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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + arsenate/out
ADP + phosphate + arsenate/in
ATP + H2O + phosphate-[phosphate-binding protein][side 1]
ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
ATP + H2O + tellurite-[phosphate-binding protein][side 1]
ADP + phosphate + tellurite[side 2] + [phosphate-binding protein][side 1]
Substrates: -
Products: -
?
CTP + H2O + phosphate/out
CDP + phosphate + phosphate/in
GTP + H2O + phosphate/out
GDP + phosphate + phosphate/in
additional information
?
-
ATP + H2O + arsenate/out

ADP + phosphate + arsenate/in
Substrates: the enzyme has about 150fold lower affinity for arsenate compared to phosphate
Products: -
?
ATP + H2O + arsenate/out
ADP + phosphate + arsenate/in
-
Substrates: the affinity of Pht1;3 for arsenate is much greater than for phosphate
Products: -
?
ATP + H2O + phosphate-[phosphate-binding protein][side 1]

ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + phosphate-[phosphate-binding protein][side 1]
ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + phosphate-[phosphate-binding protein][side 1]
ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + phosphate/out

ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: ANTR1 functions as a Na+-dependent phosphate transporter
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: phosphate is the preferred substrate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the enzyme performs phosphate uptake energized by ATP hydrolysis
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: ATP-consuming import of phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: as phosphate/proton cotransport mechanism
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: as phosphate/proton cotransport mechanism
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: Pit-1 is required for elevated phosphate-induced osteogenic gene expression in human smooth muscle cells, role of the sodium-dependent phosphate cotransporter, Pit-1, in vascular smooth muscle cell calcification, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: proton-coupled phosphate transport
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the enzyme performs phosphate uptake energized by ATP hydrolysis
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: ATP-consuming import of phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: import of phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the enzyme performs phosphate uptake energized by ATP hydrolysis
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: conformational and structural changes upon nucleotide binding analysis, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: ATP-consuming import of phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: involved in promoting drug efflux in the CIPr clone
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: involved in phosphate transport
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: confers high levels of fluoroquinolone resistance in ciproflavin resistant colony CIPr
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the organism possesses two different high-affinity phosphate ABC transporter systems, the Pst system, with isozymes PstS1 and PstS2, and the Phn system, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the organism possesses two different high-affinity phosphate ABC transporter systems, the Pst system, with isozymes PstS1 and PstS2, and the Phn system, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the enzyme is involved in the phosphate uptake system in the alfalfa symbiont Sinorhizobium meliloti, PhoB has regulatory function, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: PstSCAB is specific for phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the Pst system affects autolysis and transformation, it is most likely involved in a signalling pathway regulating the activity of the major pneumococcal autolysin
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
CTP + H2O + phosphate/out

CDP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
CTP + H2O + phosphate/out
CDP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
GTP + H2O + phosphate/out

GDP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
GTP + H2O + phosphate/out
GDP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
additional information

?
-
-
Substrates: the enzyme plays an important role in phosphate acquisition and remobilization in plants, its activity is regulated by the phosphate transporter traffic facilitator 1, PHF1, enabling the endoplasmic reticulum exit of the enzyme, mechanism, phf1-deficient phenotypes, overview
Products: -
?
additional information
?
-
-
Substrates: the enzyme binds to phosphate transporter traffic facilitator 1, PHF1, a SEC12-related plant-specific protein
Products: -
?
additional information
?
-
-
Substrates: the exceptional toxicity of arsenate, As(V), is derived from its close chemical similarity to phosphate, which allows the metalloid to be easily incorporated into plant cells through the high-affinity Pi transport system
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
-
Substrates: ALIX protein regulates vacuolar degradation of enzyme variant PHT1;1
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
-
Substrates: sodium-hydrogen exchanger regulatory factor-1 (NHERF-1) interacts with C-terminal end of sodium-dependent phosphate transporter 2a
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
Substrates: HvPHT1;1 shows preferential selectivity for phosphate and arsenate, but no transport of the other oxyanions SO42- and NO3-
Products: -
?
additional information
?
-
-
Substrates: HvPHT1;1 shows preferential selectivity for phosphate and arsenate, but no transport of the other oxyanions SO42- and NO3-
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
Substrates: protein SLC25A3 transports both copper and phosphate
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
-
Substrates: the high-affinity phosphate transporter Pst is a virulence factor for Proteus mirabilis during complicated urinary tract infection, overview
Products: -
?
additional information
?
-
-
Substrates: the organism requires a functional phosphate import system for infection of hosts via the urinary tract, Pst negatively regulates biofilm formation and pathogenesis. The mutants show an altered proteome compared to the wild-type cells
Products: -
?
additional information
?
-
-
Substrates: the high-affinity phosphate transporter Pst is a virulence factor for Proteus mirabilis during complicated urinary tract infection, overview
Products: -
?
additional information
?
-
-
Substrates: the organism requires a functional phosphate import system for infection of hosts via the urinary tract, Pst negatively regulates biofilm formation and pathogenesis. The mutants show an altered proteome compared to the wild-type cells
Products: -
?
additional information
?
-
-
Substrates: the phosphate transporter PiT-2 is involved in developmental regulation in renal tubules
Products: -
?
additional information
?
-
-
Substrates: N-terminal SPX domain of Pho90 interacts physically with regulatory protein Spl2
Products: -
?
additional information
?
-
-
Substrates: Spl2 interacts with the N-terminal SPX domain of Pho87 and Pho90
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
-
Substrates: Spl2 interacts with the N-terminal SPX domain of Pho87 and Pho90
Products: -
?
additional information
?
-
Substrates: PT4 is invlved in nutrient supply by mycorrhiza and mycorrhiza-specific phosphate transport in Solanaceae plants, regulation, overview, comparison to other Pht1 family phosphate transporters in mycorrhizal Pi transport
Products: -
?
additional information
?
-
-
Substrates: PT4 is invlved in nutrient supply by mycorrhiza and mycorrhiza-specific phosphate transport in Solanaceae plants, regulation, overview, comparison to other Pht1 family phosphate transporters in mycorrhizal Pi transport
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
Substrates: PT4 is invlved in nutrient supply by mycorrhiza and mycorrhiza-specific phosphate transport in Solanaceae plants, regulation, overview, comparison to other Pht1 family phosphate transporters in mycorrhizal Pi transport
Products: -
?
additional information
?
-
-
Substrates: PT4 is invlved in nutrient supply by mycorrhiza and mycorrhiza-specific phosphate transport in Solanaceae plants, regulation, overview, comparison to other Pht1 family phosphate transporters in mycorrhizal Pi transport
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
-
Substrates: PstS is involved in penicillin resistance of Streptococcus pneumoniae
Products: -
?
additional information
?
-
Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
Products: -
?
additional information
?
-
Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
Products: -
?
additional information
?
-
Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
Products: -
?
additional information
?
-
Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
Products: -
?
additional information
?
-
Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
Products: -
?
additional information
?
-
Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + phosphate-[phosphate-binding protein][side 1]
ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
additional information
?
-
ATP + H2O + phosphate-[phosphate-binding protein][side 1]

ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + phosphate-[phosphate-binding protein][side 1]
ADP + phosphate + phosphate[side 2] + [phosphate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out

ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: ANTR1 functions as a Na+-dependent phosphate transporter
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the enzyme performs phosphate uptake energized by ATP hydrolysis
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: ATP-consuming import of phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: as phosphate/proton cotransport mechanism
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: as phosphate/proton cotransport mechanism
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: Pit-1 is required for elevated phosphate-induced osteogenic gene expression in human smooth muscle cells, role of the sodium-dependent phosphate cotransporter, Pit-1, in vascular smooth muscle cell calcification, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: proton-coupled phosphate transport
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the enzyme performs phosphate uptake energized by ATP hydrolysis
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: ATP-consuming import of phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: import of phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the enzyme performs phosphate uptake energized by ATP hydrolysis
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: ATP-consuming import of phosphate
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: involved in promoting drug efflux in the CIPr clone
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: involved in phosphate transport
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: confers high levels of fluoroquinolone resistance in ciproflavin resistant colony CIPr
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the organism possesses two different high-affinity phosphate ABC transporter systems, the Pst system, with isozymes PstS1 and PstS2, and the Phn system, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the organism possesses two different high-affinity phosphate ABC transporter systems, the Pst system, with isozymes PstS1 and PstS2, and the Phn system, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the enzyme is involved in the phosphate uptake system in the alfalfa symbiont Sinorhizobium meliloti, PhoB has regulatory function, overview
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: -
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
-
Substrates: the Pst system affects autolysis and transformation, it is most likely involved in a signalling pathway regulating the activity of the major pneumococcal autolysin
Products: -
?
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
Substrates: -
Products: -
?
additional information

?
-
-
Substrates: the enzyme plays an important role in phosphate acquisition and remobilization in plants, its activity is regulated by the phosphate transporter traffic facilitator 1, PHF1, enabling the endoplasmic reticulum exit of the enzyme, mechanism, phf1-deficient phenotypes, overview
Products: -
?
additional information
?
-
-
Substrates: the exceptional toxicity of arsenate, As(V), is derived from its close chemical similarity to phosphate, which allows the metalloid to be easily incorporated into plant cells through the high-affinity Pi transport system
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
-
Substrates: co-existence of a high and a low affinity system
Products: -
?
additional information
?
-
-
Substrates: sodium-hydrogen exchanger regulatory factor-1 (NHERF-1) interacts with C-terminal end of sodium-dependent phosphate transporter 2a
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Substrates: co-existence of a high and a low affinity system
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Substrates: co-existence of a high and a low affinity system
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Substrates: co-existence of a high and a low affinity system
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Substrates: co-existence of a high and a low affinity system
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Substrates: the high-affinity phosphate transporter Pst is a virulence factor for Proteus mirabilis during complicated urinary tract infection, overview
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Substrates: the organism requires a functional phosphate import system for infection of hosts via the urinary tract, Pst negatively regulates biofilm formation and pathogenesis. The mutants show an altered proteome compared to the wild-type cells
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Substrates: the high-affinity phosphate transporter Pst is a virulence factor for Proteus mirabilis during complicated urinary tract infection, overview
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Substrates: the organism requires a functional phosphate import system for infection of hosts via the urinary tract, Pst negatively regulates biofilm formation and pathogenesis. The mutants show an altered proteome compared to the wild-type cells
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Substrates: the phosphate transporter PiT-2 is involved in developmental regulation in renal tubules
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Substrates: N-terminal SPX domain of Pho90 interacts physically with regulatory protein Spl2
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Substrates: Spl2 interacts with the N-terminal SPX domain of Pho87 and Pho90
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Substrates: co-existence of a high and a low affinity system
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Substrates: Spl2 interacts with the N-terminal SPX domain of Pho87 and Pho90
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Substrates: PT4 is invlved in nutrient supply by mycorrhiza and mycorrhiza-specific phosphate transport in Solanaceae plants, regulation, overview, comparison to other Pht1 family phosphate transporters in mycorrhizal Pi transport
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Substrates: PT4 is invlved in nutrient supply by mycorrhiza and mycorrhiza-specific phosphate transport in Solanaceae plants, regulation, overview, comparison to other Pht1 family phosphate transporters in mycorrhizal Pi transport
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Substrates: co-existence of a high and a low affinity system
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additional information
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Substrates: PT4 is invlved in nutrient supply by mycorrhiza and mycorrhiza-specific phosphate transport in Solanaceae plants, regulation, overview, comparison to other Pht1 family phosphate transporters in mycorrhizal Pi transport
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Substrates: PT4 is invlved in nutrient supply by mycorrhiza and mycorrhiza-specific phosphate transport in Solanaceae plants, regulation, overview, comparison to other Pht1 family phosphate transporters in mycorrhizal Pi transport
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Substrates: co-existence of a high and a low affinity system
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Substrates: PstS is involved in penicillin resistance of Streptococcus pneumoniae
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Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
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Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
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additional information
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Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
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additional information
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Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
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additional information
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Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
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additional information
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Substrates: differential regulation of the five gene encoding Pht1 phosphate transporters in Zea mays, involvement of the encoded proteins in diverse processes, including phosphate uptake from soil and transport at the symbiotic interface in mycorrhizas, phosphate (re)translocation in the shoot, and phosphate uptake during pollen tube growth, overview
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evolution

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OsPT1 belongs to the Pht1 family, like OsPT8 and OsPT4
evolution
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the enzyme belongs to the PHT1 transporters family, comparison of plant PHT1 multigenic families, overview
evolution
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the enzyme belongs to the PHT1 transporters family
evolution
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the enzyme belongs to the PHT1 transporters family
evolution
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the enzyme belongs to the PHT1 transporters family
evolution
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the enzyme belongs to the PHT1 transporters family, comparison of plant PHT1 multigenic families, overview
evolution
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the enzyme belongs to the PHT1 transporters family, comparison of plant PHT1 multigenic families, overview
evolution
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the enzyme belongs to the PHT1 transporters family, comparison of plant PHT1 multigenic families, overview
evolution
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the enzyme belongs to the PHT1 transporters family, comparison of plant PHT1 multigenic families, overview
evolution
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the enzyme belongs to the PHT1 transporters family, comparison of plant PHT1 multigenic families, overview
evolution
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8 PHT1 family genes have been identified from the potato genome
evolution
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a total of 28 phosphate transporter isoforms are identified, belonging to the PHT1, PHT2, PHT3, CaPHT4, PHT5 and PHO family
evolution
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phosphate tranbsporter family PHT4 can be classified into six distinct groups. PHT4:1 to PHT4:4 are targeted to chloroplasts, and PHT4:6-1 and PHT4:6-2 are located to Golgi apparatus. PHT4 proteins can mediate inorganic phosphate transport in yeast. They display different expression profiles in response to phosphate starvation, salicylic acid, abscisic acid and salt stress treatments. PHT4 proteins are involved in phosphate distribution between the cytoplasm and chloroplast or Golgi apparatus and also involved in stress responses
evolution
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phosphate tranbsporter family PHT4 can be classified into six distinct groups. PHT4:1 to PHT4:4 are targeted to chloroplasts, and PHT4:6-1 and PHT4:6-2 are located to Golgi apparatus. PHT4 proteins can mediate inorganic phosphate transport in yeast. They display different expression profiles in response to phosphate starvation, salicylic acid, abscisic acid and salt stress treatments. PHT4 proteins are involved in phosphate distribution between the cytoplasm and chloroplast or Golgi apparatus and also involved in stress responses
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malfunction

knockdown transformants of the gene are prepared using electroporation and RNAinterference. Knockdown transformants transport a significantly lower amount of phosphate to the host plant than wild-type. Higher amounts of phosphate are found in plants colonized with wild-type than that of non-colonized and plants colonized with knockdown PiPT
malfunction
selenite uptake is reduced in a DELTA pho84 mutant
malfunction
a triple mutant consisting of deleted low-affinity transporters Pho87, Pho90 and Pho91 is slightly more sensitive to selenite than the wild-type strain. Single mutants do not show any difference to the wild-type stain
malfunction
a triple mutant consisting of deleted low-affinity transporters Pho87, Pho90 and Pho91 is slightly more sensitive to selenite than the wild-type strain. Single mutants do not show any difference to the wild-type strain
malfunction
two independent T-DNA insertion lines from the SALK collection lacking a functional PHT4;2 allele, i.e. pht4;2-1 and pht4;2-2 mutant plants show altered activity and increased biomass due to increased leaf sizes, as well as altered starch accumulation, compared to the wild-type enzyme, phenotypes, overview
malfunction
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over-expression or knockdown of OsPT1 cause altered phosphate concentration and uptake rate and distribution in phosphate-replete rice, as well as Pi uptake-elicited changes in the root cell membrane potential. Changes in expression affects root growth and root hair development
malfunction
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the pho84DELTA strain is unable to rapidly reverse phosphate-starvation responses. Deletion of END3, encoding an essential component for endocytosis, which prevents the internalization of Pho87 and, as a consequence, leads to the stabilization of this phosphate transporter at the plasma membrane under phosphate-starving conditions, endocytosis of Pho90 is only prevented in the mutant strain lacking End3 and not in the strains lacking Pho4 or Spl2
malfunction
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the Arabidopsis accelerated cell death 6-1, acd6-1, mutant shows constitutive defense, cell death, and extreme dwarf phenotype due to a T-DNA disruption in the PHT4;1 gene. The mutant is more susceptible compared to the wild-type to virulent Pseudomonas syringae strains but not to several avirulent strains
malfunction
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null pht1;9 alleles exhibit exacerbated responses to prolonged phosphate limitation and enhanced tolerance to arsenate exposure, whereas Pht1;9 overexpression induces the opposite phenotypes. Strikingly, Pht1;9 ? Pht1;8 silencing lines display more pronounced defects than the pht1;9 mutants
malfunction
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Pht1;5-defective mutants show reduced phosphate allocation to shoots and elevated transcript levels for several phosphate starvation-response genes under low-phosphate conditions, under phosphate-replete conditions, pht1;5-1 has higher shoot phosphate content compared to the wild-type but has reduced phosphate content in roots. Overexpression of Pht1;5 affects the distribution and remobilization of phosphate between source and sink. Constitutive overexpression of Pht1;5 has the opposite effect on phosphate distribution: namely, lower phosphate levels in shoots and higher phosphate content in roots compared to the wild-type. Pht1;5 overexpression also results in altered phosphate remobilization, as evidenced by a greater than 2fold increase in the accumulation of phosphate in siliques, premature senescence, and an increase in transcript levels of genes involved in phosphate scavenging. Furthermore, Pht1;5 overexpressors exhibit increased root hair formation and reduced primary root growth that could be rescued by the application of silver nitrate, an ethylene perception inhibitor, or aminoethoxyvinylglycine, an ethylene biosynthesis inhibitor, respectively. Ethylene signaling in modulating the primary root and root hair phenotypes of Pht1;5 overexpression lines, overview
malfunction
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a phosphorylation-mimicking mutagenesis of PHT1;1 at Ser514 results in its accumulation in the endoplasmic reticulum
malfunction
downregulation of PiT1 severely impairs the proliferation of two transformed human cells lines, HepG2 and HeLa, and the tumorigenicity of HeLa cells in nude mice. An increased PiT1 expression can indeed make NIH3T3 cells more sensitive to transformation. Phenotypes of MC3T3-E1 cells overexpressing hPiT1 or hPiT2, overview
malfunction
PiT1 knock-out mice do not survive past E12.5 and from E10.5, the embryos are growth-retarded and show reduced proliferation of liver cells. Isolated mouse embryonic fibroblasts MC3T3-E1 with knocked out as well as reduced PiT1 expression levels also exhibit impaired proliferation
malfunction
knockdown of isoform PT4 leads to degenerating or dead arbuscule phenotypes
malfunction
knockdown of isoform PT1 leads to degenerating or dead arbuscule phenotypes
malfunction
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although no alterations in phosphate concentration is in isoform PT9 or PT10 knockdown plants, a significant reduction in phosphate concentration in both shoots and roots is observed in double-knockdown plants grown under both high- and low-phosphate conditions
malfunction
enzyme overexpression gives rise to multiple developmental defects including curly leaves with deep color, dwarfed stature, and reduced fertility. MPT3 overexpressing plants also accumulate higher ATP content, faster respiration rate and more reactive oxygen species than wild type plants
malfunction
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the Arabidopsis accelerated cell death 6-1, acd6-1, mutant shows constitutive defense, cell death, and extreme dwarf phenotype due to a T-DNA disruption in the PHT4;1 gene. The mutant is more susceptible compared to the wild-type to virulent Pseudomonas syringae strains but not to several avirulent strains
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malfunction
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null pht1;9 alleles exhibit exacerbated responses to prolonged phosphate limitation and enhanced tolerance to arsenate exposure, whereas Pht1;9 overexpression induces the opposite phenotypes. Strikingly, Pht1;9 ? Pht1;8 silencing lines display more pronounced defects than the pht1;9 mutants
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malfunction
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the pho84DELTA strain is unable to rapidly reverse phosphate-starvation responses. Deletion of END3, encoding an essential component for endocytosis, which prevents the internalization of Pho87 and, as a consequence, leads to the stabilization of this phosphate transporter at the plasma membrane under phosphate-starving conditions, endocytosis of Pho90 is only prevented in the mutant strain lacking End3 and not in the strains lacking Pho4 or Spl2
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metabolism

phosphate transporter mechanism in the plant cell, overview. When the supply of phosphate is limited, plants grow more roots, increase the rate of phosphate uptake by roots from soil solution, retranslocate phosphate from older leaves, and deplete the vacuolar stores of phosphate. There is also significant retranslocation of phosphate in the phloem from older leaves to the growing shoot and from the shoot to the root
metabolism
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upon phosphate starvation, these low-affinity phosphate transporters, e.g. Pho87 and Pho90, are endocytosed and targeted to the vacuole. For Pho87, this process strictly depends on SPL2, another Pho4-dependent gene that encodes a protein known to interact with the N-terminal SPX domain of the transporter
metabolism
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PHT4;1 acts upstream of the SA pathway. PHT4;1 contributes to SID2-dependent and -independent pathways
metabolism
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the enzyme is involved in arbuscular mycorrhizal, AM, symbiosis,. During arbuscular mycorrhizal symbiosis, the AM fungus colonizes the root cortical cells where it forms branched hyphae called arbuscules that function in nutrient exchange with the plant. Each arbuscule is enveloped in a plant membrane, the periarbuscular membrane, that contains a unique set of proteins including phosphate transporters such as MtPT4 that are essential for symbiotic phosphate transport
metabolism
deprotonation of residue D324 triggers phosphate cytosolic release. Multiple proton transfer events proceed during the transition from the open conformation to the inward conformation. The exit path of the D324 proton requires residue D45
metabolism
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the alternating conformations of the PstSCAB transporter are sensed by PhoR and PhoU. The sensory mechanism controls the alternate autokinase and phospho-PhoB phosphatase activities of PhoR, which ultimately control the signaling state of the response regulator PhoB
metabolism
residues D35, D38, R134, and D144 are implicated in H+ transfer across the membrane, and Y312 and N421 are involved in initial interaction and translocation of phosphate, all are essential for transport activity. When phsphate enters the binding pocket, the two aromatic moieties of Y145 and F169 and the hydrogen bonds generated from Q172, W304, Y312, D308, and K449 can build a scaffold to stabilize the structure. Subsequent interaction between phosphate and the positive residue of K449 facilitates its release. Residues D38, D93, R134, D144, D212, R216, R233, D367, K373, and E504 may form internal electrostatic interactions for structure ensemble and adaptability
metabolism
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PHT4;1 acts upstream of the SA pathway. PHT4;1 contributes to SID2-dependent and -independent pathways
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metabolism
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the alternating conformations of the PstSCAB transporter are sensed by PhoR and PhoU. The sensory mechanism controls the alternate autokinase and phospho-PhoB phosphatase activities of PhoR, which ultimately control the signaling state of the response regulator PhoB
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metabolism
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upon phosphate starvation, these low-affinity phosphate transporters, e.g. Pho87 and Pho90, are endocytosed and targeted to the vacuole. For Pho87, this process strictly depends on SPL2, another Pho4-dependent gene that encodes a protein known to interact with the N-terminal SPX domain of the transporter
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metabolism
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phosphate transporter mechanism in the plant cell, overview. When the supply of phosphate is limited, plants grow more roots, increase the rate of phosphate uptake by roots from soil solution, retranslocate phosphate from older leaves, and deplete the vacuolar stores of phosphate. There is also significant retranslocation of phosphate in the phloem from older leaves to the growing shoot and from the shoot to the root
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metabolism
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the enzyme is involved in arbuscular mycorrhizal, AM, symbiosis,. During arbuscular mycorrhizal symbiosis, the AM fungus colonizes the root cortical cells where it forms branched hyphae called arbuscules that function in nutrient exchange with the plant. Each arbuscule is enveloped in a plant membrane, the periarbuscular membrane, that contains a unique set of proteins including phosphate transporters such as MtPT4 that are essential for symbiotic phosphate transport
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metabolism
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deprotonation of residue D324 triggers phosphate cytosolic release. Multiple proton transfer events proceed during the transition from the open conformation to the inward conformation. The exit path of the D324 proton requires residue D45
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physiological function

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high-affinity phosphate uptake system encoded by pst genes is, in addition to its role in phosphate transport, involved in copper and zinc homeostasis
physiological function
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using the Xenopus laevis expression system it is demonstrated that HvPHT1,6 is a proton-coupled phosphate transporter, though it has time-dependent activation at negative membrane potentials with linear concentration dependence similar to voltage-dependent ion channels, it also transports sulfate anions coupled to protons
physiological function
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N-terminal SPX domain of Pho90 inhibits low-affinity phosphate transport through a physical interaction with regulatory protein Spl2
physiological function
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phosphorylation of the sodium-hydrogen exchanger regulatory factor-1 (NHERF-1) plays a key role in the regulation of renal phosphate transport by parathyroid hormone and dopamine. The substitution of serine for aspartic acid (S77D) in the PDZ I domain of NHERF-1 decreases the binding affinity to Npt2a
physiological function
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NPT1 is a polyspecific anion transporter. Proteoliposomes containing purified SLC17A1 transport various organic anions such as p-aminohippuric acid, acetylsalicylic acid and urate in an inside positive membrane potential (DELTA PSI-dependent manner)
physiological function
when cells are grown at low phosphate concentrations, the high-affinity phosphate transporter Pho84p is the major contributor to selenite uptake. Pho84p is very selective for phosphate as compared to selenite
physiological function
when phosphate is abundant, selenite is internalized through the low-affinity phosphate transporters (Pho87p, Pho90p, and Pho91p). Low-affinity transporters discriminate less efficiently between selenite and phosphate
physiological function
PHT4;2 contributes to phosphate transport in isolated root plastids
physiological function
GmPT1 is a low-affinity phosphate transporter, the enzyme is important in phosphate uptake by roots and translocation within the plant, presumed to occur via a phosphate/proton cotransport mechanism
physiological function
GmPT2 is a low-affinity phosphate transporter, the enzyme is important in phosphate uptake by roots and translocation within the plant, presumed to occur via a phosphate/proton cotransport mechanism
physiological function
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constitutive expressed phosphate transporter, OsPht1;1, modulates phosphate uptake and translocation in phosphate-repleted rice plants
physiological function
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Pho87 and Pho90 are low-affinity phosphate transporters having differential roles. They represent non-redundant phosphate transporters, which are tuned by the integration of multiple nutrient signalling mechanisms in order to adjust phosphate-transport capacity to the general nutritional status of the environment. Pho90 is the most important phosphate transporter under high phosphate conditions in the absence of a high-affinity phosphate-transport system. Pho84 is the major phosphate transporter in Saccharomyces cerevisiae involved in rapid phosphate signalling
physiological function
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the phosphate transporter PHT4;1 is critical for basal defense and also implicate a potential role of the circadian clock in regulating innate immunity of Arabidopsis thaliana
physiological function
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the Pht1;9 and Pht1;8 transporters play similar roles during phosphate deficiency and arsenate exposure, they participate in phosphate acquisition and arsenate uptake. Plasma membrane-localized transporter Pht1;9 mediates high-affinity phosphate ?H+ symport activity and is highly induced in phosphate-starved Arabidopsis roots
physiological function
HvPHT1;1 is a high-affinity phosphate transporter involved in uptake of phosphate from soil solution under low phosphate conditions
physiological function
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Arabidopsis thaliana Pht1;5 is implicated in mobilizing stored phosphate out of older leaves, it mobilizes phosphate between source and sink organs and influences the interaction between phosphate homeostasis and ethylene signaling. Pht1;5 is involved in the mobilization of phosphate from shoots to roots during high-phosphate conditions, remobilization of phosphate from senescing to metabolically active parts of the plant
physiological function
a certain level of PiT1 is important for proliferation, role of PiT1 in regulation of cell proliferation, overview
physiological function
a certain level of PiT1 is important for proliferation, role of PiT1 in regulation of cell proliferation, overview
physiological function
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the enzyme contributes to the enhanced arsenate uptake capacity and affinity exhibited by Pteris vittata
physiological function
isoform PT4 is required for symbiotic phosphate uptake
physiological function
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isoforms PT9 and PT10 redundantly function in phosphate uptake
physiological function
the high-affinity phosphate transporter PT5 regulates phosphate transport to nodules and nodulation in soybean. The enzyme controls phosphate entry from roots to nodules, is critical for maintaining phosphate homeostasis in nodules, and subsequently regulates soybean nodulation and growth performance
physiological function
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the enzyme is involved in the translocation of phosphate from the root to the shoot but not from the soil solution into the root
physiological function
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under both phosphate sufficient and deficient conditions, transgenic plants constitutively expressing the enzyme grew taller than the non-transformed wild type, produce a greater volume of roots, accumulate more biomass and take up more phosphate
physiological function
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phosphate transporter PHT4;1 is a salicylic acid regulator acting independently of several known salicylic acid genes
physiological function
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overexpression of the rice phosphate transporter gene PT2 enhances tolerance to low phosphorus stress in soybean and improves phosphate acquisition and seed yield
physiological function
the enzyme plays an important role in chloroplast phosphate compartmentation and ATP synthesis, which affect plant growth, and also maintains the ionic environment of thylakoids
physiological function
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cells lacking PstSCAB survive poorly in stationary phase, in nutrient-limiting media, and under osmotic conditions reflective of those in the chicken. Polyphosphate levels in the mutant cells are elevated at stationary phase. The mutant strain is highly attenuated for colonization of newly hatched chicks, with levels of bacteria at several orders of magnitude below wild-type levels. Mutant and wild type grow similarly in complex media, but the PstS disrupotion mutant exhibits a significant growth defect in minimal medium supplemented with L-lactate
physiological function
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overexpression of PHT1:4 in soybean promotes the increase of plant biomass and yield of transgenic plants upon low phosphate stress, and increases the accumulation and transportation of phosphate from roots to leaves in the transgenic soybean lines
physiological function
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overexpression of isoform PHT1:7 (with a relative expression 2-7-fold that in the control) and silencing (with a relative expression of 0.3-1% that in the control). The growth vigor is ranked in the order overexpression line > wild type > silenced line. In the absence of phosphorus, the root length of the overexpression line is approximately 2.6 times that of the wild-type, while the root length of the silenced line is approximately 0.6 times that of the wild type. The tolerance to drought stress is ranked as wild type > overexpression line > silenced line
physiological function
A0A290QKL9
Staphylococcus aureus possesses three distinct Pi transporters: PstSCAB, PitA, and NptA. The loss of a single transporter does not affect S. aureus. Disruption of any two systems significantly reduces phosphate accumulation and growth in divergent environments. In a systemic mouse model of disease, loss of any one transporter does not decrease staphylococcal virulence. Loss of NptA in conjunction with either PstSCAB or PitA significantly reduces the ability of S. aureus to cause infection
physiological function
PHT1:7 enhances tolerance to limited phosphate nutrients in apple calli. Expression of PHT1:7 complements a yeast mutant lacking PHO84 expression. Overexpression of PHT1:7 enhances phosphate tolerance in tomato, transgenic plants show increased drought tolerance
physiological function
Pht1:3 overexpression in Arabidopsis thaliana enhances absorption of phosphate and increases biomass of the transgenic plants
physiological function
expression of MPT3:1 compensates the phosphate uptake in a yeast MB192 mutant is defective in phosphate transport under phosphate deficiency. Overexpression of MPT3:1 in Oryza sativa promotes phosphate uptake by the roots, and increases the translocation of phosphate from the roots to the shoots. The transgenic rice accumulates more chlorophyll and soluble sugar in the shoots than the wild-type under phosphate deficiency. Overexpression leads to an increase in tiller number and effective panicle of per plant, and increasing grain yield under phosphate deficiency
physiological function
overexpression of PT8 suppresses rice disease resistance against the pathogens Magnaporthe oryzae and Xanthomonas oryzae pv. oryzae. In PT8-overexpressing plants, pathogen-associated molecular patterns (PAMPs)-triggered immunity (PTI) response genes, such as Rac1 and SGT1, are suppressed during treatment with PAMPs chitin or flg22. PT8 is an interactor of a rice mitogen-activated protein kinase BWMK1. Under low phosphate conditions, the overexpressing plants display better agronomic traits than the control plants
physiological function
both wild-type and strains lacking PitB are able to internalize tellurite into the cytoplasm and reduce the oxyanion to black nano-sized and rod-shaped tellurium particles. The strain lacking PitB shows an increased resistance to the tellurite toxic effects. At 0.1 mM tellurite, the biomass formation of the wild-type strain decreases by half, and the mutant strain shows greater ability to reduce tellurite with respect to the wild-type, which is related to the greater biomass production of the mutant
physiological function
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vacuolar phosphate transporter VPT1 is associated with As(V) tolerance. VPT1 mutants display enhanced tolerance to As(V) toxicity, whereas plants overexpressing VPT1 are more sensitive to As(V) as compared with the wild-type plants. Many of the plasma membrane phosphate transporter family PHT1 genes are down-regulated in the VPT1 mutant as compared with the wild type under phosphate-sufficient conditions, but not when phosphate levels are low in the medium. As(V) resistance in VPT1 mutants is prominent only under phosphate-sufficient but not under phosphate-deficient conditions
physiological function
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transcription activator MYB5P directly binds to MYB binding site motifs on the PT5 promoter and induces transcription of PT5 in rice. Growth of the shoot and primary root in an PT5 mutant is more inhibited than in wild-type plants in high-phosphate and phosphate-deficient media. The fresh weights of PT5-deficient and MYB5P-RNAi plants are comparable. There is no difference in the phosphate content of roots and shoots of PT5 mutant and MYB5P-RNAi plants grown in high-phosphate and phosphate-deficient media. Overexpression of MYB5P leads to increased phosphate accumulation in shoots and roots
physiological function
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Pt9-overexpressing roots are difficult to colonize by arbuscular mycorrhiza fungi. Pt9 complements a yeast mutant defective in phosphate transporter activity and improves the phosphate concentration in rice. Pt9 is involved in phosphate accumulation under both phosphate-deficient and phosphate-sufficient conditions
physiological function
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vacuolar phosphate transporters, VPT1 and VPT3 contribute to cytosol-to-vacuole phosphate partitioning. VPT1 plays a predominant role, and VPT3 is particularly important when VPT1 is absent. The VPT1 VPT3 double mutant is more defective in phosphate homeostasis than the VPT1 single mutant. VPT2 does not appear to contribute to phosphate homeostasis under these conditions. The VPT1 VPT3 double mutant is impaired in reproductive development with shortened siliques and impaired seed set under sufficient phosphate and displays phosphate overaccumulation in the floral organs. Excess phosphate in the pistil is inhibitory to pollen tube growth, and thus seed yield, in the mutant plants
physiological function
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PHT2;1 functions as a low-affinity phosphate transporter. A PHT2;1 mutant has reduced phosphate accumulation, plant growth and photosynthetic rates. 52.6% of the decreased metabolites in mutant plants are flavonoids, i.e. a 40% lower content of total flavonoids compared with the wild type. Mutant plants are more sensitive to UV-B irradiation and have a reduced content of phenylalanine, largely associated with the repressed expression of ADT1/MTR1. Mutant plants show decreased grain yields at relatively high levels of UV-B irradiance
physiological function
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phosphate transporters PT2 and PT8 interact with protein phosphatase type 2C PP95. PP95 dephosphorylates PT8 at Ser517. Rice plants overexpressing PP95 show reduced PT8 phosphorylation and promote PT2 and PT8 trafficking from the ER to the plasma membrane, resulting in phosphate accumulation. Under phosphate-sufficient conditions, phosphate levels are lower in young leaves and higher in old leaves in PP95 mutants than in those of the wild-type, while the overall shoot phosphate levels are the same in the mutant and the wild-type. In the wild-type, PP95 accumulates under phosphate starvation but is rapidly degraded under phosphate-sufficient conditions
physiological function
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the phosphate transporter PHT4;1 is critical for basal defense and also implicate a potential role of the circadian clock in regulating innate immunity of Arabidopsis thaliana
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physiological function
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the Pht1;9 and Pht1;8 transporters play similar roles during phosphate deficiency and arsenate exposure, they participate in phosphate acquisition and arsenate uptake. Plasma membrane-localized transporter Pht1;9 mediates high-affinity phosphate ?H+ symport activity and is highly induced in phosphate-starved Arabidopsis roots
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physiological function
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cells lacking PstSCAB survive poorly in stationary phase, in nutrient-limiting media, and under osmotic conditions reflective of those in the chicken. Polyphosphate levels in the mutant cells are elevated at stationary phase. The mutant strain is highly attenuated for colonization of newly hatched chicks, with levels of bacteria at several orders of magnitude below wild-type levels. Mutant and wild type grow similarly in complex media, but the PstS disrupotion mutant exhibits a significant growth defect in minimal medium supplemented with L-lactate
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physiological function
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Pho87 and Pho90 are low-affinity phosphate transporters having differential roles. They represent non-redundant phosphate transporters, which are tuned by the integration of multiple nutrient signalling mechanisms in order to adjust phosphate-transport capacity to the general nutritional status of the environment. Pho90 is the most important phosphate transporter under high phosphate conditions in the absence of a high-affinity phosphate-transport system. Pho84 is the major phosphate transporter in Saccharomyces cerevisiae involved in rapid phosphate signalling
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physiological function
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Staphylococcus aureus possesses three distinct Pi transporters: PstSCAB, PitA, and NptA. The loss of a single transporter does not affect S. aureus. Disruption of any two systems significantly reduces phosphate accumulation and growth in divergent environments. In a systemic mouse model of disease, loss of any one transporter does not decrease staphylococcal virulence. Loss of NptA in conjunction with either PstSCAB or PitA significantly reduces the ability of S. aureus to cause infection
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physiological function
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GmPT1 is a low-affinity phosphate transporter, the enzyme is important in phosphate uptake by roots and translocation within the plant, presumed to occur via a phosphate/proton cotransport mechanism
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physiological function
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GmPT2 is a low-affinity phosphate transporter, the enzyme is important in phosphate uptake by roots and translocation within the plant, presumed to occur via a phosphate/proton cotransport mechanism
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physiological function
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transcription activator MYB5P directly binds to MYB binding site motifs on the PT5 promoter and induces transcription of PT5 in rice. Growth of the shoot and primary root in an PT5 mutant is more inhibited than in wild-type plants in high-phosphate and phosphate-deficient media. The fresh weights of PT5-deficient and MYB5P-RNAi plants are comparable. There is no difference in the phosphate content of roots and shoots of PT5 mutant and MYB5P-RNAi plants grown in high-phosphate and phosphate-deficient media. Overexpression of MYB5P leads to increased phosphate accumulation in shoots and roots
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additional information

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OsPT1 expression is not significantly regulated by phosphate-supply level in the transgenic rice plants. Expression of OsPT1 is upregulated in rice phosphate accumulator mutant (ospho2) and not altered in phosphate starvation responsive mutant (osphr2)
additional information
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recombinant human NELL-1 and BMP-2 significantly increase phosphate transport and recombinant human NELL-1 regulates Pit transporters, detailed overview
additional information
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the SPX domain is essential for vacuolar targeting of Pho87 and Pho90 in response to glucose starvation and rapamycin treatment
additional information
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PHT4;1 expression is Rregulated by light and the circadian clock, overview. PHT4;1-1 exhibits a similar diurnal expression pattern, with peaks in the daytime and troughs in the nighttime. Treatment with a salicylic acid agonist induce a similar level of resistance against pathogens in wild-type and mutant PHT4;1
additional information
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transcriptional regulaiton of the PHT1 transporters, variation of phosphate concentration in the medium promotes a rapid modulation of PHT1 transcripts, overview
additional information
isoform PT1 is not required for symbiotic phosphate uptake
additional information
isoform PT1 is not required for symbiotic phosphate uptake
additional information
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isoform PT1 is not required for symbiotic phosphate uptake
additional information
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PHT4;1 expression is Rregulated by light and the circadian clock, overview. PHT4;1-1 exhibits a similar diurnal expression pattern, with peaks in the daytime and troughs in the nighttime. Treatment with a salicylic acid agonist induce a similar level of resistance against pathogens in wild-type and mutant PHT4;1
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additional information
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the SPX domain is essential for vacuolar targeting of Pho87 and Pho90 in response to glucose starvation and rapamycin treatment
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D144A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
D191A
residue predicted to face the extracellular side, 40% of wild-type activity in a yeast Pam2 complementation assay
D212A
residue predicted to face the extracellular side, 40% of wild-type activity in a yeast Pam2 complementation assay
D228E
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drastic increase in expression compared to wild-type, mutant shows no transport activity
D308A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
D35A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
D367A
residue predicted to face the cytoplasm side, 40-50% of wild-type activity in a yeast Pam2 complementation assay
D382A
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Km: (phosphate) 0.057 mM (in the presence of 25 mM NaCl), 0.49 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 156 nmol/mg of protein/h, results indicate that Arg-228 may participate in interactions associated with protein conformational changes required for full transport activity
D382E
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Km: (phosphate) 0.046 mM (in the presence of 25 mM NaCl), 0.73 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 96 nmol/mg of protein/h, drastic increase in expression compared to wild-type, results indicate that Arg-228 may participate in interactions associated with protein conformational changes required for full transport activity
D382N
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mutant shows no transport activity
D38A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
D93A
residue predicted to face the cytoplasm side, 40-50% of wild-type activity in a yeast Pam2 complementation assay
E122A
residue predicted to face the extracellular side, 80% of wild-type activity in a yeast Pam2 complementation assay
E504A
residue predicted to face the cytoplasm side, 40-50% of wild-type activity in a yeast Pam2 complementation assay
F169A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
K124A
residue predicted to face the extracellular side, 60% of wild-type activity in a yeast Pam2 complementation assay
K16A
residue predicted to face the cytoplasm side, 40-50% of wild-type activity in a yeast Pam2 complementation assay
K373A
residue predicted to face the cytoplasm side, 60-70% of wild-type activity in a yeast Pam2 complementation assay
K449A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
K482A
residue predicted to face the extracellular side, 80% of wild-type activity in a yeast Pam2 complementation assay
K99A
residue predicted to face the cytoplasm side, 60-70% of wild-type activity in a yeast Pam2 complementation assay
N421A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
Q172A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
R120K
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Km: (phosphate) 0.161 mM (in the presence of 25 mM NaCl), 1.48 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 250 nmol/mg of protein/h, results indicate that Arg-120 may be important for binding and translocation of the substrate
R134A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
R201K
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Km: (phosphate) 0.214 mM (in the presence of 25 mM NaCl), 2.29 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 100 nmol/mg of protein/h, results indicate that Arg-201 may be important for binding and translocation of the substrate
R216A
residue predicted to face the extracellular side, 40% of wild-type activity in a yeast Pam2 complementation assay
R228K
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drastic increase in expression compared to wild-type, Km: (phosphate) 0.103 mM (in the presence of 25 mM NaCl), 1.99 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 274 nmol/mg of protein/h, drastic increase in expression compared to wild-type, results indicate that Arg-228 may participate in interactions associated with protein conformational changes required for full transport activity
R233A
residue predicted to face the cytoplasm side, 40-50% of wild-type activity in a yeast Pam2 complementation assay
R345A
residue predicted to face the extracellular side, 60% of wild-type activity in a yeast Pam2 complementation assay
R402A
residue predicted to face the extracellular side, 40% of wild-type activity in a yeast Pam2 complementation assay
S124A
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Km: (phosphate) 0.0448 mM (in the presence of 25 mM NaCl), 0.27 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 47 nmol/mg of protein/h, results indicate that Ser-124 may function as a transient binding site for Na+ ions in close proximity to the periplasmic side
S124T
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Km: (phosphate) 0.109 mM (in the presence of 25 mM NaCl), 0.88 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 254 nmol/mg of protein/h, results indicate that Ser-124 may function as a transient binding site for Na+ ions in close proximity to the periplasmic side
W304A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
Y145A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
Y312A
mutation of residue within the transmembrane helix, partial complementation of a yeast Pam2 mutnat strain
E179Q
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mutation predicted to lock the PstB protein in either of two conformations. Mutation is predicted to reside in an outward-facing, closed conformation and signals phosphate starvation. Mutant does not show phosphate transport
E240Q
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mutation in pstC, loss of phosphate transport through the pst system, alkaline phosphatase activity remains repressed
G48I
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mutation in pstB, loss of phosphate transport through the Pst system and derepression of alkaline phosphatase activity
K49Q
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mutation in pstB, loss of phosphate transport through the Pst system and derepression of alkaline phosphatase activity
P123L
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mutation in pstC, loss of phosphate transport activity
P123L/P166L
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mutation in pstA, complete loss of phosphate transport activity
P132L
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mutation in pstA, partial loss of phosphate uptake activity
P166L
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mutation in pstA, partial loss of phosphate uptake activity
P183L
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mutation in pstC, loss of phosphate transport activity
Q160K
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mutation predicted to lock the PstB protein in either of two conformations. Mutation is predicted to reside in an inward-facing, open conformation and signals phosphate sufficiency. Mutant does not show phosphate transport
R238Q
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mutation in pstC, loss of phosphate transport through the pst system, alkaline phosphatase activity remains repressed
R238Q/E240Q
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mutation in pstC, loss of phosphate transport through the pst system, alkaline phosphatase activity remains repressed
E179Q
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mutation predicted to lock the PstB protein in either of two conformations. Mutation is predicted to reside in an outward-facing, closed conformation and signals phosphate starvation. Mutant does not show phosphate transport
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Q160K
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mutation predicted to lock the PstB protein in either of two conformations. Mutation is predicted to reside in an inward-facing, open conformation and signals phosphate sufficiency. Mutant does not show phosphate transport
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S115F
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mutant MtPT4S115F is retained in the endomembrane system and colocalizes with endoplasmic reticulum and trans-Golgi network markers. Mutation of this residue disrupts a conserved process in phosphate transporter trafficking
S117F
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mutant MtPT1S117F is retained in the endomembrane system and colocalizes with endoplasmic reticulum and trans-Golgi network markers. Mutation of this residue disrupts a conserved process in phosphate transporter trafficking
S115F
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mutant MtPT4S115F is retained in the endomembrane system and colocalizes with endoplasmic reticulum and trans-Golgi network markers. Mutation of this residue disrupts a conserved process in phosphate transporter trafficking
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S117F
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mutant MtPT1S117F is retained in the endomembrane system and colocalizes with endoplasmic reticulum and trans-Golgi network markers. Mutation of this residue disrupts a conserved process in phosphate transporter trafficking
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H75A
mutation abolishes mitchondrial transport of phosphate
L175A
mitochondrial transport of phosphate but not of Cu is compromised in the mutant. L175A mutant protein is present in mitochondria and increases steady-state COX1 levels
R138A
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mutant possesses Na+/phosphate cotransport activity comparable to that of the wild type protein, but the DELTA PSI-dependent anion transport is inactive
DELTA1-375
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mutant lacking the entire N-terminal SPX domain shows no differences in protein level or plasma membrane localisation compared to wild-type, phosphate uptake-rate is higher compared to wild-type, Km remains in the same range as wild-type, truncated mutant has increased catalytic activity
D45E
mutant has a Km similar to wild-type, but the Vmax is lowered 50fold below wild type
D45E
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mutant has a Km similar to wild-type, but the Vmax is lowered 50fold below wild type
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D22A
mutant maintains phosphate-binding affinities, but shows phosphate uptake defects
D22A/D258A
mutant fails to bind phosphate
D258A
mutant maintains phosphate-binding affinities, but shows phosphate uptake defects
D327Q
mutant fails to bind phosphate
W139A
mutant fails to bind phosphate
W378A
mutant fails to bind phosphate
D22A
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mutant maintains phosphate-binding affinities, but shows phosphate uptake defects
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D22A/D258A
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mutant fails to bind phosphate
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D258A
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mutant maintains phosphate-binding affinities, but shows phosphate uptake defects
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D327Q
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mutant fails to bind phosphate
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W378A
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mutant fails to bind phosphate
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D188K

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no ATP hydrolyzing ability
D188K
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no ATP hydrolyzing ability
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D45N

mutant has an about 10fold lower Km and 5fold lower Vmax value compared with wild-type PiPT
D45N
mutant binds phosphate but does not transport it
D45N

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mutant has an about 10fold lower Km and 5fold lower Vmax value compared with wild-type PiPT
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D45N
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mutant binds phosphate but does not transport it
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additional information

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overexpression of the s(V)-tolerant missense mutant pht1;1-3 results in decreased phosphate content and enhanced arsenic accumulation, the mutant accumulates double the arsenic found in wild-type plants, the As(V) tolerance phenotypes are enhanced in the pht1;1-3 expressor lines, pht1;1-3 exhibits a constitutive phosphate starvation response, overview
additional information
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heterologous functional expression of the Pht1;9 transporter in Saccharomyces cerevisiae strain BY4741 DELTApho84 mutant, which shows growth limitation under phosphate starvation, and complementation, expression?subcellular localization studies, reverse genetics approaches in planta, and generation of double Pht1;9?Pht1;8 silencing lines
additional information
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construction of Pht1;5 deletion and overexpression mutants, phenotypes, detailed overview. Pht1;5 overexpression alters Root hair development and primary root growth in association with ethylene signaling
additional information
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pht1;1-3 mutation in Arabidopsis thaliana
additional information
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heterologous functional expression of the Pht1;9 transporter in Saccharomyces cerevisiae strain BY4741 DELTApho84 mutant, which shows growth limitation under phosphate starvation, and complementation, expression?subcellular localization studies, reverse genetics approaches in planta, and generation of double Pht1;9?Pht1;8 silencing lines
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additional information
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smooth muscle cells expressing small interfering RNA show decreased Pit-1 mRNA and protein levels and reduced sodium-dependent phosphate transport activity compared with the control transduced cells, phosphate-induced smooth muscle cell calcification is significantly inhibited in smooth muscle cell-siRNA, and the siRNA-cells are not less susceptible to cell death than cells containing normal levels of Pit-1, overexpression of murine wild-type Pit-1 restores phosphate uptake and phosphate-induced calcification in human Pit-1 deficient cells, overview
additional information
downregulation of PiT1 in two transformed human cells lines, HepG2 and HeLa, phenotypes, overview. Overexpression of hPiT1 or hPiT2 in MC3T3-E1 cells, phgenotypes, overview. Transduction study analyzing the presence of functional hPiT1, hPiT2, and mPiT2 on the cell surface of MC3T3-E1-LXSN, -LPiT1SN, -LPiT2SN, NIH3T3-LXSN, and -LPiT1SN cells
additional information
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downregulation of PiT1 in two transformed human cells lines, HepG2 and HeLa, phenotypes, overview. Overexpression of hPiT1 or hPiT2 in MC3T3-E1 cells, phgenotypes, overview. Transduction study analyzing the presence of functional hPiT1, hPiT2, and mPiT2 on the cell surface of MC3T3-E1-LXSN, -LPiT1SN, -LPiT2SN, NIH3T3-LXSN, and -LPiT1SN cells
additional information
HvPHT1;1 activity analysis in Xenopus laevis oocytes via cRNA-injection, low external sodium concentration is critical for phosphate transporter characterization in Xenopus laevis oocytes
additional information
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HvPHT1;1 activity analysis in Xenopus laevis oocytes via cRNA-injection, low external sodium concentration is critical for phosphate transporter characterization in Xenopus laevis oocytes
additional information
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pht1;1-3 mutation in Arabidopsis
additional information
construction of promoter deletion mutants
additional information
construction of promoter deletion mutants
additional information
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construction of promoter deletion mutants
additional information
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pht1;1-3 mutation in Arabidopsis
additional information
generation of PiT1 knock-out mice and isolated mouse embryonic fibroblasts with PiT1 knockout
additional information
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generation of PiT1 knock-out mice and isolated mouse embryonic fibroblasts with PiT1 knockout
additional information
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construction of deletion mutants, mutation of either pstS and phnD leads to impaired cell growth in minimal medium, the cells are only viable in high phosphate concentrated medium
additional information
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construction of deletion mutants, mutation of either pstS and phnD leads to impaired cell growth in minimal medium, the cells are only viable in high phosphate concentrated medium
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additional information
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transgenic plants of OsPT1 overexpression lines and RNA-interference knockdown lines contain significantly higher and lower phosphate concentration, respectively, respectively, compared to that of wild-type control. OsPT1 is able to complement the nH+/phosphate co-transporter activities in a yeast mutant MB192 strain defective in phosphate-uptake. No significant difference of phosphate concentration in the roots of OsPT1-Ox1, OsPT1-Ri1 and wild-type irrespective of phosphate supply levels
additional information
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pht1;1-3 mutation in Arabidopsis
additional information
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effective symbiotic phosphate transport in mycorrhizal roots of Petunia is a hidden molecular phenotype, overview. Construction of transposon insertion mutants is established by crossing the transgenic reporter line with the mutator W138 line, from which the phosphate transporter downregulated mutant is identi?ed, which exhibits strongly reduced expression of mycorrhiza-inducible phosphate transporters in mycorrhizal roots
additional information
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the normal suppression of enzyme expression by the two-component regulatory system PhoBR is relieved in pstS-Tn5 and pstA-Tn5 mutants, which constitutively produce AP regardless of growth conditions, pst mutants show no significant growth defects during the independent culture or coculture studies in rich medium, phosphate-limiting minimal salts medium, or human urine. Mutants complemented with the complete pst operon repress AP synthesis in vitro and colonize the mouse bladder in numbers comparable to the wild-type strain HI4320, overview
additional information
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phosphate-specific transport mutants, DELTApst, show a defect in biofilm formation when grown in human urine, overview
additional information
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the normal suppression of enzyme expression by the two-component regulatory system PhoBR is relieved in pstS-Tn5 and pstA-Tn5 mutants, which constitutively produce AP regardless of growth conditions, pst mutants show no significant growth defects during the independent culture or coculture studies in rich medium, phosphate-limiting minimal salts medium, or human urine. Mutants complemented with the complete pst operon repress AP synthesis in vitro and colonize the mouse bladder in numbers comparable to the wild-type strain HI4320, overview
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additional information
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phosphate-specific transport mutants, DELTApst, show a defect in biofilm formation when grown in human urine, overview
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additional information
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strain PAM1 is transformed with PHO84pht1;1-3, a mutagenized version of the PHO84 cDNA, encoding a Gly-to-Glu mutation identical to the one present in the Arabidopsis thaliana pht1;1-3 allele. In the presence of 550 mM Pi, cells expressing PHO84pht1;1-3 exhibits more phosphatase activity than cells transformed with either PHO84 cDNA or the empty vector PAM1, the rate of Pi and As(V) transport in cells expressing PHO84pht1;1-3 is significantly lower than in the original PAM1, overview
additional information
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mutation of pstC affects the PstSCAB phosphate transport system resulting in the PhoB-phenotype, overview
additional information
PT4-deficient transgenic mutant tomato plants show a reduced number of roots and shorter lateral roots, overview
additional information
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PT4-deficient transgenic mutant tomato plants show a reduced number of roots and shorter lateral roots, overview
additional information
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pht1;1-3 mutation in Arabidopsis
additional information
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pht1;1-3 mutation in Arabidopsis
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Novak, R.; Cauwels, A.; Charpentier, E.; Tuomanen, E.
Identification of a Streptococcus pneumoniae gene locus encoding proteins of an ABC phosphate transporter and a two-component regulatory system
J. Bacteriol.
181
1126-1133
1999
Streptococcus pneumoniae
brenda
Bhatt, K.; Banerjee, S.K.; Chakraborti, P.K.
Evidence that phosphate specific transporter is amplified in a fluoroquinoline resistant Mycobacterium smegmatis
Eur. J. Biochem.
267
4028-4032
2000
Mycolicibacterium smegmatis
brenda
Braibant, M.; Lefevre, P.; de Wit, L.; Ooms, J.; Peirs, P.; Huygen, K.; Wattiez, R.; Content, J.
Identification of a second Mycobacterium tuberculosis gene cluster encoding protein of an ABC phosphate transporter
FEBS Lett.
394
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1996
Mycobacterium tuberculosis
brenda
Chan, F.Y.; Torriani, A.
PstB protein of the phosphate-specific transport system of Escherichia coli is an ATPase
J. Bacteriol.
178
3974-3977
1996
Escherichia coli
brenda
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A Mycobacterium tuberculosis gene cluster encoding proteins of a phosphate transporter homologous to the Escherichia coli Pst system
Gene
176
171-176
1996
Mycobacterium tuberculosis
brenda
Webb, D.C.; Rosenberg, H.; Cox, G.B.
Mutational analysis of the Escherichia coli phosphate-specific transport sytem, a member of the traffic ATPase (or ABC) family of membrane transporters. A role for proline residues in transmembrane helices
J. Biol. Chem.
267
24661-24668
1992
Escherichia coli
brenda
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Role of an ABC importer in mycobacterial drug resistance
Biosci. Rep.
19
293-300
1999
Mycolicibacterium smegmatis
brenda
Cox, G.B.; Webb, D.; Godovac-Zimmermann, J.; Rosenberg, H.; Rosenberg, H.
Specific amino acid residues in both the PstB and PstC proteins are required for phosphate transport by the Escherichia coli pst system
J. Bacteriol.
171
1531-1534
1989
Escherichia coli
brenda
Sarin, J.; Aggarwal, S.; Chaba, R.; Varshney, G.C.; Chakraborti, P.K.
B-subunit of phosphate-specific transporter from Mycobacterium tuberculosis is a thermostable ATPase
J. Biol. Chem.
276
44590-44597
2001
Mycobacterium tuberculosis, Escherichia coli, Mycobacterium tuberculosis H37Rv
brenda
Allenby, N.E.; O'Connor, N.; Pragai, Z.; Carter, N.M.; Miethke, M.; Engelmann, S.; Hecker, M.; Wipat, A.; Ward, A.C.; Harwood, C.R.
Post-transcriptional regulation of the Bacillus subtilis pst operon encoding a phosphate-specific ABC transporter
Microbiology
150
2619-2628
2004
Bacillus subtilis
brenda
Vyas, N.K.; Vyas, M.N.; Quiocho, F.A.
Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions
Structure
11
765-774
2003
Mycobacterium tuberculosis
brenda
Gupta, S.; Chakraborti, P.K.; Sarkar, D.
Nucleotide-induced conformational change in the catalytic subunit of the phosphate-specific transporter from M. tuberculosis: implications for the ATPase structure
Biochim. Biophys. Acta
1750
112-121
2005
Mycobacterium tuberculosis
brenda
Leung, J.C.; Barac-Nieto, M.; Hering-Smith, K.; Silverstein, D.M.
Expression of the rat renal PiT-2 phosphate transporter
Horm. Metab. Res.
37
265-269
2005
Rattus norvegicus, Didelphis virginiana, Canis lupus familiaris
brenda
Yuan, Z.C.; Zaheer, R.; Finan, T.M.
Regulation and properties of PstSCAB, a high-affinity, high-velocity phosphate transport system of Sinorhizobium meliloti
J. Bacteriol.
188
1089-1102
2006
Sinorhizobium meliloti
brenda
Fischer, R.J.; Oehmcke, S.; Meyer, U.; Mix, M.; Schwarz, K.; Fiedler, T.; Bahl, H.
Transcription of the pst operon of Clostridium acetobutylicum is dependent on phosphate concentration and pH
J. Bacteriol.
188
5469-5478
2006
Clostridium acetobutylicum
brenda
Gebhard Susann, G.S.; Tran Sieu , T.S.; Cook Gregory , C.G.
The Phn system of Mycobacterium smegmatis: a second high-affinity ABC-transporter for phosphate
Microbiology
152
3453-3465
2006
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis SG34
brenda
Soualhine, H.; Brochu, V.; Menard, F.; Papadopoulou, B.; Weiss, K.; Bergeron, M.G.; Legare, D.; Drummelsmith, J.; Ouellette, M.
A proteomic analysis of penicillin resistance in Streptococcus pneumoniae reveals a novel role for PstS, a subunit of the phosphate ABC transporter
Mol. Microbiol.
58
1430-1440
2005
Streptococcus pneumoniae
brenda
Hase, A.; Nishikoori, M.; Okuyama, H.
Induction of high affinity phosphate transporter in the duckweed Spirodela oligorrhiza
Physiol. Plant.
120
271-279
2004
Landoltia punctata
brenda
Gonzalez, E.; Solano, R.; Rubio, V.; Leyva, A.; Paz-Ares, J.
Phosphate transporter traffic facilitator1 is a plant-specific SEC12-related protein that enables the endoplasmic reticulum exit of a high-affinity phosphate transporter in Arabidopsis
Plant Cell
17
3500-3512
2005
Arabidopsis thaliana
brenda
Nagy, R.; Karandashov, V.; Chague, V.; Kalinkevich, K.; Tamasloukht, M.; Xu, G.; Jakobsen, I.; Levy, A.A.; Amrhein, N.; Bucher, M.
The characterization of novel mycorrhiza-specific phosphate transporters from Lycopersicon esculentum and Solanum tuberosum uncovers functional redundancy in symbiotic phosphate transport in solanaceous species
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42
236-250
2005
Solanum tuberosum (Q563I1), Solanum tuberosum, Solanum lycopersicum (Q563I3), Solanum lycopersicum
brenda
Li, X.; Yang, H.Y.; Giachelli, C.M.
Role of the sodium-dependent phosphate cotransporter, Pit-1, in vascular smooth muscle cell calcification
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98
905-912
2006
Homo sapiens
brenda
Jacobsen, S.M.; Lane, M.C.; Harro, J.M.; Shirtliff, M.E.; Mobley, H.L.
The high-affinity phosphate transporter Pst is a virulence factor for Proteus mirabilis during complicated urinary tract infection
FEMS Immunol. Med. Microbiol.
52
180-193
2008
Proteus mirabilis, Proteus mirabilis HI4320
brenda
Nagy, R.; Vasconcelos, M.J.; Zhao, S.; McElver, J.; Bruce, W.; Amrhein, N.; Raghothama, K.G.; Bucher, M.
Differential regulation of five Pht1 phosphate transporters from maize (Zea mays L.)
Plant Biol.
8
186-197
2006
Zea mays (Q49B46), Zea mays (Q49B45), Zea mays (Q49B44), Zea mays (Q49B43), Zea mays (Q49B42), Zea mays (Q5CC71)
brenda
Xiao, K.; Liu, J.; Dewbre, G.; Harrison, M.; Wang, Z.Y.
Isolation and characterization of root-specific phosphate transporter promoters from Medicago truncatula
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8
439-449
2006
Medicago truncatula (O22301), Medicago truncatula (O22302), Medicago truncatula
brenda
Catarecha, P.; Segura, M.D.; Franco-Zorrilla, J.M.; Garcia-Ponce, B.; Lanza, M.; Solano, R.; Paz-Ares, J.; Leyva, A.
A mutant of the Arabidopsis phosphate transporter PHT1;1 displays enhanced arsenic accumulation
Plant Cell
19
1123-1133
2007
Arabidopsis thaliana, Saccharomyces cerevisiae
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Ghoshal, A.; Mukhopadhyay, S.; Demine, R.; Forgber, M.; Jarmalavicius, S.; Saha, B.; Sundar, S.; Walden, P.; Mandal, C.; Mandal, C.
Detection and characterization of a sialoglycosylated bacterial ABC-type phosphate transporter protein from patients with visceral leishmaniasis
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Pseudomonas aeruginosa
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Arabidopsis ANTR1 is a thylakoid Na+-dependent phosphate transporter: functional characterization in Escherichia coli
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Arabidopsis thaliana (O82390), Arabidopsis thaliana
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O'May, G.A.; Jacobsen, S.M.; Longwell, M.; Stoodley, P.; Mobley, H.L.; Shirtliff, M.E.
The high-affinity phosphate transporter Pst in Proteus mirabilis HI4320 and its importance in biofilm formation
Microbiology
155
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2009
Proteus mirabilis, Proteus mirabilis HI4320
brenda
Wegmueller, S.; Svistoonoff, S.; Reinhardt, D.; Stuurman, J.; Amrhein, N.; Bucher, M.
A transgenic dTph1 insertional mutagenesis system for forward genetics in mycorrhizal phosphate transport of Petunia
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Petunia x hybrida
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Ruiz-Pavon, L.; Karlsson, P.M.; Carlsson, J.; Samyn, D.; Persson, B.; Persson, B.L.; Spetea, C.
Functionally important amino acids in the Arabidopsis thylakoid phosphate transporter: homology modeling and site-directed mutagenesis
Biochemistry
49
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2010
Arabidopsis thaliana
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Huerlimann, H.C.; Pinson, B.; Stadler-Waibel, M.; Zeeman, S.C.; Freimoser, F.M.
The SPX domain of the yeast low-affinity phosphate transporter Pho90 regulates transport activity
EMBO Rep.
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Saccharomyces cerevisiae
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Weinman, E.J.; Steplock, D.; Zhang, Y.; Biswas, R.; Bloch, R.J.; Shenolikar, S.
Cooperativity between the phosphorylation of Thr95 and Ser77 of NHERF-1 in the hormonal regulation of renal phosphate transport
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2010
Homo sapiens
brenda
Iharada, M.; Miyaji, T.; Fujimoto, T.; Hiasa, M.; Anzai, N.; Omote, H.; Moriyama, Y.
Type 1 sodium-dependent phosphate transporter (SLC17A1 Protein) is a Cl(-)-dependent urate exporter
J. Biol. Chem.
285
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Mus musculus
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Yadav, V.; Kumar, M.; Deep, D.K.; Kumar, H.; Sharma, R.; Tripathi, T.; Tuteja, N.; Saxena, A.K.; Johri, A.K.
A phosphate transporter from the root endophytic fungus Piriformospora indica plays a role in phosphate transport to the host plant
J. Biol. Chem.
285
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2010
Serendipita indica (A8N031), Serendipita indica
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Uptake of selenite by Saccharomyces cerevisiae involves the high- and low-affinity orthophosphate transporters
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Saccharomyces cerevisiae (P25297), Saccharomyces cerevisiae (P25360), Saccharomyces cerevisiae (P39535), Saccharomyces cerevisiae (P27514), Saccharomyces cerevisiae
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Miao, J.; Sun, J.; Liu, D.; Li, B.; Zhang, A.; Li, Z.; Tong, Y.
Characterization of the promoter of phosphate transporter TaPHT1.2 differentially expressed in wheat varieties
J. Genet. Genomics
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2009
Triticum sp.
brenda
Cesselin, B.; Ali, D.; Gratadoux, J.J.; Gaudu, P.; Duwat, P.; Gruss, A.; El Karoui, M.
Inactivation of the Lactococcus lactis high-affinity phosphate transporter confers oxygen and thiol resistance and alters metal homeostasis
Microbiology
155
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2009
Lactococcus lactis
brenda
Preuss, C.P.; Huang, C.Y.; Gilliham, M.; Tyerman, S.D.
Channel-like characteristics of the low-affinity barley phosphate transporter PHT1;6 when expressed in Xenopus oocytes
Plant Physiol.
152
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2010
Hordeum vulgare
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Cowan, C.M.; Zhang, X.; James, A.W.; Mari Kim, T.; Sun, N.; Wu, B.; Ting, K.; Soo, C.
NELL-1 increases pre-osteoblast mineralization using both phosphate transporter Pit1 and Pit2
Biochem. Biophys. Res. Commun.
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2012
Mus musculus
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Differential roles for the low-affinity phosphate transporters Pho87 and Pho90 in Saccharomyces cerevisiae
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Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
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Byskov, K.; Jensen, N.; Kongsfelt, I.; Wielsoe, M.; Pedersen, L.; Haldrup, C.; Pedersen, L.
Regulation of cell proliferation and cell density by the inorganic phosphate transporter PiT1
Cell Div.
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Homo sapiens (Q8WUM9), Homo sapiens, Mus musculus (Q61609), Mus musculus
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Nussaume, L.; Kanno, S.; Javot, H.; Marin, E.; Pochon, N.; Ayadi, A.; Nakanishi, T.M.; Thibaud, M.C.
Phosphate import in plants: focus on the PHT1 transporters
Front. Plant Sci.
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Arabidopsis thaliana, Saccharomyces cerevisiae, Neurospora crassa, Diversispora versiformis, Medicago truncatula, Hordeum vulgare, Solanum tuberosum, Oryza sativa, Solanum lycopersicum
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Wang, G.Y.; Shi, J.L.; Ng, G.; Battle, S.L.; Zhang, C.; Lu, H.
Circadian clock-regulated phosphate transporter PHT4;1 plays an important role in Arabidopsis defense
Mol. Plant
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516-526
2011
Arabidopsis thaliana, Arabidopsis thaliana Col-0
brenda
Remy, E.; Cabrito, T.R.; Batista, R.A.; Teixeira, M.C.; Sa-Correia, I.; Duque, P.
The Pht1;9 and Pht1;8 transporters mediate inorganic phosphate acquisition by the Arabidopsis thaliana root during phosphorus starvation
New Phytol.
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356-371
2012
Arabidopsis thaliana, Arabidopsis thaliana Col-0
brenda
Preuss, C.P.; Huang, C.Y.; Tyerman, S.D.
Proton-coupled high-affinity phosphate transport revealed from heterologous characterization in Xenopus of barley-root plasma membrane transporter, HvPHT1;1
Plant Cell Environ.
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Hordeum vulgare (Q8H6E0), Hordeum vulgare
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Nagarajan, V.K.; Jain, A.; Poling, M.D.; Lewis, A.J.; Raghothama, K.G.; Smith, A.P.
Arabidopsis Pht1;5 mobilizes phosphate between source and sink organs and influences the interaction between phosphate homeostasis and ethylene signaling
Plant Physiol.
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2011
Arabidopsis thaliana
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Irigoyen, S.; Karlsson, P.M.; Kuruvilla, J.; Spetea, C.; Versaw, W.K.
The sink-specific plastidic phosphate transporter PHT4;2 influences starch accumulation and leaf size in Arabidopsis
Plant Physiol.
157
1765-1777
2011
Arabidopsis thaliana (Q7XJR2)
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Sun, S.; Gu, M.; Cao, Y.; Huang, X.; Zhang, X.; Ai, P.; Zhao, J.; Fan, X.; Xu, G.
A constitutive expressed phosphate transporter, OsPht1;1, modulates phosphate uptake and translocation in Pi-replete rice
Plant Physiol.
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2012
Oryza sativa
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Wu, Z.; Zhao, J.; Gao, R.; Hu, G.; Gai, J.; Xu, G.; Xing, H.
Molecular cloning, characterization and expression analysis of two members of the Pht1 family of phosphate transporters in Glycine max
PLoS ONE
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Glycine max (F5A0U7), Glycine max (C0LZ80), Glycine max gantai (F5A0U7), Glycine max gantai (C0LZ80)
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Pumplin, N.; Zhang, X.; Noar, R.D.; Harrison, M.J.
Polar localization of a symbiosis-specific phosphate transporter is mediated by a transient reorientation of secretion
Proc. Natl. Acad. Sci. USA
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2012
Medicago truncatula, Medicago truncatula A17
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Liu, P.; Chen, S.; Song, A.; Zhao, S.; Fang, W.; Guan, Z.; Liao, Y.; Jiang, J.; Chen, F.
A putative high affinity phosphate transporter, CmPT1, enhances tolerance to Pi deficiency of chrysanthemum
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Chrysanthemum x morifolium
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Lapis-Gaza, H.R.; Jost, R.; Finnegan, P.M.
Arabidopsis phosphate transporter1 genes PHT1;8 and PHT1;9 are involved in root-to-shoot translocation of orthophosphate
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334
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Arabidopsis thaliana
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The phosphate transporter PHT4;1 is a salicylic acid regulator likely controlled by the circadian clock protein CCA1
Front. Plant Sci.
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Arabidopsis thaliana
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Chen, G.; Yan, W.; Yang, S.; Wang, A.; Gai, J.; Zhu, Y.
Overexpression of rice phosphate transporter gene OsPT2 enhances tolerance to low phosphorus stress in soybean
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Oryza sativa
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Park, Y.; Bang, I.
Bacterial phosphate homeostasis: Role of phosphate transporters
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Myxococcus xanthus, Escherichia coli, Mycolicibacterium smegmatis, Arthrobacter sp., Rhodobacter capsulatus, Pseudomonas aeruginosa
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Xie, X.; Huang, W.; Liu, F.; Tang, N.; Liu, Y.; Lin, H.; Zhao, B.
Functional analysis of the novel mycorrhiza-specific phosphate transporter AsPT1 and PHT1 family from Astragalus sinicus during the arbuscular mycorrhizal symbiosis
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2013
Astragalus sinicus (K0IIN5), Astragalus sinicus (K0I2D6), Astragalus sinicus
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A member of the phosphate transporter 1 (Pht1) family from the arsenic-hyperaccumulating fern Pteris vittata is a high-affinity arsenate transporter
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Pteris vittata
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Phosphate transporters OsPHT1;9 and OsPHT1;10 are involved in phosphate uptake in rice
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Oryza sativa
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ESCRT-III-Associated Protein ALIX mediates high affinity phosphate transporter trafficking to maintain phosphate homeostasis in Arabidopsis
Plant Cell
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2015
Arabidopsis thaliana
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Muehe, E.; Eisele, J.; Daus, B.; Kappler, A.; Harter, K.; Chaban, C.
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Oryza sativa
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Ren, F.; Zhao, C.Z.; Liu, C.S.; Huang, K.L.; Guo, Q.Q.; Chang, L.L.; Xiong, H.; Li, X.B.
A Brassica napus PHT1 phosphate transporter, BnPht1;4, promotes phosphate uptake and affects roots architecture of transgenic Arabidopsis
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Brassica napus
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Qin, L.; Zhao, J.; Tian, J.; Chen, L.; Sun, Z.; Guo, Y.; Lu, X.; Gu, M.; Xu, G.; Liao, H.
The high-affinity phosphate transporter GmPT5 regulates phosphate transport to nodules and nodulation in soybean
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Glycine max (C3UZD2), Glycine max
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Jia, F.; Wan, X.; Zhu, W.; Sun, D.; Zheng, C.; Liu, P.; Huang, J.
Overexpression of mitochondrial phosphate transporter 3 severely hampers plant development through regulating mitochondrial function in Arabidopsis
PLoS ONE
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Arabidopsis thaliana (Q9FMU6)
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Gonzalez, D.; Richez, M.; Bergonzi, C.; Chabriere, E.; Elias, M.
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Clostridium perfringens (A0A0H2YSI2), Clostridium perfringens
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Characterization of the high-affinity phosphate transporter PHT1;4 gene promoter of Arabidopsis thaliana in transgenic wheat
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Arabidopsis thaliana
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Arabidopsis thaliana (O82390)
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Daryadel, A.; Haykir, B.; Kueng, C.; Bugarski, M.; Bettoni, C.; Schnitzbauer, U.; Hernando, N.; Hall, A.; Wagner, C.
Acute adaptation of renal phosphate transporters in the murine kidney to oral phosphate intake requires multiple signals
Acta Physiol. (Oxf.)
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Mus musculus
brenda
Yang, S.; Feng, Y.; Zhao, Y.; Bai, J.; Wang, J.
Overexpression of a Eutrema salsugineum phosphate transporter gene EsPHT1;4 enhances tolerance to low phosphorus stress in soybean
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2020
Eutrema salsugineum
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Vuppada, R.; Hansen, C.; Strickland, K.; Kelly, K.; McCleary, W.
Phosphate signaling through alternate conformations of the PstSCAB phosphate transporter
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Escherichia coli, Escherichia coli BW25113
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Zhu, X.; Boulet, A.; Buckley, K.; Phillips, C.; Gammon, M.; Oldfather, L.; Moore, S.; Leary, S.; Cobine, P.
Mitochondrial copper and phosphate transporter specificity was defined early in the evolution of eukaryotes
eLife
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Mus musculus (Q8VEM8)
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Ahmad, I.; Rawoof, A.; Islam, K.; Momo, J.; Ramchiary, N.
Identification and expression analysis of phosphate transporter genes and metabolites in response to phosphate stress in Capsicum annuum
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Capsicum annuum
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Liao, Y.; Li, J.; Pan, R.; Chiou, T.
Structur-function analysis reveals amino acid residues of Arabidopsis phosphate transporter AtPHT1;1 crucial for its activity
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Arabidopsis thaliana (Q8VYM2)
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Kelliher, J.; Radin, J.; Grim, K.; Solorzano, P.; Degnan, P.; Kehl-Fie, T.
Acquisition of the phosphate transporter NptA enhances Staphylococcus aureus pathogenesis by improving phosphate uptake in divergent environments
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Staphylococcus aureus (A0A290QKL9), Staphylococcus aureus Newman (A0A290QKL9)
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Sinha, R.; LeVeque, R.; Bowlin, M.; Gray, M.; DiRita, V.
Phosphate transporter PstSCAB of Campylobacter jejuni is a critical determinant of lactate-dependent growth and colonization in chickens
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Campylobacter jejuni, Campylobacter jejuni 81-176
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Zhou, J.; Lu, M.; Zhang, C.; Qu, X.; Liu, Y.; Yang, J.; Yuan, J.
Isolation and functional characterisation of the PHT1 gene encoding a high-affinity phosphate transporter in Camellia oleifera
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2020
Camellia oleifera (W8QHB6)
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Yu, G.; Huang, S.; He, R.; Li, Y.; Cheng, X.
Transgenic rice overexperessing a tomato mitochondrial phosphate transporter, SlMPT3;1, promotes phosphate uptake and increases grain yield
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2018
Solanum lycopersicum (K4BDP2)
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Sun, T.; Zhou, B.; Pei, T.; Meng, H.; Zhang, J.; Ma, F.; Wei, Q.
Phosphate transporter PHT1;7 enhances phosphorus accumulation and improves low phosphorus and drought tolerance
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2021
Malus domestica (A0A6B9RIE8)
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Montenegro, R.; Vieto, S.; Wicki-Emmenegger, D.; Vasquez-Castro, F.; Coronado-Ruiz, C.; Fuentes-Schweizer, P.; Calderon, P.; Pereira, R.; Chavarrixada, M.
The putative phosphate transporter PitB (Pp1373) is involved in tellurite uptake in Pseudomonas putida KT2440
Microbiology
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0000
2021
Pseudomonas putida (Q88N43)
brenda
Luan, M.; Liu, J.; Liu, Y.; Han, X.; Sun, G.; Lan, W.; Luan, S.
Vacuolar phosphate transporter 1 (VPT1) affects arsenate tolerance by regulating phosphate homeostasis in Arabidopsis
Plant Cell Physiol.
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2018
Arabidopsis thaliana
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Liu, F.; Xu, Y.; Han, G.; Wang, W.; Li, X.; Cheng, B.
Identification and functional characterization of a maize phosphate transporter induced by mycorrhiza formation
Plant Cell Physiol.
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2018
Zea mays
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Yang, Z.; Yang, J.; Wang, Y.; Wang, F.; Mao, W.; He, Q.; Xu, J.; Wu, Z.; Mao, C.
Protein phosphatase95 regulates phosphate homeostasis by affecting phosphate transporter trafficking in rice
Plant Cell
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740-757
2020
Oryza sativa Japonica Group
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Liu, X.L.; Wang, L.; Wang, X.W.; Yan, Y.; Yang, X.L.; Xie, M.Y.; Hu, Z.; Shen, X.; Ai, H.; Lin, H.H.; Xu, G.H.; Yang, J.; Sun, S.B.
Mutation of the chloroplast-localized phosphate transporter OsPHT2;1 reduces flavonoid accumulation and UV tolerance in rice
Plant J.
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2020
Oryza sativa Japonica Group
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Amna, S.; Qamar, S.; Turab Naqvi, A.; Al-Huqail, A.; Qureshi, M.
Role of sulfur in combating arsenic stress through upregulation of important proteins, and in-silico analysis to study the interaction between phosphate transporter (PHO1), arsenic and phosphate in spinach
Plant Physiol. Biochem.
157
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2020
Spinacia oleracea (A0A0K9RUE0)
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Luan, M.; Zhao, F.; Han, X.; Sun, G.; Yang, Y.; Liu, J.; Shi, J.; Fu, A.; Lan, W.; Luan, S.
Vacuolar phosphate transporters contribute to systemic phosphate homeostasis vital for reproductive development in Arabidopsis 1
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2019
Arabidopsis thaliana
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Cao, M.; Liu, H.; Zhang, C.; Wang, D.; Liu, X.; Chen, Q.
Functional analysis of stpht1;7, a Solanum tuberosum L. phosphate transporter gene, in growth and drought tolerance
Plants (Basel)
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1384
2020
Solanum tuberosum
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Yang, W.; Baek, D.; Yun, D.; Lee, K.; Hong, S.; Bae, K.; Chung, Y.; Kwon, Y.; Kim, D.; Jung, K.; Kim, D.
Rice OsMYB5P improves plant phosphate acquisition by regulation of phosphate transporter
PLoS ONE
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2018
Oryza sativa, Oryza sativa Dongjin
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Liu, Y.; Li, C.; Gupta, M.; Verma, N.; Johri, A.; Stroud, R.; Voth, G.
Key computational findings reveal proton transfer as driving the functional cycle in the phosphate transporter PiPT
Proc. Natl. Acad. Sci. USA
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2021
Serendipita indica (G4TS85), Serendipita indica DSM 11827 (G4TS85)
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Ruili, L.; Jiaoling, W.; Lei, X.; Meihao, S.; Keke, Y.; Hongyu, Z.
Functional analysis of phosphate transporter OsPHT4 family members in rice
Rice Sci.
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493-503
2020
Oryza sativa Japonica Group, Oryza sativa Japonica Group Shishoubaimao
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Tsai, J.; Chu, C.; Lin, M.; Chou, Y.; Hong, R.; Yen, C.; Hsiao, C.; Sun, Y.
Structure of the sodium-dependent phosphate transporter reveals insights into human solute carrier SLC20
Sci. Adv.
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2020
Thermotoga maritima (Q9WY99), Homo sapiens (Q08357), Thermotoga maritima DSM 3109 (Q9WY99)
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Dong, Z.; Li, W.; Liu, J.; Li, L.; Pan, S.; Liu, S.; Gao, J.; Liu, L.; Liu, X.; Wang, G.; Dai, L.
The rice phosphate transporter protein OsPT8 regulates disease resistance and plant growth
Sci. Rep.
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5408
2019
Oryza sativa Japonica Group (Q8H6G8)
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