EC Number   |
General Information |
Reference |
|---|
    1.5.1.47 | evolution |
homology of DmrA to dihydrofolate reductases leads to the proposal that DmrA evolved from an ancestral dihydrofolate reductase following horizontal transfer of tetrahydromethanopterin (H4MPT) biosynthesis genes from anaerobic archaea to aerobic bacteria. Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB (EC 1.5.1.3), that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA. DmrA shares no sequence homology with the FMN-containing dihydromethanopterin reductase discovered in archaea (DmrX) or related archaeallike flavoproteins (AfpA and DmrB) from beta-proteobacteria. Phylogenetic analysis and tree. Conformational modeling of DmrA and DfrB |
-, 764758 |
| 1.5.1.47 | metabolism |
dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. In the pathways of H4MPT and tetrahydrofolate (H4F) biosynthesis, the last step requires the activity of dihydromethanopterin reductase (Dmr) or dihydrofolate reductase (Dfr). Methylobacterium extorquens AM1 contains one dihydromethanopterin reductase (DmrA) and two putative dihydrofolate reductases, DfrA and DfrB, that, respectively, share 26% identity (41% similarity) and 34% identity (53% similarity) with DmrA |
-, 764758 |
| 1.5.1.47 | physiological function |
methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. Dihydromethanopterin reductase (DmrA) catalyzes the final step of tetrahydromethanopterin (H4MPT) biosynthesis. The facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F) |
-, 764758 |
