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Information on EC 4.1.1.102 - phenacrylate decarboxylase
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EC Tree
4.1.1.102 phenacrylate decarboxylaseIUBMB Comments
The enzyme, found in fungi, catalyses the decarboxylation of phenacrylic acids present in plant cell walls. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase.
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Word Map
- 4.1.1.102
-
p-coumaric
- styrene
- 4-vinylguaiacol
- decarboxylases
- 4-vinylphenol
-
4-vinyl
-
prfmn
-
phenylacrylic
-
1,3-dipolar
- synthesis
- pentosaceus
- 4-ethylphenol
-
vanillyl
- degradation
- brewing
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
phenolic acid decarboxylase, ferulic acid decarboxylase, fadase, phenacrylate decarboxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FADase
FDC1
ferulic acid decarboxylase
-
-
-
-
PAD
PAD1
phenolic acid decarboxylase
FDC1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-coumarate = 4-vinylphenol + CO2
(1)
-
-
-
ferulate = 4-vinylguaiacol + CO2
(3)
-
-
-
trans-cinnamate = styrene + CO2
(2)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3-phenylprop-2-enoate carboxy-lyase
The enzyme, found in fungi, catalyses the decarboxylation of phenacrylic acids present in plant cell walls. It requires a prenylated flavin cofactor that is produced by EC 2.5.1.129, flavin prenyltransferase.
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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-coumarate
4-vinylphenol + CO2
104% of the activity with ferulate
-
-
?
4-coumarate
4-vinylphenol + CO2
104% of the activity with ferulate
-
-
?
4-hydroxycinnamate
4-hydroxystyrene + CO2
66% of the rate with ferulate
-
-
?
caffeate
3,4-dihydroxystyrene + CO2
-
14% of the activity with ferulate
-
?
caffeate
3,4-dihydroxystyrene + CO2
-
14% of the activity with ferulate
-
?
additional information
?
-
no substrates: 2- or 3-hydroxycinnamate
-
-
?
additional information
?
-
-
no substrates: 2- or 3-hydroxycinnamate
-
-
?
additional information
?
-
CO2 release must occur after protonation of the product. For a range of para- and meta-substituted phenylacrylic acids, the log(kcat/KM) value for the reaction correlates well with the Hammett delta- parameter with rho = 0.39 and r2 = 0.93 consistent with the rate-determining step being the formation of styrene from the prenylated flavin-product adduct through a cycloelimination reaction
-
-
?
additional information
?
-
-
CO2 release must occur after protonation of the product. For a range of para- and meta-substituted phenylacrylic acids, the log(kcat/KM) value for the reaction correlates well with the Hammett delta- parameter with rho = 0.39 and r2 = 0.93 consistent with the rate-determining step being the formation of styrene from the prenylated flavin-product adduct through a cycloelimination reaction
-
-
?
additional information
?
-
proposed mechanism involves the formation of a putative pentacyclic intermediate formed by a 1,3 dipolar cyclo-addition of cofactor prenylated FMN with the alpha-beta double bond of the substrate, which serves to activate the substrate toward decarboxylation. Prenylated FMN is able to function as a dipole in a 1,3 dipolar cyclo-addition reaction as the initial step
-
-
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(Z)-2-fluoro-2-nitro-vinylbenzene
potent irreversible inhibitor. At 0.05 mM, enzyme is inactive within 10 min
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
0.2-1 mM, slightly enhances decarboxylation of ferulic acid without affecteing decarboxylation of 4-coumarate
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Structural and functional characterization of the transcriptional regulator Rv3488 of Mycobacterium tuberculosis H37Rv.
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7
5 - 7
-
pH 5.0-6.0: maximal activity, pH 7.0: about 45% of maximal activity
4 - 7
pH 4.0: about 30% of maximal activity, pH 7.0: about 60% of maximal activity
4 - 7
pH 4.0: maximal activity, pH 7.0: about 65% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
-
10°C: about 39% of maximal activity, 30°C: maximal activity, 40°C: no activity
10 - 50
10°C: about 70% of maximal activity, 50°C: about 40% of maximal activity
20 - 50
20°C: about 70% of maximal activity, 50°C: about 30% of maximal activity
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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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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
an endogenous amino thiol-like compound with a molecular weight greater than 1400 Da activates
physiological function
-
gene expression in Streptomyces lividans leads to expression of FDC1 and conversion of trans-cinnamic acid to styrene
physiological function
protein PAD1 catalyzes the formation of a diffusible cofactor required by FDC for decarboxylase activity. Escherichia coli protein UbiX can also activate FDC
physiological function
-
an endogenous amino thiol-like compound with a molecular weight greater than 1400 Da activates
-
physiological function
-
gene expression in Streptomyces lividans leads to expression of FDC1 and conversion of trans-cinnamic acid to styrene
-
Show AA Sequence and Transmembrane Helices (738 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
oligomer
x * 57898, mass spectrometry, x * 57898, calculated from sequence, recombinant His-tagged protein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures in complex with substrate analogues. FADase possesses a half-opened bottom beta-barrel with the catalytic pocket located between the middle of the core beta-barrel and the helical bottom. Its structure shared a high degree of similarity with members of the phenolic acid decarboxylase (PAD) superfamily. FADase catalyzed reactions by an open-closed mechanism involving a pocket on the surface of the enzyme. During decarboxylation of ferulic acid by FADase, Trp25 and Tyr27 are required for the entering and proper orientation of the substrate while Glu134 and Asn23 participate in proton transfer
modeling of structure based on PDB entry 2GC9. Residue Met57 is located at the entrance of the pocket and in the immediate vicinity of possible catalytic residues Arg60 and Glu82. Residue Met103 is spatially more distant from the two catalytic residues and located deeper in the active-site pocket
to 2.45 A resolution. The conformational flexibility of the beta2e-alpha5 loop allows access to the active site. The structure implicates Glu285 as the general base. An about 30-A-long pocket adjacent to the catalytic site may accommodate the isoprenoid tail of the substrate needed for ubiquinone biosynthesis in yeast
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F95L/D112N/V151I
F95L/D112N/V151I
M57L
mutation does not increase the ratio of decarboxylation activity toward ferulate to 4-coumarate
M57L
-
mutation does not increase the ratio of decarboxylation activity toward ferulate to 4-coumarate
-
F95L/D112N/V151I
approximately 34fold higher catalytic activity than wild-type for the production of 4-vinylguaiacol from ferulic acid, possibly due to formation of a compact active site compared with that of the wild-type
F95L/D112N/V151I
-
approximately 34fold higher catalytic activity than wild-type for the production of 4-vinylguaiacol from ferulic acid, possibly due to formation of a compact active site compared with that of the wild-type
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21 (DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
brewing
a positive relationship exists between single nucleotide polymorphisms in phenylacrylic acid decarboxylase PAD1 and ferulic acid decarboxylase FDC1 genes and the ferulic acid decarboxylation ability of industrial yeast strains. Sake, shochu, and standard top-fermenting yeasts contain a nonsense mutation of FDC1, whereas a frameshift mutation is identified in the FDC1 gene of bottom-fermenting yeast. No nonsense or frameshift mutations are detected in laboratory, wine, or weizen beer yeast strains. When FDC1 is introduced into sake and shochu yeast strains, the transformants exhibit ferulic acid decarboxylation activity
degradation
synthesis
degradation
-
expression of aldehyde dehydrogenase Ald5, phenylacrylic acid decarboxylase Pad1, and alcohol acetyltransferases Atf1 and Atf2 increases conversion of coniferyl aldehyde, ferulic acid and p-coumaric acid. Combined overexpression of ALD5, PAD1, ATF1 and ATF2 helps Saccharomyces cerevisiae in phenolics conversion and tolerance
degradation
Saccharomyces cerevisiae CEN.PK 102-3A
-
expression of aldehyde dehydrogenase Ald5, phenylacrylic acid decarboxylase Pad1, and alcohol acetyltransferases Atf1 and Atf2 increases conversion of coniferyl aldehyde, ferulic acid and p-coumaric acid. Combined overexpression of ALD5, PAD1, ATF1 and ATF2 helps Saccharomyces cerevisiae in phenolics conversion and tolerance
-
synthesis
synthesis of vanillin by use of ferulic acid decarboxylase Fdc from Bacillus pumilus and 4-vinylguaiacol oxygenase Cso2 from Caulobacter segnis. In the first stage, Escherichia coli cells expressing Fdc rapidly decarboxylate ferulic acid and completely convert 75 mM of this substrate to 4-vinylguaiacol within 2 h at pH 9.0. In the second stage, Escherichia coli cells expressing Cso2 efficiently oxidize 4-vinylguaiacol to vanillin. The concentration of vanillin reaches 52 mM (7.8 g/l) in 24 h
synthesis
-
by expressing Rhodobacter sphaeroides tyrosine ammonia lyase, in Streptomyces mobaraense, which permits the synthesis of p-coumaric acid from glucose, a strain is obtained that produces high amounts of 4-vinylphenol
synthesis
for 4-vinylphenol production directly from cellulose, L-tyrosine ammonia lyase derived from Rhodobacter sphaeroides and phenolic acid decarboxylase from Streptomyces sviceus are introduced into endoglucanase-secreting Streptomyces lividans, and the 4-vinylphenol biosynthetic pathway is constructed therein. The created transformants successfully produce 4-vinylphenol directly from cellulose
synthesis
-
styrene production from biomass-derived carbon sources, by culture of Streptomyces lividans expressing FDC1 together with Streptomyces lividans/p-encP, which produces trans-cinnamic acid. The coculture system combined with the recovery of styrene using polystyrene resin beads XAD-4 allows the production of styrene from glucose, cellobiose, or xylooligosaccharides, respectively
synthesis
-
4-hydroxystilbene is synthesized from p-coumaric acid in four parallel continuous flow reactors, using a 3D printing process with agarose bioinks, and a subsequent palladium(II) acetate-catalysed Heck reaction, with a total yield of 14.7% on a milligram scale. The enzyme shows 38% residual activity after the printing process
synthesis
-
styrene production from biomass-derived carbon sources, by culture of Streptomyces lividans expressing FDC1 together with Streptomyces lividans/p-encP, which produces trans-cinnamic acid. The coculture system combined with the recovery of styrene using polystyrene resin beads XAD-4 allows the production of styrene from glucose, cellobiose, or xylooligosaccharides, respectively
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang H.-K, H.H.; Chen L.-F, C.L.; Tokashiki M, T.M.; Ozawa T, O.T.; Taira T, T.T.; Ito S, I.S.
An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii
AMB Express
2
4
2012
Meyerozyma guilliermondii (G3XHW5), Meyerozyma guilliermondii, Meyerozyma guilliermondii ATCC 9058 (G3XHW5)
brenda
Zago, A.; Degrassi, G.; Bruschi, C.V.
Cloning, sequencing, and expression in Escherichia coli of the Bacillus pumilus gene for ferulic acid decarboxylase
Appl. Environ. Microbiol.
61
4484-4486
1995
Bacillus pumilus (Q45361), Bacillus pumilus
brenda
Bhuiya, M.W.; Lee, S.G.; Jez, J.M.; Yu, O.
Structure and mechanism of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae
Appl. Environ. Microbiol.
81
4216-4223
2015
Saccharomyces cerevisiae (Q03034), Saccharomyces cerevisiae
brenda
Gu, W.; Li, X.; Huang, J.; Duan, Y.; Meng, Z.; Zhang, K.Q.; Yang, J.
Cloning, sequencing, and overexpression in Escherichia coli of the Enterobacter sp. Px6-4 gene for ferulic acid decarboxylase
Appl. Microbiol. Biotechnol.
89
1797-1805
2011
Enterobacter sp. (C6F3U5), Enterobacter sp. Px6-4 (C6F3U5)
brenda
Lee, H.; Park, J.; Jung, C.; Han, D.; Seo, J.; Ahn, J.H.; Chong, Y.; Hur, H.G.
Enhancement of the catalytic activity of ferulic acid decarboxylase from Enterobacter sp. Px6-4 through random and site-directed mutagenesis
Appl. Microbiol. Biotechnol.
99
9473-9481
2015
Enterobacter sp. (C6F3U5), Enterobacter sp. Px6-4 (C6F3U5)
brenda
Huang, Z.; Dostal, L.; Rosazza, J.P.
Purification and characterization of a ferulic acid decarboxylase from Pseudomonas fluorescens
J. Bacteriol.
176
5912-5918
1994
Pseudomonas fluorescens (Q9R4W3), Pseudomonas fluorescens
brenda
Mukai, N.; Masaki, K.; Fujii, T.; Iefuji, H.
Single nucleotide polymorphisms of PAD1 and FDC1 show a positive relationship with ferulic acid decarboxylation ability among industrial yeasts used in alcoholic beverage production
J. Biosci. Bioeng.
118
50-55
2014
Saccharomyces cerevisiae (Q03034)
brenda
Furuya, T.; Miura, M.; Kuroiwa, M.; Kino, K.
High-yield production of vanillin from ferulic acid by a coenzyme-independent decarboxylase/oxygenase two-stage process
New Biotechnol.
32
335-339
2015
Bacillus pumilus (Q45361)
brenda
Gu, W.; Yang, J.; Lou, Z.; Liang, L.; Sun, Y.; Huang, J.; Li, X.; Cao, Y.; Meng, Z.; Zhang, K.Q.
Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4
PLoS ONE
6
e16262
2011
Enterobacter sp. (C6F3U5), Enterobacter sp. Px6-4 (C6F3U5)
brenda
Lin, F.; Ferguson, K.L.; Boyer, D.R.; Lin, X.N.; Marsh, E.N.
Isofunctional enzymes PAD1 and UbiX catalyze formation of a novel cofactor required by ferulic acid decarboxylase and 4-hydroxy-3-polyprenylbenzoic acid decarboxylase
ACS Chem. Biol.
10
1137-1144
2015
Saccharomyces cerevisiae (Q03034), Saccharomyces cerevisiae
brenda
Ferguson, K.L.; Arunrattanamook, N.; Marsh, E.N.
Mechanism of the novel prenylated flavin-containing enzyme ferulic acid decarboxylase probed by isotope effects and linear free-energy relationships
Biochemistry
55
2857-2863
2016
Saccharomyces cerevisiae (Q03034), Saccharomyces cerevisiae
brenda
Noda, S.; Kawai, Y.; Tanaka, T.; Kondo, A.
4-Vinylphenol biosynthesis from cellulose as the sole carbon source using phenolic acid decarboxylase- and tyrosine ammonia lyase-expressing Streptomyces lividans
Biores. Technol.
180
59-65
2015
Streptomyces hygroscopicus, Streptomyces sviceus (B5HL29), Streptomyces sviceus, Streptomyces cattleya (F8JS69)
brenda
Fujiwara, R.; Noda, S.; Kawai, Y.; Tanaka, T.; Kondo, A.
4-Vinylphenol production from glucose using recombinant Streptomyces mobaraense expressing a tyrosine ammonia lyase from Rhodobacter sphaeroides
Biotechnol. Lett.
38
1543-1549
2016
Streptomyces mobaraensis
brenda
Ferguson, K.L.; Eschweiler, J.D.; Ruotolo, B.T.; Marsh, E.N.G.
Evidence for a 1,3-dipolar cyclo-addition mechanism in the decarboxylation of phenylacrylic acids catalyzed by ferulic acid decarboxylase
J. Am. Chem. Soc.
139
10972-10975
2017
Saccharomyces cerevisiae (Q03034)
brenda
Fujiwara, R.; Noda, S.; Tanaka, T.; Kondo, A.
Styrene production from a biomass-derived carbon source using a coculture system of phenylalanine ammonia lyase and phenylacrylic acid decarboxylase-expressing Streptomyces lividans transformants
J. Biosci. Bioeng.
122
730-735
2016
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH499
brenda
Adeboye, P.; Bettiga, M.; Olsson, L.
ALD5, PAD1, ATF1 and ATF2 facilitate the catabolism of coniferyl aldehyde, ferulic acid and p-coumaric acid in Saccharomyces cerevisiae
Sci. Rep.
7
42635
2017
Saccharomyces cerevisiae
brenda
Peng, M.; Mittmann, E.; Wenger, L.; Hubbuch, J.; Engqvist, M.K.M.; Niemeyer, C.; Rabe, K.S.
3D-printed phenacrylate decarboxylase flow reactors for the chemoenzymatic synthesis of 4-hydroxystilbene
Chemistry
25
15998-16001
2019
Enterobacter sp.
brenda
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