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Microbiology and Molecular Biology Reviews, March 2000, p. 153-179, Vol. 64, No. 1
School of Plant Sciences, The University of
Reading, Reading,1 and Drug Design
Group, Department of Biochemistry, University of Cambridge,
Cambridge,2 United Kingdom
This review summarizes the recent discovery of the cupin superfamily (from the Latin term "cupa," a small barrel) of functionally diverse proteins that initially were limited to several higher plant proteins such as seed storage proteins, germin (an oxalate oxidase), germin-like proteins, and auxin-binding protein. Knowledge of the three-dimensional structure of two vicilins, seed proteins with a characteristic
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Copyright © 2000, American Society for Microbiology. All rights reserved.
Microbial Relatives of the Seed Storage Proteins of
Higher Plants: Conservation of Structure and Diversification of
Function during Evolution of the Cupin Superfamily
-barrel core, led to the identification of a small number of conserved residues and thence to the discovery of several microbial proteins which share these key amino acids. In particular, there is a highly conserved pattern of two histidine-containing motifs with a varied intermotif spacing. This cupin signature is found as a central component of many microbial proteins including certain types of phosphomannose isomerase, polyketide synthase, epimerase, and dioxygenase. In addition, the signature has been identified within the N-terminal effector domain in a subgroup of bacterial AraC transcription factors. As well as these single-domain cupins, this survey has identified other classes of two-domain bicupins including bacterial gentisate 1,2-dioxygenases and 1-hydroxy-2-naphthoate dioxygenases, fungal oxalate decarboxylases, and legume sucrose-binding proteins. Cupin evolution is discussed from the perspective of the structure-function relationships, using data from the genomes of several prokaryotes, especially Bacillus subtilis. Many of these functions involve aspects of sugar metabolism and cell wall synthesis and are concerned with responses to abiotic stress such as heat, desiccation, or starvation. Particular emphasis is also given to the oxalate-degrading enzymes from microbes, their biological significance, and their value in a range of medical and other applications.
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Corresponding author. Mailing address: School of Plant
Sciences, The University of Reading, Whiteknights P.O. Box 221, Reading RG6 6AS, United Kingdom. Phone: 44-118-931-6313. Fax: 44-118-931-6577. E-mail: J.M.Dunwell{at}reading.ac.uk.
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