAMGLAVEGFRPVMEVQFLGFVFEVFDAIAGQIARTRFRSGGTKTAPVTIRSPFGGGVHTPELHADNLEGILAQSPGLKVVIPSGPYDAKGLLISSIRSNDPVVYLEHMKLYRSFREEVPEEEYTIDIGKANVKKEGNDISIITYGAMVQESMKAAEELEKDGYSVEVIDLRTVQPIDVDTIVASVEKTGRAVVVQEAQRQAGVGAAVVAELSERAILSLEAPIGRVAAADTIYPFTQAENVWLPNKNDIIEKAKETLEF

Experimental data[edit source | edit]

  • experimentally validated: no data available

Expression & Regulation[edit source | edit]

Operon[edit source | edit]

Regulation[edit source | edit]

  • sigma factor:
  • regulator:

Transcription pattern[edit source | edit]

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

Protein stability[edit source | edit]

  • half-life: no data available

Biological Material[edit source | edit]

Mutants[edit source | edit]

Expression vector[edit source | edit]

lacZ fusion[edit source | edit]

GFP fusion[edit source | edit]

two-hybrid system[edit source | edit]

FLAG-tag construct[edit source | edit]

Antibody[edit source | edit]

Other Information[edit source | edit]

You are kindly invited to share additional interesting facts.

Literature[edit source | edit]

References[edit source | edit]

  1. R Allyn Forsyth, Robert J Haselbeck, Kari L Ohlsen, Robert T Yamamoto, Howard Xu, John D Trawick, Daniel Wall, Liangsu Wang, Vickie Brown-Driver, Jamie M Froelich, Kedar G C, Paula King, Melissa McCarthy, Cheryl Malone, Brian Misiner, David Robbins, Zehui Tan, Zhan-yang Zhu Zy, Grant Carr, Deborah A Mosca, Carlos Zamudio, J Gordon Foulkes, Judith W Zyskind
    A genome-wide strategy for the identification of essential genes in Staphylococcus aureus.
    Mol. Microbiol.: 2002, 43(6);1387-400
    [PubMed:11952893] [WorldCat.org] (P p)
  2. 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 2.19 2.20 2.21 2.22 2.23 2.24 2.25 2.26 2.27 2.28 2.29 2.30 2.31 2.32 2.33 2.34 2.35 2.36 2.37 2.38 2.39 2.40 2.41 2.42 2.43 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 source | edit]

Alexander Scherl, Patrice François, Manuela Bento, Jacques M Deshusses, Yvan Charbonnier, Véronique Converset, Antoine Huyghe, Nadia Walter, Christine Hoogland, Ron D Appel, Jean-Charles Sanchez, Catherine G Zimmermann-Ivol, Garry L Corthals, Denis F Hochstrasser, Jacques Schrenzel
Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth.
J. Microbiol. Methods: 2005, 60(2);247-57
[PubMed:15590099] [WorldCat.org] [DOI] (P p)