The database of epoxide hydrolases and haloalkane dehalogenases: one structure, many functions.
The epoxide hydrolases and haloalkane dehalogenases database (EH/HD) integrates sequence and structure of a highly diverse protein family, including mainly the Asp-hydrolases of EHs and HDs but also proteins, such as Ser-hydrolases non-heme peroxidases, prolyl iminopetidases and 2-hydroxymuconic semialdehyde hydrolases. These proteins have a highly conserved structure, but display a remarkable diversity in sequence and function. A total of 305 protein entries were assigned to 14 homologous families, forming two superfamilies. Annotated multisequence alignments and phylogenetic trees are provided for each homologous family and superfamily. Experimentally derived structures of 19 proteins are superposed and consistently annotated. Sequence and structure of all 305 proteins were systematically analysed. Thus, deeper insight is gained into the role of a highly conserved sequence motifs and structural elements.


BACKGROUND
The EH/HD database is available at http://www.led.uni-stuttgart.de
Barth
Sandra
S
Institute of Technical Biochemistry, University of Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany.
Fischer
Markus
M
Schmid
Rolf D
RD
Pleiss
Jürgen
J
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D030562:Databases, Protein; D004282:Documentation / Q000379:methods*; D004851:Epoxide Hydrolases / Q000737:chemistry* / Q000145:classification; D006867:Hydrolases / Q000737:chemistry* / Q000145:classification; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D016415:Sequence Alignment / Q000379:methods*; D020539:Sequence Analysis, Protein / Q000379:methods*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D006867:Hydrolases; D004851:Epoxide Hydrolases; C046137:haloalkane dehalogenase