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Information on EC 1.6.3.1 - NAD(P)H oxidase (H2O2-forming) and Organism(s) Arabidopsis thaliana and UniProt Accession Q9FIJ0

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EC Tree
     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.3 With oxygen as acceptor
                1.6.3.1 NAD(P)H oxidase (H2O2-forming)
IUBMB Comments
Requires FAD, heme and calcium. When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalysed biosynthesis of thyroid hormones.
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Arabidopsis thaliana
UNIPROT: Q9FIJ0
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nad(p)h oxidase, p47phox, gp91phox, nadph-oxidase, p67phox, duox2, duox1, nadph oxidase 4, phagocyte nadph oxidase, nadph oxidase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AtrbohD NADPH oxidase
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-
AtrbohF NADPH oxidase
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-
dual oxidase
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-
-
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Duox
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-
-
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large NOX
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-
-
-
LNOX
-
-
-
-
NADPH oxidase
p138 thyroid-oxidase
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-
-
-
p138tox
-
-
-
-
ThOX
-
-
-
-
ThOX2
-
-
-
-
thyroid NADPH oxidase
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-
-
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thyroid oxidase
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-
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thyroid oxidase 2
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
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reduction
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-
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-
SYSTEMATIC NAME
IUBMB Comments
NAD(P)H:oxygen oxidoreductase (H2O2-forming)
Requires FAD, heme and calcium. When calcium is present, this transmembrane glycoprotein generates H2O2 by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen. The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups. This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H2O2 for the thyroid peroxidase-catalysed biosynthesis of thyroid hormones.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-22-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
-
-
-
-
?
NADPH + H+ + O2
NADP+ + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
lignin deposition induced by cellulose biosynthesis inhibition is regulated by JAR1-1 and NADPH oxidase-dependent signalling processes
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-
?
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
NADH + H+ + O2
NAD+ + H2O2
show the reaction diagram
-
-
-
-
?
NADPH + H+ + O2
NADP+ + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
lignin deposition induced by cellulose biosynthesis inhibition is regulated by JAR1-1 and NADPH oxidase-dependent signalling processes
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphenylene iodinium
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inhibition of NAD(P)H oxidase, causes wild-type plants to phenocopy the isoform rdh2/Atrbohc mutant
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
calyculin
isoform RbohD is directly phosphorylated in vivo. Phophorylation is enhanced in presence of protein phosphatase inhibitor calyculin. Calyculin itself induces reactive oxygen species production and dramatically enhances the ionomycin-induced reactive oxygen species production of isoform RbohD
ionomycin
reactive oxygen species production by isoform RbohD is induced in presence of ionomycin. Ionomycin induces calcium influx into the cell, and following Ca2+ binding to the EF-hand motif of RbohD, conformational changes result in activation
SRC2 protein
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enhances the reactive oxygen species-producing activity of NADPH oxidase RbohF
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform RbohD
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the plant hormone abscisic acid triggers production of reactive oxygen species in guard cells via the AtrbohD and AtrbohF NADPH oxidases, leading to stomatal closure. The ABA-activated SnRK2 protein kinase open stomata 1 (OST1) regulates AtrbohF activity
Manually annotated by BRENDA team
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root hair bulge
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RBOHD_ARATH
921
0
103909
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 111000, FLAG-tagged enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
isoform RbohD is directly phosphorylated in vivo. Phophorylation is enhanced in presence of protein phosphatase inhibitor calyculin
phosphoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S174A
-
substitution of Ser174 to Ala results in about 40% reduction in the phosphorylation of AtrbohF by SnRK2 protein kinase open stomata 1 (OST1)
additional information
-
mutants lacking the activity of isoform rdh2/Atrbohc exhibit an impaired root epidermal cell wall, and mutant root hair bulges burst more than wild-type when challegned in situ with hypo-osmotic low ionic strength medium
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ogasawara, Y.; Kaya, H.; Hiraoka, G.; Yumoto, F.; Kimura, S.; Kadota, Y.; Hishinuma, H.; Senzaki, E.; Yamagoe, S.; Nagata, K.; Nara, M.; Suzuki, K.; Tanokura, M.; Kuchitsu, K.
Synergistic activation of the Arabidopsis NADPH oxidase AtrbohD by Ca2+ and phosphorylation
J. Biol. Chem.
283
8885-8892
2008
Arabidopsis thaliana (Q9FIJ0), Arabidopsis thaliana
Manually annotated by BRENDA team
Macpherson, N.; Takeda, S.; Shang, Z.; Dark, A.; Mortimer, J.C.; Brownlee, C.; Dolan, L.; Davies, J.M.
NADPH oxidase involvement in cellular integrity
Planta
227
1415-1418
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Hamann, T.; Bennett, M.; Mansfield, J.; Somerville, C.
Identification of cell-wall stress as a hexose-dependent and osmosensitive regulator of plant responses
Plant J.
57
1015-1026
2009
Arabidopsis thaliana
Manually annotated by BRENDA team
Sirichandra, C.; Gu, D.; Hu, H.C.; Davanture, M.; Lee, S.; Djaoui, M.; Valot, B.; Zivy, M.; Leung, J.; Merlot, S.; Kwak, J.M.
Phosphorylation of the Arabidopsis AtrbohF NADPH oxidase by OST1 protein kinase
FEBS Lett.
583
2982-2986
2009
Arabidopsis thaliana
Manually annotated by BRENDA team
Kawarazaki, T.; Kimura, S.; Iizuka, A.; Hanamata, S.; Nibori, H.; Michikawa, M.; Imai, A.; Abe, M.; Kaya, H.; Kuchitsu, K.
A low temperature-inducible protein AtSRC2 enhances the ROS-producing activity of NADPH oxidase AtRbohF
Biochim. Biophys. Acta
1833
2775-2780
2013
Arabidopsis thaliana
Manually annotated by BRENDA team