A putative FAD‐binding domain in a distinct group of oxidases including a protein involved in plant development
Open Access
- 1 June 1995
- journal article
- research article
- Published by Wiley in Protein Science
- Vol. 4 (6) , 1243-1244
Abstract
Using methods for database screening with individual protein sequences and alignment blocks, a conserved domain is delineated in a group of proteins including several FAD‐dependent oxidases. Two motifs within this domain resemble phosphate‐binding loops and may be directly involved in FAD binding. These motifs can be readily distinguished from previously described nucleotide‐binding sites using a method for database screening with position‐dependent weight matrices derived from alignment blocks. Unexpectedly, this group of known and predicted FAD‐dependent oxidases includes the product of the DIMINUTO gene, which is involved in Arabidopsis development, and its homologues from man and Mycobacterium leprae.Keywords
This publication has 13 references indexed in Scilit:
- The DIMINUTO gene of Arabidopsis is involved in regulating cell elongation.Genes & Development, 1995
- Detection of conserved segments in proteins: iterative scanning of sequence databases with alignment blocks.Proceedings of the National Academy of Sciences, 1994
- A P‐loop‐like motif in a widespread ATP pyrophosphatase domain: Implications for the evolution of sequence motifs and enzyme activityProteins: Structure, Function, and Bioinformatics, 1994
- Issues in searching molecular sequence databasesNature Genetics, 1994
- Biosynthesis and Function of Enzymes with Covalently Bound FlavinAnnual Review of Nutrition, 1993
- Prediction of Protein Secondary Structure at Better than 70% AccuracyJournal of Molecular Biology, 1993
- Binding of nucleotides by proteinsCurrent Opinion in Structural Biology, 1992
- The P-loop — a common motif in ATP- and GTP-binding proteinsTrends in Biochemical Sciences, 1990
- Basic local alignment search toolJournal of Molecular Biology, 1990
- Site‐directed mutagenesis of the FAD‐binding histidine of 6‐hydroxy‐D‐nicotine oxidaseFEBS Letters, 1989