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Gene Review

frdA  -  anaerobic fumarate reductase catalytic and...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4150, JW4115
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Disease relevance of frdA


High impact information on frdA


Chemical compound and disease context of frdA


Biological context of frdA


Anatomical context of frdA


Associations of frdA with chemical compounds

  • In contrast, a third mutant (the narX32 mutant) required molybdenum but did not exhibit full repression of frdA-lacZ expression even when nitrate was present [15].
  • However, the mutation did not impair the ability of the membrane-bound fumarate reductase complex to function with succinate as substrate, as evidenced by unchanged turnover numbers for phenazine methosulfate and 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone (a quinone analogue) reductase activities [7].
  • To better define the individual roles of the FrdC and FrdD polypeptides in FRD complex formation and quinone binding, we selectively mutagenized the frdCD genes [8].
  • The catalytic domain of fumarate reductase consists of the FrdA subunit, which contains the active site, and a FAD prosthetic group covalently attached to His44, plus the FrdB subunit which contains at least two of the three nonidentical iron-sulfur clusters of the enzyme [10].
  • The data confirm that cysteine 247 of FrdA is responsible for the N-ethylmaleimide sensitivity shown by fumarate reductase but is not required for catalytic activity or the tight-binding of oxalacetate, as previously thought [19].

Physical interactions of frdA


Other interactions of frdA


Analytical, diagnostic and therapeutic context of frdA


  1. Genetic and physical characterization of lambda transducing phages (lambda frdA) containing the fumarate reductase gene of Escherichia coli K12. Cole, S.T., Guest, J.R. Mol. Gen. Genet. (1980) [Pubmed]
  2. Regulation of Escherichia coli fumarate reductase (frdABCD) operon expression by respiratory electron acceptors and the fnr gene product. Jones, H.M., Gunsalus, R.P. J. Bacteriol. (1987) [Pubmed]
  3. The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes. Lauterbach, F., Körtner, C., Albracht, S.P., Unden, G., Kröger, A. Arch. Microbiol. (1990) [Pubmed]
  4. Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris. Extensive sequence divergence of the membrane anchors and absence of an frd-linked ampC cephalosporinase gene. Cole, S.T. Eur. J. Biochem. (1987) [Pubmed]
  5. Crystallization and preliminary X-ray crystallographic analysis of a periplasmic tetrahaem flavocytochrome c3 from Shewanella frigidimarina NCIMB400 which has fumarate reductase activity. Bamford, V., Dobbin, P.S., Lee, S.C., Reilly, A., Powell, A.K., Richardson, D.J., Hemmings, A.M. Acta Crystallogr. D Biol. Crystallogr. (1999) [Pubmed]
  6. Structure of the Escherichia coli fumarate reductase respiratory complex. Iverson, T.M., Luna-Chavez, C., Cecchini, G., Rees, D.C. Science (1999) [Pubmed]
  7. Oxidation of reduced menaquinone by the fumarate reductase complex in Escherichia coli requires the hydrophobic FrdD peptide. Cecchini, G., Thompson, C.R., Ackrell, B.A., Westenberg, D.J., Dean, N., Gunsalus, R.P. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  8. Electron transfer from menaquinol to fumarate. Fumarate reductase anchor polypeptide mutants of Escherichia coli. Westenberg, D.J., Gunsalus, R.P., Ackrell, B.A., Cecchini, G. J. Biol. Chem. (1990) [Pubmed]
  9. Influence of nar (nitrate reductase) genes on nitrate inhibition of formate-hydrogen lyase and fumarate reductase gene expression in Escherichia coli K-12. Stewart, V., Berg, B.L. J. Bacteriol. (1988) [Pubmed]
  10. Fumarate reductase mutants of Escherichia coli that lack covalently bound flavin. Blaut, M., Whittaker, K., Valdovinos, A., Ackrell, B.A., Gunsalus, R.P., Cecchini, G. J. Biol. Chem. (1989) [Pubmed]
  11. Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site. Iverson, T.M., Luna-Chavez, C., Croal, L.R., Cecchini, G., Rees, D.C. J. Biol. Chem. (2002) [Pubmed]
  12. Molybdenum effector of fumarate reductase repression and nitrate reductase induction in Escherichia coli. Iuchi, S., Lin, E.C. J. Bacteriol. (1987) [Pubmed]
  13. Homology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species. Lévêque, F., Plateau, P., Dessen, P., Blanquet, S. Nucleic Acids Res. (1990) [Pubmed]
  14. In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA operon control regions of Escherichia coli K-12. Li, J., Kustu, S., Stewart, V. J. Mol. Biol. (1994) [Pubmed]
  15. Nitrate- and molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli. Kalman, L.V., Gunsalus, R.P. J. Bacteriol. (1990) [Pubmed]
  16. Structure of fumarate reductase on the cytoplasmic membrane of Escherichia coli. Lemire, B.D., Robinson, J.J., Bradley, R.D., Scraba, D.G., Weiner, J.H. J. Bacteriol. (1983) [Pubmed]
  17. Electron-transfer complexes of Ascaris suum muscle mitochondria. III. Composition and fumarate reductase activity of complex II. Kita, K., Takamiya, S., Furushima, R., Ma, Y.C., Suzuki, H., Ozawa, T., Oya, H. Biochim. Biophys. Acta (1988) [Pubmed]
  18. Isolation and characterization of the tubular organelles induced by fumarate reductase overproduction in Escherichia coli. Elmes, M.L., Scraba, D.G., Weiner, J.H. J. Gen. Microbiol. (1986) [Pubmed]
  19. Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis. Schröder, I., Gunsalus, R.P., Ackrell, B.A., Cochran, B., Cecchini, G. J. Biol. Chem. (1991) [Pubmed]
  20. Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli. Wood, D., Darlison, M.G., Wilde, R.J., Guest, J.R. Biochem. J. (1984) [Pubmed]
  21. Location and nucleotide sequence of frdB, the gene coding for the iron-sulphur protein subunit of the fumarate reductase of Escherichia coli. Cole, S.T., Grundström, T., Jaurin, B., Robinson, J.J., Weiner, J.H. Eur. J. Biochem. (1982) [Pubmed]
  22. Overlap between ampC and frd operons on the Escherichia coli chromosome. Grundström, T., Jaurin, B. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  23. Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli. Darlison, M.G., Guest, J.R. Biochem. J. (1984) [Pubmed]
  24. Overexpression, purification, and crystallization of the membrane-bound fumarate reductase from Escherichia coli. Luna-Chavez, C., Iverson, T.M., Rees, D.C., Cecchini, G. Protein Expr. Purif. (2000) [Pubmed]
  25. Identification and localization of enzymes of the fumarate reductase and nitrate respiration systems of escherichia coli by crossed immunoelectrophoresis. van der Plas, J., Hellingwerf, K.J., Seijen, H.G., Guest, J.R., Weiner, J.H., Konings, W.N. J. Bacteriol. (1983) [Pubmed]
  26. Purification and characterization of membrane-bound fumarate reductase from anaerobically grown Escherichia coli. Dickie, P., Weiner, J.H. Can. J. Biochem. (1979) [Pubmed]
  27. Evidence that centre 2 in Escherichia coli fumarate reductase is a [4Fe-4S]cluster. Cammack, R., Patil, D.S., Weiner, J.H. Biochim. Biophys. Acta (1986) [Pubmed]
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