A putative FAD-binding domain in a distinct group of oxidases including a protein involved in plant development.
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.
Mushegian
A R
AR
Department of Microbiology, University of Washington, Seattle 98195, USA.
Koonin
E V
EV
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000254:growth & development; D029681:Arabidopsis Proteins; D001665:Binding Sites / Q000235:genetics; D017124:Conserved Sequence; D005182:Flavin-Adenine Dinucleotide; D005420:Flavoproteins / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics*; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D029681:Arabidopsis Proteins; C091574:DIM1 protein, Arabidopsis; D005420:Flavoproteins; D010940:Plant Proteins; D005182:Flavin-Adenine Dinucleotide; D010088:Oxidoreductases