Structural analysis of the fds operon encoding the NAD+-linked formate dehydrogenase of Ralstonia eutropha.

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  • Author(s): Oh JI;Oh JI; Bowien B
  • Source:
    The Journal of biological chemistry [J Biol Chem] 1998 Oct 09; Vol. 273 (41), pp. 26349-60.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
      Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
    • Subject Terms:
      Operon*; Cupriavidus necator/*enzymology ; Formate Dehydrogenases/*genetics ; NAD/*metabolism; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA Primers ; Electrons ; Formate Dehydrogenases/chemistry ; Formate Dehydrogenases/metabolism ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; Molecular Sequence Data ; Promoter Regions, Genetic ; Protein Conformation ; Sequence Homology, Amino Acid
    • Abstract:
      The fdsGBACD operon encoding the four subunits of the NAD+-reducing formate dehydrogenase of Ralstonia eutropha H16 was cloned and sequenced. Sequence comparisons indicated a high resemblance of FdsA (alpha-subunit) to the catalytic subunits of formate dehydrogenases containing a molybdenum (or tungsten) cofactor. The NH2-terminal region (residues 1-240) of FdsA, lacking in formate dehydrogenases not linked to NAD(P)+, exhibited considerable similarity to that of NuoG of the NADH:ubiquinone oxidoreductase from Escherichia coli as well as to HoxU and the NH2-terminal segment of HndD of NAD(P)+-reducing hydrogenases. FdsB (beta-subunit) and FdsG (gamma-subunit) are closely related to NuoF and NuoE, respectively, as well as to HoxF and HndA. It is proposed that the NH2-terminal domain of FdsA together with FdsB and FdsG constitute a functional entity corresponding to the NADH dehydrogenase (diaphorase) part of NADH:ubiquinone oxidoreductase and the hydrogenases. No significant similarity to any known protein was observed for FdsD (delta-subunit). The predicted product of fdsC showed the highest resemblance to FdhD from E. coli, a protein required for the formation of active formate dehydrogenases in this organism. Transcription of the fds operon is subject to formate induction. A promoter structure resembling the consensus sequence of sigma70-dependent promoters from E. coli was identified upstream of the transcriptional start site determined by primer extension analysis.
    • Molecular Sequence:
      GENBANK AJ223295
    • Accession Number:
      0 (DNA Primers)
      0U46U6E8UK (NAD)
      EC 1.17.1.9 (Formate Dehydrogenases)
    • Publication Date:
      Date Created: 19981003 Date Completed: 19981102 Latest Revision: 20210209
    • Publication Date:
      20221213
    • Accession Number:
      10.1074/jbc.273.41.26349
    • Accession Number:
      9756865