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Information on EC 1.5.1.47 - dihydromethanopterin reductase [NAD(P)+]
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1.5.1.47 dihydromethanopterin reductase [NAD(P)+]IUBMB Comments
The enzyme, characterized from the bacterium Methylobacterium extorquens, is involved in biosynthesis of dephospho-tetrahydromethanopterin. The specific activity with NADH is 15% of that with NADPH at the same concentration . It does not reduce 7,8-dihydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase).
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Word Map
- 1.5.1.47
- archaea
- extorquens
-
methylobacterium
- fmn
-
methanogenic
- dihydrofolate
- tetrahydrofolate
-
one-carbon
-
corners
- reductases
-
nadph-dependent
- formaldehyde
-
six-histidine
- mononucleotide
- flavin
- xenovorans
-
cubic
-
cage
-
burkholderia
-
methane-producing
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
dihydromethanopterin reductase, h2mpt reductase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dihydromethanopterin reductase
DmrA
H2MPT reductase
Mnod_4941
dihydromethanopterin reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,6,7,8-tetrahydromethanopterin + NAD(P)+ = 7,8-dihydromethanopterin + NAD(P)H + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydromethanopterin:NAD(P)+ 5,6-oxidoreductase
The enzyme, characterized from the bacterium Methylobacterium extorquens, is involved in biosynthesis of dephospho-tetrahydromethanopterin. The specific activity with NADH is 15% of that with NADPH at the same concentration [1]. It does not reduce 7,8-dihydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7,8-dihydromethanopterin + NAD(P)H + H+
5,6,7,8-tetrahydromethanopterin + NAD(P)+
the enzyme is involved in tetrahydromethanopterin biosynthesis
-
-
?
7,8-dihydromethanopterin + NAD(P)H + H+
5,6,7,8-tetrahydromethanopterin + NAD(P)+
dihydrofolate is not a substrate, no activity with reduced methyl viologen
-
-
?
7,8-dihydromethanopterin + NAD(P)H + H+
5,6,7,8-tetrahydromethanopterin + NAD(P)+
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
the enzyme is involved in tetrahydromethanopterin biosynthesis
-
-
?
7,8-dihydromethanopterin + NAD(P)H + H+
5,6,7,8-tetrahydromethanopterin + NAD(P)+
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
dihydrofolate is not a substrate, no activity with reduced methyl viologen
-
-
?
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
-
?
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
?
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
?
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
?, r
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
?, r
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
?, r
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
?, r
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
?, r
dihydrosarcinapterin + NADPH + H+
tetrahydrosarcinapterin + NADP+
-
-
-
-
?
dihydrosarcinapterin + NADPH + H+
tetrahydrosarcinapterin + NADP+
-
-
-
?
dihydrosarcinapterin + NADPH + H+
tetrahydrosarcinapterin + NADP+
-
-
-
?
dihydrosarcinapterin + NADPH + H+
tetrahydrosarcinapterin + NADP+
-
-
-
?
dihydrosarcinapterin + NADPH + H+
tetrahydrosarcinapterin + NADP+
-
-
-
?
dihydrosarcinapterin + NADPH + H+
tetrahydrosarcinapterin + NADP+
-
-
-
?
dihydrosarcinapterin + NADPH + H+
tetrahydrosarcinapterin + NADP+
-
-
-
?
dihydrosarcinapterin + NADPH + H+
tetrahydrosarcinapterin + NADP+
-
-
-
?
additional information
?
-
-
no activity with 7,8-dihydrofolate
-
-
-
additional information
?
-
no activity with 7,8-dihydrofolate
-
-
-
additional information
?
-
-
no activity with 7,8-dihydrofolate
-
-
-
additional information
?
-
no activity with 7,8-dihydrofolate
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
7,8-dihydromethanopterin + NAD(P)H + H+
5,6,7,8-tetrahydromethanopterin + NAD(P)+
the enzyme is involved in tetrahydromethanopterin biosynthesis
-
-
?
7,8-dihydromethanopterin + NAD(P)H + H+
5,6,7,8-tetrahydromethanopterin + NAD(P)+
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
the enzyme is involved in tetrahydromethanopterin biosynthesis
-
-
?
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
r
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
r
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
r
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
r
7,8-dihydromethanopterin + NADPH + H+
5,6,7,8-tetrahydromethanopterin + NADP+
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
the specific activity with NADH is 15% of the rate observed with NADPH
NADPH
the specific activity with NADH is 15% of the rate observed with NADPH
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.193
7,8-dihydromethanopterin
pH 5.3, 23°C, recombinant C-terminally His4-tagged enzyme
additional information
additional information
Michaelis-Menten kinetics
-
0.195
dihydrosarcinapterin
pH 5.3, temperature not specified in the publication
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
7,8-dihydromethanopterin
pH 5.3, 23°C, recombinant C-terminally His4-tagged enzyme
1.5
dihydrosarcinapterin
pH 5.3, temperature not specified in the publication
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.77
7,8-dihydromethanopterin
pH 5.3, 23°C, recombinant C-terminally His4-tagged enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.24
substrate dihydrosarcinapterin, pH 5.3, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 6.3
pH 4.8: about 55% of maximal activity, pH 6.3: about 70% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 35
20°C: about 90% of maximal activit, 35°C: about 70% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
brenda
additional information
-
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
-
brenda
additional information
-
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
-
brenda
additional information
-
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
-
brenda
additional information
-
the facultative methylotroph Methylobacterium extorquens AM1, growth on single-carbon (C1) substrates involves the use of both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F)
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
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
-
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
-
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
-
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
-
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
-
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)
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DMRA_METEA
Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
135
0
15222
Swiss-Prot
-
B8IHA6_METNO
Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060)
305
0
32843
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
2 * 17000, SDS-PAGE
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzymes from Escherichia coli strain BL21 by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dmrA, phylogenetic analysis and tree, recombinant expression of N-terminally His6-tagged and C-terminally His4-tagged enzyme in Escherichia coli strain BL21
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Caccamo, M.A.; Malone, C.S.; Rasche, M.E.
Biochemical characterization of a dihydromethanopterin reductase involved in tetrahydromethanopterin biosynthesis in Methylobacterium extorquens AM1
J. Bacteriol.
186
2068-2073
2004
Methylorubrum extorquens (C5B2R8), Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1 (C5B2R8)
brenda
Burton, M.; Abanobi, C.; Wang, K.; Ma, Y.; Rasche, M.
Substrate specificity analysis of dihydrofolate/dihydromethanopterin reductase homologs in methylotrophic alpha-proteobacteria
Front. Microbiol.
9
2439
2018
Hyphomicrobium nitrativorans, Methylobacterium nodulans (B8IHA6), Methylobacterium nodulans, Methylorubrum extorquens (C5B2R8), Methylorubrum extorquens NCIMB 9133 (C5B2R8), Methylorubrum extorquens DSM 1338 (C5B2R8), Methylorubrum extorquens ATCC 14718 (C5B2R8), Methylobacterium nodulans LMG 21967 (B8IHA6), Methylorubrum extorquens JCM 2805 (C5B2R8)
brenda
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