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.
Original language | English (US) |
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Pages (from-to) | 1-6 |
Number of pages | 6 |
Journal | Proteins: Structure, Function and Genetics |
Volume | 59 |
Issue number | 1 |
DOIs | |
State | Published - Apr 1 2005 |
Keywords
- Actinobacteria
- Carboxylesterase
- Fungal lipase
- Genomic context
- Structure prediction
- Triad
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology