01615nas a2200181   4500008004100000245012100041210006900162300001000231490000800241520089300249653003301142653008301175100001901258700001901277700001801296700001301314856010601327       2005                        eng d00aCombining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin0 aCombining data from genomes Y2H and 3D structure indicates that   a591-60 v5793 aGenomes, functional genomics data and 3D structure reflect different aspects of protein function. Here, we combine these data to predict that BolA, a widely distributed protein family with unknown function, is a reductase that interacts with a glutaredoxin. Comparisons at the 3D structure level as well as at the sequence profile level indicate homology between BolA and OsmC, an enzyme that reduces organic peroxides. Complementary to this, comparative analyses of genomes and genomics data provide strong evidence of an interaction between BolA and the mono-thiol glutaredoxin family. The interaction between BolA and a mono-thiol glutaredoxin is of particular interest because BolA does not, in contrast to its homolog OsmC, have evolutionarily conserved cysteines to provide it with reducing equivalents. We propose that BolA uses the mono-thiol glutaredoxin as the source for these.10a*Genome Glutaredoxins Models10aMolecular Oxidoreductases/chemistry/*metabolism Phylogeny Protein Conformation1 aHuynen, M., A.1 aSpronk, C., A.1 aGabaldón, T.1 aSnel, B.  uhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15670813