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NCBI: 10-JUN-2013

⊟Summary[edit | edit source]

  • organism: Staphylococcus aureus COL
  • locus tag: SACOL0960 [new locus tag: SACOL_RS04920 ]
  • pan locus tag?: SAUPAN003059000
  • symbol: rocD
  • pan gene symbol?: rocD
  • synonym:
  • product: ornithine--oxo-acid transaminase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: SACOL0960 [new locus tag: SACOL_RS04920 ]
  • symbol: rocD
  • product: ornithine--oxo-acid transaminase
  • replicon: chromosome
  • strand: +
  • coordinates: 961329..962519
  • length: 1191
  • 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
    ATGACTAAATCTGAAAAAATTATTGAGTTAACAAATCATTACGGAGCACATAATTATTTA
    CCATTGCCAATTGTCATTTCAGAAGCTGAAGGGGTATGGGTTAAAGATCCTGAAGGCAAT
    AAATATATGGATATGTTATCTGCATATTCCGCTGTTAACCAAGGTCATAGACATCCGAAA
    ATTATTCAAGCATTAAAAGATCAAGCTGATAAAGTGACTTTAGTTTCACGTGCTTTTCAT
    AGTGATAACTTAGGTGAATGGTACGAAAAAATTTGTAAACTGGCAGGTAAAGATAAAGCT
    TTACCAATGAATACAGGTGCTGAAGCAGTAGAAACAGCTTTGAAAGCAGCACGACGCTGG
    GCATACGATGTTAAAGGAATTGAGCCAAATAAAGCAGAAATCATTGCATTTAATGGTAAC
    TTCCATGGTCGAACAATGGCGCCAGTTTCATTATCTTCAGAAGCAGAATACCAACGTGGT
    TATGGTCCGTTATTAGATGGATTTAGAAAAGTTGATTTTGGAGATGTAGATGCATTGAAA
    GCTGCAATTAATGAAAATACTGCAGCAGTTTTAGTAGAACCAATTCAAGGTGAAGCGGGT
    ATAAATATACCGCCAGAAGGATATTTGAAAGCAATTAGAGAATTATGTGATGAACATAAT
    GTCTTATTTATTGCTGACGAAATCCAAGCAGGATTAGGTCGTTCGGGTAAATTATTTGCT
    ACGGATTGGGATAATGTAAAACCTGATGTCTATATTTTAGGTAAAGCACTAGGTGGTGGA
    GTCTTCCCAATTTCTGTTGTATTAGCAGATAAAGAAGTATTAGATGTCTTTACACCTGGC
    TCACATGGTTCAACATTTGGTGGTAATCCACTTGCTTGTGCTGCATCAATTGCTGCATTA
    GATGTTATCGTTGATGAGGATTTACCAGGCCGCTCTTTAGAATTAGGAGATTATTTTAAA
    GAACAATTAAAGCAAATTGATCATCCATCAATTAAAGAAGTCCGTGGACGTGGTTTGTTT
    ATAGGTGTGGAACTTAATGAAAGTGCTAGACCATATTGTGAAGCTTTGAAAGAAGAAGGC
    TTATTATGTAAAGAAACGCATGATACTGTCATTCGTTTTGCACCACCATTAATTATTACT
    AAAGAAGAATTGGACCTTGCACTTGAAAAAATAAGACATGTATTTCAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1191

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: SACOL0960 [new locus tag: SACOL_RS04920 ]
  • symbol: RocD
  • description: ornithine--oxo-acid transaminase
  • length: 396
  • theoretical pI: 5.02774
  • theoretical MW: 43417.2
  • GRAVY: -0.183333

⊟Function[edit | edit source]

  • reaction:
    EC 2.6.1.13?  ExPASy
    Ornithine aminotransferase L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid
  • TIGRFAM:
    ornithine--oxo-acid transaminase (TIGR01885; EC 2.6.1.13; HMM-score: 538.4)
    and 16 more
    transaminase, acetylornithine/succinylornithine family (TIGR00707; HMM-score: 402)
    Metabolism Energy metabolism Amino acids and amines succinylornithine transaminase family (TIGR03246; EC 2.6.1.81; HMM-score: 310.5)
    Metabolism Central intermediary metabolism Polyamine biosynthesis putrescine aminotransferase (TIGR03372; EC 2.6.1.82; HMM-score: 256.2)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Biotin adenosylmethionine-8-amino-7-oxononanoate transaminase (TIGR00508; EC 2.6.1.62; HMM-score: 249.2)
    Metabolism Central intermediary metabolism Other 4-aminobutyrate transaminase (TIGR00700; EC 2.6.1.19; HMM-score: 248.1)
    Metabolism Central intermediary metabolism Other 2,4-diaminobutyrate 4-transaminase (TIGR00709; EC 2.6.1.-; HMM-score: 209.8)
    Cellular processes Cellular processes Adaptations to atypical conditions diaminobutyrate--2-oxoglutarate aminotransferase (TIGR02407; EC 2.6.1.76; HMM-score: 188.8)
    L-lysine 6-transaminase (TIGR03251; EC 2.6.1.36; HMM-score: 155.7)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Heme, porphyrin, and cobalamin glutamate-1-semialdehyde-2,1-aminomutase (TIGR00713; EC 5.4.3.8; HMM-score: 143.3)
    Metabolism Central intermediary metabolism Other 4-aminobutyrate aminotransferase (TIGR00699; EC 2.6.1.19; HMM-score: 107)
    Genetic information processing Protein synthesis tRNA and rRNA base modification cysteine desulfurase IscS (TIGR02006; EC 2.8.1.7; HMM-score: 16.4)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other cysteine desulfurase IscS (TIGR02006; EC 2.8.1.7; HMM-score: 16.4)
    cysteine desulfurase, NifS family (TIGR03403; EC 2.8.1.7; HMM-score: 15.6)
    Metabolism Energy metabolism Amino acids and amines tyrosine aminotransferase (TIGR01264; EC 2.6.1.5; HMM-score: 15.1)
    tyrosine/nicotianamine family aminotransferase (TIGR01265; HMM-score: 15)
    cysteine desulfurase NifS (TIGR03402; EC 2.8.1.7; HMM-score: 11.8)
  • TheSEED  :
    • Ornithine aminotransferase (EC 2.6.1.13)
    Amino Acids and Derivatives Arginine; urea cycle, polyamines Arginine and Ornithine Degradation  Ornithine aminotransferase (EC 2.6.1.13)
  • PFAM:
    PLP_aminotran (CL0061) Aminotran_3; Aminotransferase class-III (PF00202; HMM-score: 446.1)
    and 4 more
    Aminotran_1_2; Aminotransferase class I and II (PF00155; HMM-score: 24.2)
    DegT_DnrJ_EryC1; DegT/DnrJ/EryC1/StrS aminotransferase family (PF01041; HMM-score: 23)
    Beta_elim_lyase; Beta-eliminating lyase (PF01212; HMM-score: 14.9)
    Aminotran_5; Aminotransferase class-V (PF00266; HMM-score: 12.1)

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

  • domains:
  • modifications:
  • cofactors: pyridoxal 5'-phosphate
  • 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): 0.007347
    • TAT(Tat/SPI): 0.00029
    • LIPO(Sec/SPII): 0.000678
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

⊟Protein sequence[edit | edit source]

  • MTKSEKIIELTNHYGAHNYLPLPIVISEAEGVWVKDPEGNKYMDMLSAYSAVNQGHRHPKIIQALKDQADKVTLVSRAFHSDNLGEWYEKICKLAGKDKALPMNTGAEAVETALKAARRWAYDVKGIEPNKAEIIAFNGNFHGRTMAPVSLSSEAEYQRGYGPLLDGFRKVDFGDVDALKAAINENTAAVLVEPIQGEAGINIPPEGYLKAIRELCDEHNVLFIADEIQAGLGRSGKLFATDWDNVKPDVYILGKALGGGVFPISVVLADKEVLDVFTPGSHGSTFGGNPLACAASIAALDVIVDEDLPGRSLELGDYFKEQLKQIDHPSIKEVRGRGLFIGVELNESARPYCEALKEEGLLCKETHDTVIRFAPPLIITKEELDLALEKIRHVFQ

⊟Experimental data[edit | edit source]

  • experimentally validated: PeptideAtlas
  • protein localization: Cytoplasmic [1] [2] [3] [4]
  • quantitative data / protein copy number per cell: 683 [5]
  • interaction partners:
    SACOL2657(arcA)arginine deiminase  [6] (data from MRSA252)
    SACOL1637(dnaK)molecular chaperone DnaK  [6] (data from MRSA252)
    SACOL2415(gpmA)phosphoglyceromutase  [6] (data from MRSA252)
    SACOL1741(icd)isocitrate dehydrogenase  [6] (data from MRSA252)
    SACOL2623(mqo2)malate:quinone oxidoreductase  [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)
    SACOL0839(pgk)phosphoglycerate kinase  [6] (data from MRSA252)
    SACOL1745(pyk)pyruvate kinase  [6] (data from MRSA252)
    SACOL0584(rplA)50S ribosomal protein L1  [6] (data from MRSA252)
    SACOL2236(rplB)50S ribosomal protein L2  [6] (data from MRSA252)
    SACOL2227(rplE)50S ribosomal protein L5  [6] (data from MRSA252)
    SACOL2220(rplO)50S ribosomal protein L15  [6] (data from MRSA252)
    SACOL1257(rplS)50S ribosomal protein L19  [6] (data from MRSA252)
    SACOL1725(rplT)50S ribosomal protein L20  [6] (data from MRSA252)
    SACOL1702(rplU)50S ribosomal protein L21  [6] (data from MRSA252)
    SACOL1700(rpmA)50S ribosomal protein L27  [6] (data from MRSA252)
    SACOL1274(rpsB)30S ribosomal protein S2  [6] (data from MRSA252)
    SACOL1769(rpsD)30S ribosomal protein S4  [6] (data from MRSA252)
    SACOL2222(rpsE)30S ribosomal protein S5  [6] (data from MRSA252)
    SACOL2206(rpsI)30S ribosomal protein S9  [6] (data from MRSA252)
    SACOL2214(rpsK)30S ribosomal protein S11  [6] (data from MRSA252)
    SACOL0594(tuf)elongation factor Tu  [6] (data from MRSA252)
    SACOL0564pyridoxal biosynthesis lyase PdxS  [6] (data from MRSA252)
    SACOL0944NADH dehydrogenase  [6] (data from MRSA252)
    SACOL0973fumarylacetoacetate hydrolase  [6] (data from MRSA252)
    SACOL1759universal stress protein  [6] (data from MRSA252)

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulators: ArgR (repression) regulon, CcpA regulon
    ArgR(TF)important in Arginine biosynthesis, Arginine degradation; RegPrecise 
    CcpA(TF)important in Carbon catabolism; RegPrecise 

⊟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 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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