1.5.1.47: dihydromethanopterin reductase [NAD(P)+]
This is an abbreviated version!
For detailed information about dihydromethanopterin reductase [NAD(P)+], go to the full flat file.
Word Map on EC 1.5.1.47
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1.5.1.47
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archaea
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extorquens
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methylobacterium
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fmn
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methanogenic
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dihydrofolate
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tetrahydrofolate
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one-carbon
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corners
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reductases
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nadph-dependent
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formaldehyde
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six-histidine
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mononucleotide
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flavin
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xenovorans
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cubic
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cage
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burkholderia
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methane-producing
- 1.5.1.47
- archaea
- extorquens
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methylobacterium
- fmn
-
methanogenic
- dihydrofolate
- tetrahydrofolate
-
one-carbon
-
corners
- reductases
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nadph-dependent
- formaldehyde
-
six-histidine
- mononucleotide
- flavin
- xenovorans
-
cubic
-
cage
-
burkholderia
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methane-producing
Reaction
Synonyms
dihydromethanopterin reductase, DmrA, H2MPT reductase, Mnod_4941
ECTree
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General Information
General Information on EC 1.5.1.47 - dihydromethanopterin reductase [NAD(P)+]
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evolution
metabolism
physiological function
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
evolution
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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
-
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
-
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
-
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
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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
metabolism
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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
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metabolism
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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
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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
-
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
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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)
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)
-
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)
-
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)
-
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)
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