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Information on EC 1.2.7.8 - indolepyruvate ferredoxin oxidoreductase and Organism(s) Thermococcus kodakarensis and UniProt Accession O07835

for references in articles please use BRENDA:EC1.2.7.8
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EC Tree
IUBMB Comments
Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
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This record set is specific for:
Thermococcus kodakarensis
UNIPROT: O07835 not found.
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Word Map
The taxonomic range for the selected organisms is: Thermococcus kodakarensis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
indolepyruvate ferredoxin oxidoreductase, phenylpyruvate oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-(indol-3-yl)pyruvate synthase (ferredoxin)
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-
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arylpyruvate-ferredoxin oxidoreductase
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-
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hydroxyphenylpyruvate oxidase
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indolepyruvate oxidase
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IOR
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phenylpyruvate oxidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidative decarboxylation
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-
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating)
Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
CAS REGISTRY NUMBER
COMMENTARY hide
158886-06-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
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-
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r
indolepyruvate + CoA + oxidized methylviologen
indoleacetyl-CoA + CO2 + reduced methylviologen
show the reaction diagram
-
-
-
-
?
p-hydroxyphenylpyruvate + CoA + oxidized ferredoxin
p-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
-
-
-
-
r
phenylpyruvate + CoA + oxidized ferredoxin
phenylacetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(indol-3-yl)pyruvate + CoA + oxidized ferredoxin
S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin
show the reaction diagram
-
-
-
-
r
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
192000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
half-life in presence of air is 15 min at 25°C
644701
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cloning and sequence analysis of the IOR gene, 2 genes iorA and iorB, encoding alpha and beta subunits are tandemly arranged, KOD1-IOR overproduced in anaerobically incubated Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Siddiqui, M.A.; Fujiwara, S.; Imanaka, T.
Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. KOD1 possesses a mosaic structure showing features of various oxidoreductases
Mol. Gen. Genet.
254
433-439
1997
Thermococcus kodakarensis, Thermococcus kodakarensis (O07835 and O07836)
Manually annotated by BRENDA team
Siddiqui, M.A.; Fujiwara, S.; Takagi, M.; Imanaka, T.
In vitro heat effect on heterooligomeric subunit assembly of thermostable indolepyruvate ferredoxin oxidoreductase
FEBS Lett.
434
372-376
1998
Pyrococcus furiosus, Thermococcus kodakarensis
Manually annotated by BRENDA team