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Information on EC 2.1.1.231 - flavonoid 4'-O-methyltransferase
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EC Tree
2.1.1.231 flavonoid 4'-O-methyltransferaseIUBMB Comments
The enzyme catalyses the 4'-methylation of naringenin. In vitro it catalyses the 4'-methylation of apigenin, quercetin, daidzein and genistein.
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Word Map
- 2.1.1.231
- quercetin
-
4'-o-methylation
- flavone
- naringenin
- luteolin
-
saccharopolyspora
-
4'-methylated
- flavanones
- acacetin
- rebeccamycin
-
rhamnosyl
- kaempferol
- apigenin
-
spinosyn
-
indolocarbazole
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
4'-o-methyltransferase, somt-2, somt2, f 4'-omt, germiii, s-adenosyl-l-methionine:flavonoid 4'-o-methyltransferase, b-ring 4'omt, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4'OMT
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 4'-hydroxyflavanone = S-adenosyl-L-homocysteine + a 4'-methoxyflavanone
S-adenosyl-L-methionine + a 4'-hydroxyflavanone = S-adenosyl-L-homocysteine + a 4'-methoxyflavanone
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-
-
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S-adenosyl-L-methionine + a 4'-hydroxyflavanone = S-adenosyl-L-homocysteine + a 4'-methoxyflavanone
kinetic analysis indicates a Ping-Pong mechanism and excludes the formation of a ternary complex
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase
The enzyme catalyses the 4'-methylation of naringenin. In vitro it catalyses the 4'-methylation of apigenin, quercetin, daidzein and genistein.
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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
4'-hydroxyflavanone + S-adenosyl-L-methionine
4'-methoxyflavanone + S-adenosyl-L-homocysteine
-
-
-
-
?
apigenin + S-adenosyl-L-methionine
acacetin + S-adenosyl-L-homocysteine
-
-
-
-
?
genistein + S-adenosyl-L-methionine
biochanin A + S-adenosyl-L-homocysteine
-
-
-
-
?
kaempferol + S-adenosyl-L-methionine
kaempferide + S-adenosyl-L-homocysteine
-
-
-
-
?
S-adenosyl-L-methionine + 3'-O-methyleriodictyol
S-adenosyl-L-homocysteine + 3',4'-O-dimethyleriodictyol
-
product identification by mass spectrometry
-
?
S-adenosyl-L-methionine + alizarin
S-adenosyl-L-homocysteine + methylalizarin
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-
-
?
S-adenosyl-L-methionine + apigenin
S-adenosyl-L-homocysteine + acacetin
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36% of the activity relative to naringenin. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
-
-
?
S-adenosyl-L-methionine + chrysoeriol
S-adenosyl-L-homocysteine + 4'-O-methylchrysoeriol
-
-
-
?
S-adenosyl-L-methionine + daidzein
S-adenosyl-L-homocysteine + formononetin
-
90% of the activity relative to naringenin. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
-
-
?
S-adenosyl-L-methionine + eriodictyol
S-adenosyl-L-homocysteine + 4'-O-methyleriodictyol
-
-
-
?
S-adenosyl-L-methionine + fisetin
S-adenosyl-L-homocysteine + 4'-methoxyfisetin
8% activity with fisetin compared to quercetin
-
-
?
S-adenosyl-L-methionine + genistein
S-adenosyl-L-homocysteine + biochanin A
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62% of the activity relative to naringenin. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
-
-
?
S-adenosyl-L-methionine + isorhamnetin
S-adenosyl-L-homocysteine + 4'-O-methylisorhamnetin
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-
-
?
S-adenosyl-L-methionine + kaempferol
S-adenosyl-L-homocysteine + 4'-O-methylkaempferol
-
-
-
?
S-adenosyl-L-methionine + luteolin
S-adenosyl-L-homocysteine + 4'-methoxyluteolin
67% activity with luteolin compared to quercetin
-
-
?
S-adenosyl-L-methionine + myricetin
S-adenosyl-L-homocysteine + 4'-methoxymyricetin
20% activity with luteolin compared to quercetin
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 4'-methoxyquercetin
best substrate, 85% conversion at 2 mM substrate
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 4'-methylquercetin
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Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + 4'-O-methylquercetin
-
-
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + tamarixetin
-
-
-
?
S-adenosyl-L-methionine + quercetin 3-O-beta-D-glucoside
S-adenosyl-L-homocysteine + 4'-methoxyquercetin 3-O-beta-D-glucoside
16% activity with quercetin glucoside compared to quercetin
-
-
?
S-adenosyl-L-methionine + naringenin
S-adenosyl-L-homocysteine + ponciretin
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i.e. 4',5,7-trihyroxyflavanone. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
i.e. 4'-methoxy-5,7-dihydroxyflavanone
-
?
S-adenosyl-L-methionine + naringenin
S-adenosyl-L-homocysteine + ponciretin
i.e. 4',5,7-trihyroxyflavanone, the enzyme transfers a methyl group to 4'-hydroxyl group of naringenin
i.e. 4'-methoxy-5,7-dihydroxyflavanone
-
?
S-adenosyl-L-methionine + naringenin
S-adenosyl-L-homocysteine + ponciretin
i.e. 4',5,7-trihyroxyflavanone, reaction of SOMT-2
i.e. 4'-methoxy-5,7-dihydroxyflavanone
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?
additional information
?
-
the only substrates found for CrOMT6 are 3'-O-methyl-eriodictyol (homoeriodictyol) and the corresponding flavones and flavonols, substrate specificty, overview. No or poor activity with naringenin, pentahydroxyflavanone, hesperetin, myricetin, 7,3'-O-dimethylquercetin, 7-O-methylquercetin, syringetin, apigenin, luteolin, tricetin, velutin, dihydrokaempferol, dihydroquercetin, dihydromyricetin, and 3'-O-methyl-dihydroquercetin, and also no activity with ferulic acid, coniferyl alcohol, vanillic acid vanillin, eugenol, isoeugenol, and guaicol. Not only the B-ring configuration, but also the size and shape of the A-ring are critical parts of the substrate specificity
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-
?
additional information
?
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-
the only substrates found for CrOMT6 are 3'-O-methyl-eriodictyol (homoeriodictyol) and the corresponding flavones and flavonols, substrate specificty, overview. No or poor activity with naringenin, pentahydroxyflavanone, hesperetin, myricetin, 7,3'-O-dimethylquercetin, 7-O-methylquercetin, syringetin, apigenin, luteolin, tricetin, velutin, dihydrokaempferol, dihydroquercetin, dihydromyricetin, and 3'-O-methyl-dihydroquercetin, and also no activity with ferulic acid, coniferyl alcohol, vanillic acid vanillin, eugenol, isoeugenol, and guaicol. Not only the B-ring configuration, but also the size and shape of the A-ring are critical parts of the substrate specificity
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-
?
additional information
?
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enzyme specifically methylates the hydroxy substituent in 4'-position of the flavones, flavanones and isoflavones in the presence of S-adenosyl-L-methionine. No activity towards hydroxycinnamic acid derivatives
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-
?
additional information
?
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SOMT-2 has a regiospecific methylation activity, resulting in transforming 4'-hydroxyl group of flavonoids B-ring to 4'-methyl group. Caffeic acid, catechol, ferulic acid, and oricinol are biotransformed at less than 1%
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-
?
additional information
?
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among the flavonoids, quercetin is the most favorable substrate, followed by luteolin, myricetin, quercetin glucoside, and fisetin, while only a single product is formed in each case. Product identification by mass-spectrometry and NMR spectrometric analysis. Susbtrate specificity, overview. Mechanistic overview of the regiospecific modification, a double bond between the C2 and the C3 and a single-ring-appended conjugate-hydroxyl group are crucial for the favorable enzymatic conversions of the GerMIII catalysis, modeling and molecular docking. Of all of the anthraquinones that are tested, only alizarin is methylated by the GerMIII at a detectable amount, whereas the methylation of all of the other remaining compounds is not evident. The common feature among the GerMIII substrates is the existence of two neighboring hydroxyl groups in the presence of a double bond between the C2 and the C3, as found in the quercetin, luteolin, myricetin, fisetin, and quercetin glucoside. GerMIII does not methylate many substrates including the close flavonoid relative catechin, which lacks the double bond between the C2 and the C3
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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
S-adenosyl-L-methionine + 3'-O-methyleriodictyol
S-adenosyl-L-homocysteine + 3',4'-O-dimethyleriodictyol
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-
-
?
S-adenosyl-L-methionine + naringenin
S-adenosyl-L-homocysteine + ponciretin
i.e. 4',5,7-trihyroxyflavanone, the enzyme transfers a methyl group to 4'-hydroxyl group of naringenin
i.e. 4'-methoxy-5,7-dihydroxyflavanone
-
?
S-adenosyl-L-methionine + quercetin
S-adenosyl-L-homocysteine + tamarixetin
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
required, 2fold activation at 20 mM. Mg2+ comprises an octahedral coordination environment that is suitable for the two aspartic-acid residues Asp279 and Asp308 and two water molecules
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
activity is increased, in both in vitro and in vivo carnation tissues, by the inoculation with Fusarium oxysporum f. sp. dianthi
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetic analysis
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
GerMIII is present on the biosynthetic gene cluster of dihydrochalcomycin, a macrolide antibiotic that is produced by the Streptomyces sp. KCTC 0041BP. Based on its dependency on the metallic cofactor requirement for its reaction, the enzyme resembles the Class-II plant OMTs
metabolism
the enzyme catalyzes the last step in the biosynthesis of the bioactive flavonoid ponciretin, biosynthetic pathways starting with glucose, overview
physiological function
the methylation at the 4'-hydroxyl group of the B-ring of flavonoids confers a structural constraint for autooxidation, importance of the regiospecific 4'-OMT
additional information
a double bond between the C2 and the C3 and a single-ring-appended conjugate-hydroxyl group are crucial for the favorable enzymatic conversions of the GerMIII catalysis, modeling and molecular docking
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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). SOMT2_SOYBN
358
0
40436
Swiss-Prot
other Location (Reliability: 4)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
three-dimensional enzyme structure analysis and modelling, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
coexpression of Oryza sativa ROMT-9, which methylates specifically at the 3'-hydroxyl group of quercetin and SOMT-2, which methylates at the 4'-hydroxyl group, in Escherichia coli. Reaction products of quercetin with the transformant show two methylation products that correspond to the 3'-methylated and the 3',4'-dimethylated quercetin. More than 90% of quercetin is converted into the 3',4'-dimethylated quercetin after 24 h incubation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography
recombinant His-tagged OMT6 in Escherichia coli by nickel affinity chromatgraphy
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of Oryza sativa ROMT-9, which methylates specifically at the 3'-hydroxyl group of quercetin and SOMT-2, which methylates at the 4'-hydroxyl group, in Escherichia coli
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DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli, functional coexpression of plant enzymes, e.g. 4-coumaroyl-CoA ligase and chalcone synthase, of different origins catalyzing steps in flavonoid biosynthesis pathways for production of naringenin from p-coumaric acid and synthesis of ponciretin and sakuranetin from naringenin in engineered and transformed Escherichia coli strain BL21(DE3)
expressed in Escherichia coli as a glutathione S-transferase fusion protein. Escherichia coli harboring SOMT-2 is grown with daidzein, geninstein, apigenin, naringenin, and quercetin, respectively, and reaction products were analyzed with thin layer chromatography and HPLC
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gene CrOMT6, DNA and amino acid sequence determination and analysis, qualitative RT-PCR expression analysis, sequence comparison and phylogenetic tree, expression of His-tagged OMT6 in Escherichia coli
gene gerMIII, GerMIII is present on the biosynthetic gene cluster of dihydrochalcomycin, a macrolide antibiotic that is produced by the Streptomyces sp. KCTC 0041BP, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
coexpression of Oryza sativa ROMT-9, which methylates specifically at the 3'-hydroxyl group of quercetin and SOMT-2, which methylates at the 4'-hydroxyl group, in Escherichia coli. Reaction products of quercetin with the transformant show two methylation products that correspond to the 3'-methylated and the 3',4'-dimethylated quercetin. More than 90% of quercetin is converted into the 3',4'-dimethylated quercetin after 24 h incubation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Curir, P.; Lanzotti, V.; Dolci, M.; Dolci, P.; Pasini, C.; Tollin, G.
Purification and properties of a new S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase from carnation (Dianthus caryophyllus L.)
Eur. J. Biochem.
270
3422-3431
2003
Dianthus caryophyllus
brenda
Schroeder, G.; Wehinger, E.; Lukacin, R.; Wellmann, F.; Seefelder, W.; Schwab, W.; Schroeder, J.
Flavonoid methylation: a novel 4'-O-methyltransferase from Catharanthus roseus, and evidence that partially methylated flavanones are substrates of four different flavonoid dioxygenases
Phytochemistry
65
1085-1094
2004
Catharanthus roseus (Q6VCW3), Catharanthus roseus
brenda
Kim, D.H.; Kim, B.G.; Lee, Y.; Ryu, J.Y.; Lim, Y.; Hur, H.G.; Ahn, J.H.
Regiospecific methylation of naringenin to ponciretin by soybean O-methyltransferase expressed in Escherichia coli
J. Biotechnol.
119
155-162
2005
Glycine max
brenda
Kim, B.G.; Shin, K.H.; Lee, Y.; Hur, H.G.; Lim, Y.; Ahn, J.H.
Multiple regiospecific methylations of a flavonoid by plant O-methyltransferases expressed in E. coli
Biotechnol. Lett.
27
1861-1864
2005
Glycine max
brenda
Kim, M.; Kim, B.; Ahn, J.
Biosynthesis of bioactive O-methylated flavonoids in Escherichia coli
Appl. Microbiol. Biotechnol.
97
7195-7204
2013
Glycine max (C6TAY1)
brenda
Darsandhari, S.; Dhakal, D.; Shrestha, B.; Parajuli, P.; Seo, J.H.; Kim, T.S.; Sohng, J.K.
Characterization of regioselective flavonoid O-methyltransferase from the Streptomyces sp. KCTC 0041BP
Enzyme Microb. Technol.
113
29-36
2018
Streptomyces sp. KCTC 0041BP (Q331Q6)
brenda
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Release 2023.1 (January 2023)
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