Protein domain of unknown function DUF1023 is an α/β hydrolase

Authors

  • Mingzhu Zheng,

    1. Department of Biochemistry, University of Texas, Southwestern Medical Center, Dallas, Texas
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  • Krzysztof Ginalski,

    Corresponding author
    1. Department of Biochemistry, University of Texas, Southwestern Medical Center, Dallas, Texas
    2. Interdisciplinary Centre for Mathematical and Computational Modeling, Warsaw University, Warsaw, Poland
    • Department of Biochemistry, University of Texas, Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, Texas 75390-9038
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  • Leszek Rychlewski,

    1. BioInfoBank Institute, Poznań, Poland
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  • Nick V. Grishin

    1. Howard Hughes Medical Institute, University of Texas, Southwestern Medical Center, Dallas, Texas
    2. Department of Biochemistry, University of Texas, Southwestern Medical Center, Dallas, Texas
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Abstract

Pfam family DUF1023 consists entirely of uncharacterized proteins generated by sequencing the genomes of Actinobacteria (Bateman A., et al., Nucleic Acids Res. 2004;32 Database issue:D138–141.) Utilizing sequence similarity detection methods, we infer homology between DUF1023 and α/β hydrolases. DUF1023 proteins conserve the core secondary structures in α/β hydrolase fold, and share similar catalytic machinery as that of α/β hydrolases. We predict DUF1023 spatial structure and deduce that they function as hydrolases utilizing catalytic Ser-His-Asp triad with the serine as a nucleophile. Proteins 2005. © 2005 Wiley-Liss, Inc.

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