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Protein domain of unknown function DUF1023 is an α/β hydrolase
Author(s) -
Zheng Mingzhu,
Ginalski Krzysztof,
Rychlewski Leszek,
Grishin Nick V.
Publication year - 2005
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20388
Subject(s) - hydrolase , catalytic triad , computational biology , structural genomics , serine hydrolase , structural similarity , homology (biology) , serine , genome , biology , nucleic acid , function (biology) , biochemistry , sequence alignment , chemistry , protein structure , genetics , enzyme , peptide sequence , amino acid , gene
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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