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Information on EC 7.3.2.4 - ABC-type nitrate transporter

for references in articles please use BRENDA:EC7.3.2.4
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EC Tree
IUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of nitrate, nitrite, and cyanate.
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This record set is specific for:
UNIPROT: Q05085
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Word Map
  • 7.3.2.4
  • shoot
  • seedling
  • low-affinity
  • xenopus
  • auxin
  • dual-affinity
  • nitrate-inducible
  • nitrate-dependent
  • assimilatory
  • root-to-shoot
  • remobilization
  • transceptor
  • hydroponic
  • nitrate-responsive
  • nh4no3
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
+
nitrate-[nitrate-binding protein][side 1]
=
+
+
+
[nitrate-binding protein][side 1]
Synonyms
nitrate transporter, nrt1.1, nrt2.1, atnrt2.1, nark2, nrt1.5, nrt2.5, nrt2.4, nitrate/nitrite transporter, nrt1.8, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nitrate transporter
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ABC-type nitrate/nitrite transporter
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-
-
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nitrate-transporting ATPase
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-
-
-
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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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, nitrate-importing)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of nitrate, nitrite, and cyanate.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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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
ATP + H2O + nitrate/out
ADP + phosphate + nitrate/in
show the reaction diagram
-
-
-
?
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
ATP + H2O + nitrate/out
ADP + phosphate + nitrate/in
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PTR7_ARATH
590
0
64922
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the mode of action ofNRT1.1 is controlled by phosphorylation of a key residue Thr101
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
hanging drop vapor diffusion method, using 100 mM sodium acetate, pH 4.5, 30% PEG300 and 3% (w/v) 2-methyl-2,4-pentanediol
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H356A
the mutation results in complete loss of nitrate binding ability
T101D
the variant shows increased nitrate uptake of approximately 2.8fold compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in High Five insect cells
expressed in Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Parker, J.L.; Newstead, S.
Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1
Nature
507
68-72
2014
Arabidopsis thaliana (Q05085), Arabidopsis thaliana
Manually annotated by BRENDA team
Sun, J.; Bankston, J.R.; Payandeh, J.; Hinds, T.R.; Zagotta, W.N.; Zheng, N.
Crystal structure of the plant dual-affinity nitrate transporter NRT1.1
Nature
507
73-77
2014
Arabidopsis thaliana (Q05085)
Manually annotated by BRENDA team