PMC:516016 / 22809-24903 JSONTXT

{"project":"2_test","denotations":[{"id":"15307895-9020585-8201961","span":{"begin":476,"end":478},"obj":"9020585"},{"id":"15307895-14722619-8201962","span":{"begin":716,"end":718},"obj":"14722619"},{"id":"15307895-3479790-8201963","span":{"begin":1053,"end":1055},"obj":"3479790"},{"id":"15307895-12641475-8201964","span":{"begin":1847,"end":1849},"obj":"12641475"}],"text":"Other subfamilies/ members\nIn the above sections we have described the 11 subfamilies that have some functional characterization. In this section we describe the other 6 subfamilies that have no functional characterization, except they are associated with other domains or have been structurally characterized.\nThe CBS associated subfamily contains the hypothetical protein BH3175 from Bacillus halodurans. The BH3175 protein contains two homologous copies of the CBS domain [54]. Scott et al. have recently shown that tandem pairs of CBS domains act as sensors of cellular energy status by binding AMP, ATP, or S-adenosyl methionine and mutations in CBS domains impair this binding in several hereditary disorders [55]. Although we do not know the substrate or activity of this subfamily of the HotDog superfamily, we can suggest that this step is regulated in an energy dependent manner by the CBS domains.\n3-hydroxyacyl-CoA dehydrogenase is an enzyme involved in fatty acid metabolism, catalyzing the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA [56]. The hydroxyacyl-CoA dehydrogenase-associated subfamily includes 3-hydroxyacyl-CoA dehydrogenase from Agrobacterium tumefaciens strain C58, which contains a HotDog domain at its C-terminus and the two domains (3HCDH_N and 3HCDH) associated with 3-hydroxyacyl-CoA dehydrogenase activity are located at the N-terminus and central portion of this protein. The combination of activities may allow substrate to be passed from one domain to the next.\nOther subfamilies in the superfamily include the YiiD protein from E. coli, where an acetyltransferase domain is fused. The human mesenchymal stem cell protein DSCD75 and its counterpart in mouse also contain a HotDog domain. A Structural proteomics project has shown that the conserved hypothetical E. coli protein YbaW contains a Hotdog fold [10]. Finally the Ralstonia solanacearum hypothetical protein RSp0367, containing a HotDog domain and two AMP-binding domains, found in proteins involved in ATP-dependent covalent binding of AMP to their substrate, is a member of another subfamily."}