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Information on EC 1.5.1.50 - dihydromonapterin reductase
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EC Tree
1.5.1.50 dihydromonapterin reductaseIUBMB Comments
The enzyme, found in many Gram negative bacteria, also slowly reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase). The enzyme has no activity with NADH.
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The enzyme appears in viruses and cellular organisms
Synonyms
dihydromonapterin reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FolM
H2-MPt reductase
-
-
-
-
PA3437
pteridine reductase
PTR1
additional information
FolM
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,6,7,8-tetrahydromonapterin + NADP+ = 7,8-dihydromonapterin + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
5,6,7,8-tetrahydromonapterin:NADP+ oxidoreductase
The enzyme, found in many Gram negative bacteria, also slowly reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate (cf. EC 1.5.1.3, dihydrofolate reductase). The enzyme has no activity with NADH.
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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
6-hydroxymethyldihydropterin + NADPH + H+
? + NADP+
weak activity
-
-
?
7,8-dihydroneopterin + NADPH + H+
5,6,7,8-tetrahydroneopterin + NADP+
stereoisomer of biopterin, high activity
-
-
?
dihydromonapterin + NADPH + H+
tetrahydromonapterin + NADP+
best substrate
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
low activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
high activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
high activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
high activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
high activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
high activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
high activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
high activity
-
-
?
7,8-dihydrobiopterin + NADPH + H+
5,6,7,8-tetrahydrobiopterin + NADP+
high activity
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
-
activity of dihydrofolate reductase, EC 1.5.1.3. Activity with 7,8-dihydromonapterin is 16fold higher than that with 7,8-dihydrofolate
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
moderate activity
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
best substrate
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
best substrate
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
best substrate
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
best substrate
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
best substrate
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
best substrate
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
best substrate
-
-
?
7,8-dihydrofolate + NADPH + H+
5,6,7,8-tetrahydrofolate + NADP+
best substrate
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
high activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
high activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
high activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
high activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
high activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
high activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
high activity
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromonapterin + NADP+
high activity
-
-
?
additional information
?
-
isoform FolM possesses weak dihydrofolate reductase activity, EC 1.5.1.3
-
-
?
additional information
?
-
no substrate: folic acid, biopterin. Enzyme is able to reduce dihydrofolate, EC 1.5.1.3
-
-
?
additional information
?
-
no substrates: quinonoid form of dihydromonapterin, monapterin, dihydroneopterin
-
-
?
additional information
?
-
-
no substrates: quinonoid form of dihydromonapterin, monapterin, dihydroneopterin
-
-
?
additional information
?
-
although presumably not its primary physiological functions, this SDR pteridine reductase also exhibits dihydrofolate reductase (DHFR) activity in vitro. Substrate specificity, overview. No activity with biopterin and folate
-
-
-
additional information
?
-
substrate specificity, overview. No activity with biopterin and folate
-
-
-
additional information
?
-
substrate specificity, overview. No activity with biopterin and folate
-
-
-
additional information
?
-
substrate specificity, overview. No activity with biopterin and folate
-
-
-
additional information
?
-
substrate specificity, overview. No activity with biopterin and folate
-
-
-
additional information
?
-
substrate specificity, overview. No activity with biopterin and folate
-
-
-
additional information
?
-
substrate specificity, overview. No activity with biopterin and folate
-
-
-
additional information
?
-
substrate specificity, overview. No activity with biopterin and folate
-
-
-
additional information
?
-
substrate specificity, overview. No activity with biopterin and folate
-
-
-
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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-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
7,8-dihydromonapterin + NADPH + H+
5,6,7,8-tetrahydromoapterin + NADP+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
cofactor binding increases in presence of betaine, and weakens in presence of ethylene glycol and polyethylene glycol 400
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.63
recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydroneopterin
1.87
recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydrobiopterin
4.3
recombinant enzyme, pH 6.0, 25°C, substrate 7,8-dihydromonapterin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
evolution
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
evolution
-
the enzyme belong to the short-chain dehydrogenase/reductase (SDR) family of enzymes. Despite the overall low sequence identity among members of the SDR family (about 15-30%), a central catalytic YX3K motif is highly conserved, as is an N-terminal glycine motif (TGX3GXG), involved in cofactor binding and recognition. The pteridine reductases in the SDR family have an arginine in place of the glycine at position 6 in this motif (TGX3RXG)
-
physiological function
dihydroneopterin triphosphate epimerase folX and dihydromonapterin reductase folM are essential for Pseudomonas aeruginosa phenylalanine hydroxylase function in Escherichia coli
physiological function
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR)
physiological function
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. FolM from Escherichia coli displays activity only with the dihydro form of its pterin substrate
physiological function
-
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR)
-
physiological function
-
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR)
-
physiological function
-
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR)
-
physiological function
-
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR)
-
physiological function
-
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR)
-
physiological function
-
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR)
-
physiological function
-
FolM produces tetrahydromonapterin (H4MPt), the cofactor of phenylalanine hydroxylase in specific bacteria. Although PA3437 is originally defined as FolM and is encoded in a gene cluster with other genes involved in tetrahydromoapterin (H4MPt) biosynthesis (FolE and FolX), its high activity with dihydrofolate (H2F) implicates this pteridine reductase as a potential backup dihydrofolate reductase (DHFR)
-
Show AA Sequence and Transmembrane Helices (818 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DMSO
both DMSO and ethylene glycol decrease the stability of isoform FolM
Ethylene glycol
both DMSO and ethylene glycol decrease the stability of isoform FolM
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene folM, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli
gene folM, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli
gene folM, recombinant overexpression of N-terminally His6-tagged enzyme in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Giladi, M.; Altman-Price, N.; Levin, I.; Levy, L.; Mevarech, M.
FolM, a new chromosomally encoded dihydrofolate reductase in Escherichia coli
J. Bacteriol.
185
7015-7018
2003
Escherichia coli (P0AFS3)
brenda
Pribat, A.; Blaby, I.K.; Lara-Nunez, A.; Gregory, J.F.; de Crecy-Lagard, V.; Hanson, A.D.
FolX and FolM are essential for tetrahydromonapterin synthesis in Escherichia coli and Pseudomonas aeruginosa
J. Bacteriol.
192
475-482
2010
Escherichia coli (P0AFS3), Escherichia coli
brenda
Bhojane, P.P.; Duff, M.R.; Patel, H.C.; Vogt, M.E.; Howell, E.E.
Investigation of osmolyte effects on FolM: comparison with other dihydrofolate reductases
Biochemistry
53
1330-1341
2014
Escherichia coli (P0AFS3)
brenda
Labine, M.; DePledge, L.; Feirer, N.; Greenwich, J.; Fuqua, C.; Allen, K.
Enzymatic and mutational analysis of the PruA pteridine reductase required for pterin-dependent control of biofilm formation in Agrobacterium tumefaciens
J. Bacteriol.
202
e00098-20
2020
Escherichia coli (P0AFS3), Pseudomonas aeruginosa (Q9HYG9), Pseudomonas aeruginosa ATCC 15692 (Q9HYG9), Pseudomonas aeruginosa 1C (Q9HYG9), Pseudomonas aeruginosa PRS 101 (Q9HYG9), Pseudomonas aeruginosa DSM 22644 (Q9HYG9), Pseudomonas aeruginosa CIP 104116 (Q9HYG9), Pseudomonas aeruginosa LMG 12228 (Q9HYG9), Pseudomonas aeruginosa JCM 14847 (Q9HYG9)
brenda
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Release 2023.1 (January 2023)
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