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Information on EC 1.14.13.235 - indole-3-acetate monooxygenase
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The expected taxonomic range for this enzyme is: Pseudomonas putida
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EC NUMBER 
COMMENTARY 
1.14.13.235
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RECOMMENDED NAME
GeneOntology No.
indole-3-acetate monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(indol-3-yl)acetate + NADH + H+ + O2 = (2-hydroxy-1H-indol-3-yl)acetate + NAD+ + H2O
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(indol-3-yl)acetate,NADH:oxygen oxidoreductase (2-hydroxylating)
The enzyme, characterized from Pseudomonas putida strains, catalyses the first step in a pathway for degradation of the plant hormone indole-3-acetate. When acting on indole, the enzyme forms indoxyl, which reacts spontaneously with oxygen to form the blue dye indigo.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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strain 1290 is able to to use indole-3-acetic acid as a sole source of carbon, nitrogen, and energy. In root elongation assays, strain 1290 completely abolishes the inhibitory effect of exogenous indole-3-acetic acid on the elongation of radish roots
physiological function
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enzyme catalyzes the first step in degradation of the plant hormone indole-3-acetate. Transformation of Pseudomonas putida KT2440, which cannot degrade IAA, with the Iac gene cluster confers the ability to grow on indole-3-acetate as a sole source of carbon and energy, but not the ability to chemotaxis towards indole-3-acetate
physiological function
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enzyme catalyzes the first step in degradation of the plant hormone indole-3-acetate. Transformation of Pseudomonas putida KT2440, which cannot degrade IAA, with the Iac gene cluster confers the ability to grow on indole-3-acetate as a sole source of carbon and energy, but not the ability to chemotaxis towards indole-3-acetate; strain 1290 is able to to use indole-3-acetic acid as a sole source of carbon, nitrogen, and energy. In root elongation assays, strain 1290 completely abolishes the inhibitory effect of exogenous indole-3-acetic acid on the elongation of radish roots
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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
(indol-3-yl)acetate + NADH + H+ + O2
(2-hydroxyindol-3-yl)acetate + NAD+ + H2O
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?
(indol-3-yl)acetate + NADH + H+ + O2
(2-hydroxyindol-3-yl)acetate + NAD+ + H2O
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?
additional information
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enzyme catalyzes the hydroxylation of position 3 of the indole ring to produce indoxyl, which in the presence of oxygen dimerizes to form indigo
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additional information
?
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enzyme catalyzes the hydroxylation of position 3 of the indole ring to produce indoxyl, which in the presence of oxygen dimerizes to form indigo
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
with indole-3-acetate as the sole source of carbon and energy, the expression of IacA is more than 2 orders of magnitude greater than with glucose
with indole-3-acetate as the sole source of carbon and energy, the expression of IacA is more than 2 orders of magnitude greater than with glucose
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with indole-3-acetate as the sole source of carbon and energy, the expression of IacA is more than 2 orders of magnitude greater than with glucose
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
agriculture
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coinoculation of roots with strain 1290 and 1 mM of indole-3-acetic acid has a positive effect on root development. In coinoculation experiments on radish roots, strain 1290 is partially able to alleviate the inhibitory effect of bacteria that in culture overproduce indole-3-acetic acid
agriculture
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coinoculation of roots with strain 1290 and 1 mM of indole-3-acetic acid has a positive effect on root development. In coinoculation experiments on radish roots, strain 1290 is partially able to alleviate the inhibitory effect of bacteria that in culture overproduce indole-3-acetic acid
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.235)
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