Information on EC 3.6.3.26 - nitrate-transporting ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.6.3.26
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RECOMMENDED NAME
GeneOntology No.
nitrate-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + nitrate/out = ADP + phosphate + nitrate/in
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
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transmembrane transport
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (nitrate-importing)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports NO3-, NO2- and OCN-.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
treatments with the ethylene precursor, aminocyclopropane carboxylic acid and the ethylene biosynthesis inhibitor, aminoethoxyvinylglycine are found to affect nitrate uptake
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-
Manually annotated by BRENDA team
ssp. chinensis Makino, cultivar Suzhouqing, gene BcNRT1
UniProt
Manually annotated by BRENDA team
Chlamydomonas sp.
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-
-
Manually annotated by BRENDA team
gene nrt2
UniProt
Manually annotated by BRENDA team
gene nrt2
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
gene nrt2
UniProt
Manually annotated by BRENDA team
gene nrt2
UniProt
Manually annotated by BRENDA team
strain M5a1
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-
Manually annotated by BRENDA team
strain M5a1
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-
Manually annotated by BRENDA team
gene Medtr5g093170.1
UniProt
Manually annotated by BRENDA team
gene Medtr5g093170.1
UniProt
Manually annotated by BRENDA team
cv. Gatersleben, boron is found to affect nitrate uptake, boron deficiency causes decrease in nitrate uptake
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-
Manually annotated by BRENDA team
strain ATCC 29133, mutant UCD425
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Manually annotated by BRENDA team
different strains which are derivatives of the NCYC495 leu2 ura3 strain, enzyme is highly expressed in media containing nitrate as sole nitrogen source, addition of glutamine or ammonium decreased nitrate uptake and enzyme level
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Manually annotated by BRENDA team
strain PAO1, wild type and deletion mutants, NarK1 deletion does not affect nitrate uptake while NarK2 deletion causes strongly reduced nitrate uptake rates
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-
Manually annotated by BRENDA team
strain PCC7942, ABC-type bispecific nitrate/nitrite transporter is encoded by the four genes nrtA, -B, -C, and -D
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-
Manually annotated by BRENDA team
PCC6301
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
cultivar Recital
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + abscisic acid/out
ADP + phosphate + abscisic acid/in
show the reaction diagram
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-
-
-
?
ATP + H2O + nitrate/out
ADP + phosphate + nitrate/in
show the reaction diagram
ATP + H2O + nitrite/out
ADP + phosphate + nitrite/in
show the reaction diagram
ATP + H2O + NO2-/out
ADP + phosphate + NO2-/in
show the reaction diagram
ATP + H2O + NO3-/out
ADP + phosphate + NO3-/in
show the reaction diagram
additional information
?
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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
ATP + H2O + nitrate/out
ADP + phosphate + nitrate/in
show the reaction diagram
ATP + H2O + nitrite/out
ADP + phosphate + nitrite/in
show the reaction diagram
ATP + H2O + NO3-/out
ADP + phosphate + NO3-/in
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
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the nrt1.8-1 mutant shows a nitrate-dependent Cd2+-sensitive phenotype, while wild-type NRT1.8 is upregulated by Cd2+ stress
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cd2+
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the nrt1.8-1 mutant shows a nitrate-dependent Cd2+-sensitive phenotype
Cyanate
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competitively inhibits nitrite transport
NH4+
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the C-terminal domain of NrtC is involved in the ammonium-promoted inhibition of the nitrate/nitrite transporter
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAR2
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additional information
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the nrt1.8-1 mutant shows a nitrate-dependent Cd2+-sensitive phenotype, and nitrate transport by NRT1.8 is pH-dependent
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
nitrate
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about
0.0416 - 3.1
nitrate/out
0.001
nitrite
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about
additional information
additional information
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uptake kinetics of recombinant NRT1.9 in NRT1.9-injected oocytes, pH 5.5
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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recombinant NRT1.9 in frog oocytes, transport assay at
8.2 - 9.6
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assay at, medium pH
additional information
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nitrate transport by NRT1.8 is pH-dependent
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6
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truncated soluble form of NrtA at pH 5.5
5.1 - 5.9
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His-tagged NrtA1 at pH 5.5
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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histochemical analysis shows that NRT1.8 is expressed predominantly in xylem parenchyma cells within the vasculature
Manually annotated by BRENDA team
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highly expressed in dry seeds, especially at the end of seed maturation, weak expression in the surrounding endosperm
Manually annotated by BRENDA team
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histochemical analysis shows that NRT1.8 is expressed predominantly in xylem parenchyma cells within the vasculature
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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vacuole membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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2 * 48000, AtNRT2.1, SDS-PAGE, + 2 * 26000, myc-tagged AtNAR2.1, SDS-PAGE, the functional unit for high-affinity nitrate influx may be a tetramer consisting of two subunits each of AtNRT2.1 and AtNAR2.1
38000
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truncated NrtA, gel filtration
38770
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calculated from deduced amino acid sequence
38890
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His-tagged NrtA1, MALDI-TOF
40000
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x * 40000, diffuse signal, SDS-PAGE
45000
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His-tagged NrtA1, silver staining and immunoblotting of two-dimensional gel electrophoresis
47300
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x * 47300, NarK1, calculated from the deduced amino acid sequence
48000
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2 * 48000, AtNRT2.1, SDS-PAGE, + 2 * 26000, myc-tagged AtNAR2.1, SDS-PAGE, the functional unit for high-affinity nitrate influx may be a tetramer consisting of two subunits each of AtNRT2.1 and AtNAR2.1
50000
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x * 50000, SDS-PAGE
50600
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x * 50600, NarK2, calculated from the deduced amino acid sequence
57000
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x * 57000, calculated from the deduced amino acid sequence
61099
x * 61099, calculated from the deduced amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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x-ray crystallography
monomer
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1 * 38000, gel filtration
tetramer
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2 * 48000, AtNRT2.1, SDS-PAGE, + 2 * 26000, myc-tagged AtNAR2.1, SDS-PAGE, the functional unit for high-affinity nitrate influx may be a tetramer consisting of two subunits each of AtNRT2.1 and AtNAR2.1
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
additional information
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nitrogen sources trigger Ynt1 ubiquitinylation, Ynt1 becomes modified with ubiquitin during down-regulation as a result of nitrate assimilation or the shift to a preferred nitrogen source
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo and nitrate-bound enzyme, hanging drop vapor diffusion method, using 22% (w/v) PEG 400, 0.05 M sodium citrate pH 4.5, 0.07 M sodium chloride and 1.5% (w/v) PEG 600
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hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 4.5, 30% PEG300 and 3% (w/v) 2-methyl-2,4-pentanediol
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hanging drop vapor diffusion method
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
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Ni2+-chelating Sepharose fast-flow column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a fusion protein between a 2-kb fragment of the ATNRT2.7 promoter and either the beta-glucuronidase or green fluorescent protein reporter gene stably introduced into the Arabidopsis thaliana ecotype Wassilewskija; expressed as GFP-fusion protein using Agrobacterium tumefaciens, correct localization; Xenopus laevis oocytes are injected with nuclease-free water or ATNRT2.7 mRNA, ATNRT2.7 mRNA-injected oocytes take up significantly more nitrate than water-injected controls
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ansient expression of the NRT1.8:enhanced green fluorescent protein fusion in onion epidermal cells and Arabidopsis protoplasts
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expressed as GUS-fusion protein in Arabidopsis thaliana
expressed in cells the nrtABCD deletion mutant NA3 of Synechococcus elongatus which restores the ability of the cell to grow on nitrate as sole nitrogen source
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expressed in cultivar Oryza sativa japonica
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expressed in Escherichia coli
expressed in Escherichia coli strain M15
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expressed in High Five insect cells
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expressed in Lactococcus lactis
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expressed in Saccharomyces cerevisiae
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expressed in Xenopus laevis oocytes
expressed in Xenopus spp. oocytes
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expression of the pNRT2.1::LUC reporter gene construct in transgenic Arabidopsis thaliana plants, genotyping, overview
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gene BcNRT1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Brassica campestris mesophyll protoplasts from pEarleyGate101 and pEarleyGate104 vectors or the cauliflower mosaic virus 35S promoter using the BcNRT1 promoter for analysis of subcellular localization by YFP fluorescence labeling, expression analysis by quantitative RT-PCR
gene Medtr5g093170.1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of NRT1.3 in Xenopus laevis oocytes
gene nrt2, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis
gene nrt2, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis; gene nrt2, DNA and amino acid sequence determination and analysis, detailed phylogenetic analysis
heterologous expression of NRT2.4 in Xenopus laevis oocytes
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mutants and GFP-fusion protein, GFP-fusion protein is active and correctly localized
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narK gene expressed in NarK2 and NarK1/NarK2 deletion mutants of Pseudomonas aeruginosa PAO1, narK gene expression is capable of restoring the anaerobic growth of Pseudomonas aeruginosa PAO1, although at reduced rates compared with the wild type
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the nitrite transporting system is encoded by the four genes nrtA, -B, -C, and -D, organized in the CynABD operon genes, physical map of the cynABDS genomic region
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transient expression of GFP-NRT1.9 fusion protein in Arabidopsis thaliana mesophyll protoplasts using the CMV 35S promoter
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truncated NrtA protein lacking the N-terminal 81 amino acids, expressed in Escherichia coli cells as a histidine-tagged soluble protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is downregulated by iron deficiency
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enzyme expression is downregulated by nitrogen deficiency
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enzyme expression is induced under nitrogen starvation
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enzyme expression is strongly influenced by plant nitrogen status at flowering during the first 300-400 degree-days after flowering
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ex-pression of CHL1 (NRT1.1), NRT1.2, NRT2.1, NRT2.2, and/or NRT2.4 is regulated at the transcriptional level by nitrate, nitrite, ammonium, glutamine, N starvation, light, sucrose, diurnal rhythm, and/or pH
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gene expression of Nrt2.1 and Nrt2.3 is repressed by NH4+
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gene expression of Nrt2.1 and Nrt2.3 is strongly induced by low NO3- concentration
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in response to salt stress (24 h treatment with 100 mM Na+), the expression of the root stele NO-3 transporter gene NPF2.3 is maintained
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in roots, enzyme expression can be decreased by 79% by potassium deficiency
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in roots, enzyme expression can be increased by 33% by supply of high nitrate (2.5 mM)
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mRNA level of NRT1.5 is down-regulated by salt, drought as well as cadmium treatments
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MtNRT1.3 is environmentally downregulated by the addition of NO3- to the roots
MtNRT1.3 is environmentally upregulated by the absence of NO3-, not as a result of a systemic signalling of plant N status
NPF6.8 expression is insensitive to auxin
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NPF6.8 expression is stimulated by abscisic acid
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NRT1.8 is upregulated by nitrate. NRT1.8 is the only nitrate assimilatory pathway gene that is strongly upregulated by Cd2+ stress in roots
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NRT2.1 transgenic Arabidopsis and Nicotiana reveal post-transcriptional repression of nitrate uptake in response to ammonium or dark treatments. In wild type, both the AtNRT2.1 mRNA level and the HATS are downregulated by prolonged dark. In the Arabidopsis 35S-NRT2.1 plant, the mRNA level remains unchanged in response to prolonged dark, but the HATS and NRT2.1 protein levels are reduced. cadmium treatment reduces the activity of NRT1.8 in the shoot
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NRT2.4 expression is induced by nitrate
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transporters NRT1.6, NRT1.7, NRT2.1, and NRT2.4 are inducible by nitrate. In wild type, expression of NRT1.8 is upregulated by cadmium
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H356A
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the mutation results in complete loss of nitrate binding ability
T101A
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inactivation of the high-affinity component of the transporter by preventing phosphorylation at Thr101
T101D
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the variant shows increased nitrate uptake of approximately 2.8fold compared to the wild type enzyme
F145A
the mutant displays binding to both nitrate and nitrite
F265A
the mutant retains very weak binding to nitrate but not to nitrite
F367A
the mutation abrogates binding to both nitrate and nitrite
F47A
the mutation abrogates binding to both nitrate and nitrite
N173A
the mutant retains some binding to substrate, albeit drastically reduced in comparison to the wild type
R303A
the mutation completely abrogates binding to nitrate or nitrite
R87A
the mutation completely abrogates binding to nitrate or nitrite
W50A
the mutation abrogates binding to both nitrate and nitrite
Y261A,
the mutation completely abrogates binding to nitrate or nitrite
A145G
the mutant shows wild type activity
A92G
the mutant shows wild type activity
C309S
the mutant shows wild type activity
C378S
the mutant shows wild type activity
D267G
the mutant shows reduced activity compared to the wild type enzyme
F114S
the mutant shows reduced activity compared to the wild type enzyme
F19S
the mutant shows reduced activity compared to the wild type enzyme
G140S
the mutant shows reduced activity compared to the wild type enzyme
G315S
the mutant shows reduced activity compared to the wild type enzyme
G69S
the mutant shows reduced activity compared to the wild type enzyme
G70P
the mutant shows wild type activity
G89S
the mutant shows wild type activity
I118L
the mutant shows wild type activity
L8V
the mutant shows wild type activity
P50S
the mutant shows reduced activity compared to the wild type enzyme
P84T
the mutant shows reduced activity compared to the wild type enzyme
R129S
the mutant shows wild type activity
T78S
the mutant shows wild type activity
Y97S
the mutant shows wild type activity
C309S
-
the mutant shows wild type activity
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G140S
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the mutant shows reduced activity compared to the wild type enzyme
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G69S
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the mutant shows reduced activity compared to the wild type enzyme
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T78S
-
the mutant shows wild type activity
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DELTA232-286
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enzyme does not disappear in response to glutamine
K243R
-
no effect on down-regulation by glutamine
K243R/K253R
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reduced down-regulation in response to glutamine
K243R/K253R/K270R
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no ubiquitinylation, strongly reduced down-regulation in response to glutamine
K253R
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reduced down-regulation in response to glutamine
K253R/K270R
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reduced down-regulation in response to glutamine
K270R
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reduced down-regulation in response to glutamine
additional information