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EC Tree
IUBMB Comments Also catalyses eliminative removal of unsaturated terminal residues from oligosaccharides of D-galacturonate.
The enzyme appears in viruses and cellular organisms
Synonyms
oligogalacturonate lyase, oligogalacturonide lyase, yeogl, oligogalacturonan lyase,
more
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lyase, oligogalacturonide
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oligogalacturonan lyase
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oligogalacturonide trans-eliminase
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oligogalacturonide transeliminase
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unsaturated oligogalacturonate transeliminase
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oligogalacturonate lyase
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oligogalacturonate lyase
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oligogalacturonate lyase
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YeOGL
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4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
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4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
also catalyses eliminative removal of unsaturated terminal residues from oligosaccharides of D-galacturonate
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4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
active site structure modeling and beta-elimination reaction mechanism, overview
4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate = 2 5-dehydro-4-deoxy-D-glucuronate
active site structure modeling and beta-elimination reaction mechanism, overview
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oligogalacturonide lyase
Also catalyses eliminative removal of unsaturated terminal residues from oligosaccharides of D-galacturonate.
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1-methyl-di-D-galacturonate
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alpha-(1-4)-linked
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1-methyl-tri-D-galacturonate
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alpha-(1-4)-linked
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3-methyl-tri-D-galacturonate
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best substrate, alpha-(1-4)-linked
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4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate
2 5-dehydro-4-deoxy-D-glucuronate
4-O-(4-deoxy-alpha-L-threo-hex-4-enopyranuronosyl)-beta-D-galactopyranuronic acid
4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid + D-galacturonic acid
Erwinia aroidea
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i.e. O-(4-deoxy-beta-L-5-threo-hexopyranos-4-enyluronic acid)-(1,4)-D-galacturonic acid
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acid-soluble pectic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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the first product is 4,5-unsaturated galacturonic acid and this compound is converted into 4-deoxy-5-keto-D-fructuronic acid by an unknown mechanism
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acid-soluble pectic acid
4-deoxy-5-keto-D-glucuronic acid
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very slow degradation
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DELTA4,5-unsaturated di-D-galacturonate
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alpha-(1-4)-linked
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DELTA4,5-unsaturated tri-D-galacturonate
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alpha-(1-4)-linked
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di-D-galacturonate
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digalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
digalacturonic acid
4-deoxy-5-keto-D-glucuronic acid + galacturonic acid
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tetragalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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the first product is 4,5-unsaturated galacturonic acid and this compound is converted into 4-deoxy-5-keto-D-fructuronic acid by an unknown mechanism
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tetragalacturonic acid
4-deoxy-5-keto-D-glucuronic acid + ?
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tri-D-galacturonate
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trigalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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the first product is 4,5-unsaturated galacturonic acid and this compound is converted into 4-deoxy-5-keto-D-fructuronic acid by an unknown mechanism
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trigalacturonic acid
4-deoxy-5-keto-D-glucuronic acid + digalacturonic acid + galacturonic acid
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unsaturated digalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
unsaturated digalacturonic acid
4-deoxy-5-keto-D-glucuronic acid + ?
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unsaturated trigalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
unsaturated trigalacturonic acid
4-deoxy-5-keto-D-glucuronic acid + unsaturated digalacturonic acid
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additional information
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4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate
2 5-dehydro-4-deoxy-D-glucuronate
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4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate
2 5-dehydro-4-deoxy-D-glucuronate
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digalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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digalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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the first product is 4,5-unsaturated galacturonic acid and this compound is converted into 4-deoxy-5-keto-D-fructuronic acid by an unknown mechanism
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digalacturonic acid
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digalacturonic acid
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tetragalacturonic acid
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tetragalacturonic acid
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trigalacturonic acid
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trigalacturonic acid
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unsaturated digalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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unsaturated digalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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unsaturated oligogalacturonates are degraded more rapidly than oligogalacturonates having no unsaturated galacturonic acid residues
the first product is 4,5-unsaturated galacturonic acid and this compound is converted into 4-deoxy-5-keto-D-fructuronic acid by an unknown mechanism
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unsaturated trigalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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unsaturated trigalacturonic acid
4-deoxy-5-keto-D-fructuronic acid + ?
Erwinia aroidea
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unsaturated oligogalacturonates are degraded more rapidly than oligogalacturonates having no unsaturated galacturonic acid residues
the first product is 4,5-unsaturated galacturonic acid and this compound is converted into 4-deoxy-5-keto-D-fructuronic acid by an unknown mechanism
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additional information
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no activity with 2-methyl-di-G-galacturonate and 2-methyl-tri-G-galacturonate
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additional information
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Erwinia aroidea
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two pathways are involved in metabolism of pectic substances: one route through galacturonic acid, involving galacturonic acid isomerase and the other through unsaturated digalacturonic acid, involving EC 4.2.2.5, with the formation of 4-deoxy-5-hexosulose uronic acid. Both pathways yield 2-keto-3-deoxy-D-gluconic acid as common product
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4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate
2 5-dehydro-4-deoxy-D-glucuronate
additional information
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Erwinia aroidea
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two pathways are involved in metabolism of pectic substances: one route through galacturonic acid, involving galacturonic acid isomerase and the other through unsaturated digalacturonic acid, involving EC 4.2.2.5, with the formation of 4-deoxy-5-hexosulose uronic acid. Both pathways yield 2-keto-3-deoxy-D-gluconic acid as common product
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4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate
2 5-dehydro-4-deoxy-D-glucuronate
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4-(4-deoxy-alpha-D-gluc-4-enuronosyl)-D-galacturonate
2 5-dehydro-4-deoxy-D-glucuronate
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Mn2+
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best cofactor, optimal concentration: 0.1 mM
Mn2+
activates, octahedral metal binding site, coordination structure involving N-His287, O-Gln350, N-His353, and His-355, overview
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pectate
substrate inhibition at high concentrations
EDTA
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EDTA
Erwinia aroidea
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no inhibition by EDTA
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0.15 - 5.3
digalacturonic acid
0.12
trigalacturonic acid
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1.6
unsaturated digalacturonic acid
Erwinia aroidea
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additional information
additional information
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0.15
digalacturonic acid
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5.3
digalacturonic acid
Erwinia aroidea
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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0.0053
Erwinia aroidea
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additional information
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substrate specificity
additional information
Erwinia aroidea
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additional information
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7
Erwinia aroidea
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6.5 - 8
Erwinia aroidea
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pH 6.5: about 45% of maximal activity, pH 8.0: about 55% of maximal activity
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3937
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brenda
Erwinia aroidea
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brenda
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brenda
subsp. enterocolitica, gene ogl, locus YE1876
UniProt
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subsp. enterocolitica, gene ogl, locus YE1876
UniProt
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3937
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phytopathogenic strain 3937. Expression level of oligogalacturonate lyase gene ogl is reduced in null knockout iaaM mutant strain Ech138
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brenda
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brenda
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brenda
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metabolism
OGL is involved in the pectin degradation pathway performing extracellular pectin depolymerization, overview. In the initial stages, intracellular di- and trigalacturonides are processed into saturated monogalacturonate, GalA, and a 4,5-unsaturated GalA-like monosaccharide, 5-keto-4-deoxyuronate, by the combined activities of an exo-acting family 2 pectate lyase,YePL2B, and oligogalacturonate lyase, YeOGL/YePL22, a lyase family preferentially active on digalacturonides
metabolism
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OGL is involved in the pectin degradation pathway performing extracellular pectin depolymerization, overview. In the initial stages, intracellular di- and trigalacturonides are processed into saturated monogalacturonate, GalA, and a 4,5-unsaturated GalA-like monosaccharide, 5-keto-4-deoxyuronate, by the combined activities of an exo-acting family 2 pectate lyase,YePL2B, and oligogalacturonate lyase, YeOGL/YePL22, a lyase family preferentially active on digalacturonides
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44124
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x * 44124, calculation from nucleotide sequence
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x * 44124, calculation from nucleotide sequence
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x * 44124, calculation from nucleotide sequence
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additional information
YeOGL adopts a seven-bladed beta-propeller fold that has structural similarity to the WD40 family of proteins
additional information
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YeOGL adopts a seven-bladed beta-propeller fold that has structural similarity to the WD40 family of proteins
additional information
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YeOGL adopts a seven-bladed beta-propeller fold that has structural similarity to the WD40 family of proteins
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purified recombinant detagged YeOGL, hanging drop vapor diffusion method, 12.5 mg/ml protein in 20 mM Tris-HCl, precipitation from 0.2 M CaCl2, 0.1 M NaOAc, pH 4.8, 20% PEG 3350, and cryoprotection by 15% ethylene glycol, 18°C, X-ray diffraction structure determination and analysis at 1.65 A resolution
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recombinant N-terminally His-tagged YeOGL from Escherichia coli by nickel affinity chromatography, ultrafiltration, His-tag cleavage through thrombin, and gel filtration
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gene ogl, phylogenetic tree of the OGL family, expression of YeOGL containing a thrombin-cleavable N-terminal His6 tag in Escherichia coli BL21-pLysS (DE3) cells
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Hatanaka, C.; Ozawa, J.
An oligogalacturonate transeliminase from Erwinia aroideae
Agric. Biol. Chem.
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1618-1624
1970
Erwinia aroidea
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brenda
Moran, F.; Nasuno, S.; Starr, M.P.
Oligogalacturonide trans-eliminase of Erwinia carotovora
Arch. Biochem. Biophys.
125
734-741
1968
Erwinia aroidea
brenda
Hatanaka, C.; Ozawa, J.
Pectolytic enzymes of exo-types. Part I. Oligogalacturonide transeliminase of a Pseudomonas
Agric. Biol. Chem.
35
1617-1624
1971
Pseudomonas sp.
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brenda
Reverchon, S.; Robert-Baudouy, J.
Molecular cloning of an Erwinia chrysanthemi oligogalacturonate lyase gene involved in pectin degradation
Gene
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125-133
1987
Dickeya chrysanthemi, Dickeya chrysanthemi 3937
brenda
Shevchik, V.E.; Condemine, G.; Robert-Baudouy, J.; Hugouvieux-Cotte-Pattat, N.
The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937
J. Bacteriol.
181
3912-3919
1999
Dickeya chrysanthemi, Dickeya chrysanthemi 3937
brenda
Reverchon, S.; Huang, Y.; Bourson, C.; Robert-Baudouy, J.
Nucleotide sequences of the Erwinia chrysanthemi ogl and pelE genes negatively regulated by the kdgR gene product
Gene
85
125-134
1989
Dickeya chrysanthemi, Dickeya chrysanthemi 3937
brenda
Kester, H.C.M.; Magaud, D.; Roy, C.; Anker, D.; Doutheau, A.; Shevchik, V.; Hugouvieux-Cotte-Pattat, N.; Benen, J.A.E.; Visser, J.
Performance of selected microbial pectinases on synthetic monomethyl-esterified di- and trigalacturonates
J. Biol. Chem.
274
37053-37059
1999
Dickeya chrysanthemi
brenda
Yang, S.; Zhang, Q.; Guo, J.; Charkowski, A.O.; Glick, B.R.; Ibekwe, A.M.; Cooksey, D.A.; Yang, C.H.
Global effect of indole-3-acetic acid biosynthesis on multiple virulence factors of Erwinia chrysanthemi 3937
Appl. Environ. Microbiol.
73
1079-1088
2007
Dickeya chrysanthemi
brenda
Abbott, D.W.; Gilbert, H.J.; Boraston, A.B.
The active site of oligogalacturonate lyase provides unique insights into cytoplasmic oligogalacturonate beta-elimination
J. Biol. Chem.
285
39029-39038
2010
Yersinia enterocolitica (A1JMA5), Yersinia enterocolitica, Yersinia enterocolitica 8081 (A1JMA5)
brenda
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