Information on EC 1.5.1.39 - FMN reductase [NAD(P)H]

for references in articles please use BRENDA:EC1.5.1.39
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.39
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RECOMMENDED NAME
GeneOntology No.
FMN reductase [NAD(P)H]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
FMNH2 + NAD(P)+ = FMN + NAD(P)H + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
5,6-dimethylbenzimidazole biosynthesis I (aerobic)
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bacterial bioluminescence
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vitamin B12 metabolism
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Riboflavin metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
FMNH2:NAD(P)+ oxidoreductase
Contains FMN. The enzyme can utilize NADH and NADPH with similar reaction rates. Different from EC 1.5.1.42, FMN reductase (NADH) and EC 1.5.1.38, FMN reductase (NADPH). The luminescent bacterium Vibrio harveyi possesses all three enzymes [1]. Also reduces riboflavin and FAD, but more slowly.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a non-infectious strain
UniProt
Manually annotated by BRENDA team
a non-infectious strain
UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FMNH2 + NAD(P)+
FMN + NAD(P)H + H+
show the reaction diagram
FMNH2 + NAD+
FMN + NADH + H+
show the reaction diagram
FMNH2 + NADP+
FMN + NADPH + H+
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
FMNH2 + NAD(P)+
FMN + NAD(P)H + H+
show the reaction diagram
FMNH2 + NAD+
FMN + NADH + H+
show the reaction diagram
FMNH2 + NADP+
FMN + NADPH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
the enzyme has a hemin binding activity, pronbably in the hydrophobic pocket near loops beta4-alpha5 and beta8-beta9, docking of biliverdin IXalpha and FMN , overview
additional information
enzyme ChuY binds nucleotides as cofactors., cofactor binding structure, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, using 0.1 M Bis-Tris, pH 6.5, 50 mM CaCl2, and 30% PEG MME 550 as precipitants, ChuY crystals belong to the primitive monoclinic space group P21 with two molecules forming an asymmetric unit, multi-wavelength anomalous dispersion, using a SeMet-labeled crystal at a resolution of 2.4 A
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by metal affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene chuY, encoded in the chu gene cluster of strain CFT073, recombinant expression as His-tagged enzyme in Escherichia coli, complementation of an Escherichia coli chuY-knockout strain with expression of the wild-type gene
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
Show AA Sequence (519 entries)
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