Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
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 + acidic amino acid/out
ADP + phosphate + acidic amino acid/in
-
Substrates: crucial role for the uptake of amino acids into the endosperm and supplying the developing embryo with amino acids during early embryogenesis
Products: -
?
ATP + H2O + alpha-aminoadipic acid-[polar amino acid-binding protein][side 1]
ADP + phosphate + alpha-aminoadipic acid[side 2] + [polar amino acid-binding protein][side 1]
ATP + H2O + alpha-aminoisobutyric acid/out
ADP + phosphate + alpha-aminoisobutyric acid/in
-
Substrates: -
Products: -
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
ATP + H2O + betaine/out
ADP + phosphate + betaine/in
ATP + H2O + citrulline/out
ADP + phosphate + citrulline/in
-
Substrates: -
Products: -
?
ATP + H2O + glycine/out
ADP + phosphate + glycine/in
-
Substrates: -
Products: -
?
ATP + H2O + His/out
ADP + phosphate + His/in
ATP + H2O + histidine/out
ADP + phosphate + histidine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-alanine/out
ADP + phosphate + L-alanine/in
ATP + H2O + L-Arg/out
ADP + phosphate + L-Arg/in
ATP + H2O + L-arginine-[L-arginine -binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
ATP + H2O + L-arginine/out
ADP + phosphate + L-arginine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Asp/out
ADP + phosphate + L-Asp/in
ATP + H2O + L-asparagine-[L-asparagine-binding protein][side 1]
ADP + phosphate + L-asparagine[side 2] + [L-asparagine-binding protein][side 1]
ATP + H2O + L-asparagine/out
ADP + phosphate + L-asparagine
-
Substrates: -
Products: -
?
ATP + H2O + L-aspartate-[L-aspartate-binding protein][side 1]
ADP + phosphate + L-aspartate[side 2] + [L-aspartate-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-aspartate/out
ADP + phosphate + L-aspartate/in
ATP + H2O + L-citrulline-[L-citrulline-binding protein][side 1]
ADP + phosphate + L-citrulline[side 2] + [L-citrulline-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-citrulline/out
ADP + phosphate + L-citrulline/in
-
Substrates: -
Products: -
?
ATP + H2O + L-cysteine/out
ADP + phosphate + L-cysteine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Gln/out
ADP + phosphate + L-Gln/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Glu/out
ADP + phosphate + L-Glu/in
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
ATP + H2O + L-glutamate/out
ADP + phosphate + L-glutamate/in
ATP + H2O + L-glutamic acid-[L-glutamic acid-binding protein][side 1]
ADP + phosphate + L-glutamic acid[side 2] + [L-glutamic acid-binding protein][side 1]
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
ATP + H2O + L-glutamine/out
ADP + phosphate + glutamine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamine/out
ADP + phosphate + L-glutamine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
ATP + H2O + L-histidine/out
ADP + phosphate + L-histidine/in
ATP + H2O + L-Leu/out
ADP + phosphate + L-Leu/in
-
Substrates: -
Products: -
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
ATP + H2O + L-Lys/out
ADP + phosphate + L-Lys/in
ATP + H2O + L-lysine-[L-lysine-binding protein][side 1]
ADP + phosphate + L-lysine[side 2] + [L-lysine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
ATP + H2O + L-methionine/out
ADP + phosphate + L-methionine/in
ATP + H2O + L-Orn/out
ADP + phosphate + L-Orn/in
-
Substrates: the histidine-binding protein HisJ binds L-His and L-Arg tightly and L-Lys and L-Orn less tightly
Products: -
?
ATP + H2O + L-ornithine-[L-ornithine-binding protein][side 1]
ADP + phosphate + L-ornithine[side 2] + [L-ornithine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-phenylalanine/out
ADP + phosphate + L-phenylalanine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-threonine/out
ADP + phosphate + L-threonine/in
-
Substrates: -
Products: -
?
ATP + H2O + neutral amino acid/out
ADP + phosphate + neutral amino acid/in
-
Substrates: -
Products: -
?
ATP + H2O + polar amino acid-[polar amino acid-binding protein][side 1]
ADP + phosphate + polar amino acid[side 2] + [polar amino acid-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
ATP + H2O + Pro/out
ADP + phosphate + Pro/in
CTP + H2O + His/out
CDP + phosphate + His/in
-
Substrates: dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 50% of the ATPase activity with ATP
Products: -
?
GTP + H2O + His/out
GDP + phosphate + His/in
-
Substrates: dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 53% of the ATPase activity with ATP
Products: -
?
UTP + H2O + His/out
UDP + phosphate + His/in
-
Substrates: dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 37% of the ATPase activity with ATP
Products: -
?
additional information
?
-
ATP + H2O + alpha-aminoadipic acid-[polar amino acid-binding protein][side 1]
ADP + phosphate + alpha-aminoadipic acid[side 2] + [polar amino acid-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + alpha-aminoadipic acid-[polar amino acid-binding protein][side 1]
ADP + phosphate + alpha-aminoadipic acid[side 2] + [polar amino acid-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
Substrates: acidic and neutral polar amino acid uptake, essential for diazotropic physiology of the bacterium, transports Asp, Glu, Asn, Gln, Met, Thr, Ala, Ser, Gly, and His
Products: -
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
Substrates: essential for basic amino acid uptake, transports Lys, Arg, Orn, His, and Gln
Products: -
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
Substrates: amino acid uptake, catalyzes the transport of all the D- and L-isomers of the amino acids normally found in proteins
Products: -
?
ATP + H2O + betaine/out
ADP + phosphate + betaine/in
-
Substrates: -
Products: -
?
ATP + H2O + betaine/out
ADP + phosphate + betaine/in
-
Substrates: the histidine transport system Hut is also involved in proline and betaine uptake
Products: -
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
Substrates: -
Products: -
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
Substrates: -
Products: -
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
Substrates: -
Products: -
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
Substrates: the histidine transport system Hut is also involved in proline and betaine uptake
Products: -
?
ATP + H2O + L-alanine/out
ADP + phosphate + L-alanine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-alanine/out
ADP + phosphate + L-alanine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-alanine/out
ADP + phosphate + L-alanine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-alanine/out
ADP + phosphate + L-alanine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-alanine/out
ADP + phosphate + L-alanine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Arg/out
ADP + phosphate + L-Arg/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Arg/out
ADP + phosphate + L-Arg/in
-
Substrates: the histidine-binding protein HisJ binds L-His and L-Arg tightly and L-Lys and L-Orn less tightly
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Substrates: preferred amino acid
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-Asp/out
ADP + phosphate + L-Asp/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Asp/out
ADP + phosphate + L-Asp/in
-
Substrates: -
Products: -
?
ATP + H2O + L-asparagine-[L-asparagine-binding protein][side 1]
ADP + phosphate + L-asparagine[side 2] + [L-asparagine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-asparagine-[L-asparagine-binding protein][side 1]
ADP + phosphate + L-asparagine[side 2] + [L-asparagine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-asparagine-[L-asparagine-binding protein][side 1]
ADP + phosphate + L-asparagine[side 2] + [L-asparagine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-aspartate/out
ADP + phosphate + L-aspartate/in
-
Substrates: -
Products: -
?
ATP + H2O + L-aspartate/out
ADP + phosphate + L-aspartate/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Glu/out
ADP + phosphate + L-Glu/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Glu/out
ADP + phosphate + L-Glu/in
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate/out
ADP + phosphate + L-glutamate/in
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate/out
ADP + phosphate + L-glutamate/in
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate/out
ADP + phosphate + L-glutamate/in
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate/out
ADP + phosphate + L-glutamate/in
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate/out
ADP + phosphate + L-glutamate/in
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamic acid-[L-glutamic acid-binding protein][side 1]
ADP + phosphate + L-glutamic acid[side 2] + [L-glutamic acid-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamic acid-[L-glutamic acid-binding protein][side 1]
ADP + phosphate + L-glutamic acid[side 2] + [L-glutamic acid-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
Substrates: the enzyme is specific for glutamine
Products: -
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
-
Substrates: the enzyme is the only transport system for L-glutamine but not for L-glutamic acid and L-asparagine
Products: -
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
-
Substrates: the enzyme is the only transport system for L-glutamine but not for L-glutamic acid and L-asparagine
Products: -
?
ATP + H2O + L-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-histidine/out
ADP + phosphate + L-histidine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-histidine/out
ADP + phosphate + L-histidine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-histidine/out
ADP + phosphate + L-histidine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Lys/out
ADP + phosphate + L-Lys/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Lys/out
ADP + phosphate + L-Lys/in
-
Substrates: the histidine-binding protein HisJ binds L-His and L-Arg tightly and L-Lys and L-Orn less tightly
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
Substrates: -
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
Substrates: -
Products: -
?
ATP + H2O + L-methionine/out
ADP + phosphate + L-methionine/in
-
Substrates: transported to a lesser extent than branched-chain amino acids
Products: -
?
ATP + H2O + L-methionine/out
ADP + phosphate + L-methionine/in
-
Substrates: transported to a lesser extent than branched-chain amino acids
Products: -
?
ATP + H2O + L-methionine/out
ADP + phosphate + L-methionine/in
-
Substrates: -
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
Substrates: -
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
Substrates: -
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
Substrates: Ser388 and Val389 are exposed into the amino acid binding site for transport, also used by agonist action for signaling
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
Substrates: -
Products: -
?
ATP + H2O + Pro/out
ADP + phosphate + Pro/in
-
Substrates: -
Products: -
?
ATP + H2O + Pro/out
ADP + phosphate + Pro/in
-
Substrates: the histidine transport system Hut is also involved in proline and betaine uptake
Products: -
?
additional information
?
-
Substrates: no activity with betaine, gamma-aminobutyric acid, and taurine
Products: -
?
additional information
?
-
-
Substrates: no activity with betaine, gamma-aminobutyric acid, and taurine
Products: -
?
additional information
?
-
Substrates: the enzyme also generates significant inward currents for neutral aliphatic (Ile, Leu, Met), aromatic (Phe, Trp, Tyr) and even acidic amino acids
Products: -
?
additional information
?
-
-
Substrates: the enzyme also generates significant inward currents for neutral aliphatic (Ile, Leu, Met), aromatic (Phe, Trp, Tyr) and even acidic amino acids
Products: -
?
additional information
?
-
Substrates: the enzyme transports essential cationic and neutral amino acids with preference for L-arginine
Products: -
?
additional information
?
-
-
Substrates: the enzyme transports essential cationic and neutral amino acids with preference for L-arginine
Products: -
?
additional information
?
-
-
Substrates: LHT1 displays high affinity for neutral amino acids, L-His, and acidic amino acids. Amino acid permease 1 mediates uptake of several neutral amino acids as well as L-Glu and L-His but, similar to LHT1, activity for L-Arg and L-Lys is not detected
Products: -
?
additional information
?
-
-
Substrates: LHT1 displays high affinity for neutral amino acids, L-His, and acidic amino acids. Amino acid permease 1 mediates uptake of several neutral amino acids as well as L-Glu and L-His but, similar to LHT1, activity for L-Arg and L-Lys is not detected
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the transmembrane transport of single amino acid, multiple amino acids, auxin (indole-3-acetic acid) or gamma-aminobutyric acid
Products: -
?
additional information
?
-
-
Substrates: broad specificity for polar amino acids
Products: -
?
additional information
?
-
-
Substrates: broad specificity for polar amino acids
Products: -
?
additional information
?
-
-
Substrates: 1H, 13C, and 15N backbone resonance assignments for apo HisJ and holo HisJ from Escherichia coli. Structural information about the interactions between HisJ and HisQM and to clarify the mechanism of the histidine transfer from the periplasm to the cytoplasm
Products: -
?
additional information
?
-
-
Substrates: specifically transports branched-chain amino acids
Products: -
?
additional information
?
-
-
Substrates: specifically transports branched-chain amino acids
Products: -
?
additional information
?
-
Substrates: specificity of L-lysine transport in wild-type cells and in recombinantly parasite AAP7 expressing yeast 22DELTA7AA cells, overview
Products: -
?
additional information
?
-
-
Substrates: specificity of L-lysine transport in wild-type cells and in recombinantly parasite AAP7 expressing yeast 22DELTA7AA cells, overview
Products: -
?
additional information
?
-
-
Substrates: broad specificity for polar amino acids
Products: -
?
additional information
?
-
-
Substrates: contributes to the alpha-aminoadipic acid flux
Products: -
?
additional information
?
-
-
Substrates: contributes to the alpha-aminoadipic acid flux
Products: -
?
additional information
?
-
-
Substrates: broad specificity for polar amino acids
Products: -
?
additional information
?
-
-
Substrates: broad specificity for polar amino acids
Products: -
?
additional information
?
-
-
Substrates: broad specificity for polar amino acids
Products: -
?
additional information
?
-
-
Substrates: Gap1 is a transporting amino acid transceptor that triggers the activation of the protein kinase A pathway
Products: -
?
additional information
?
-
-
Substrates: Gap1p transports all naturally occurring amino acids
Products: -
?
additional information
?
-
-
Substrates: the GTG motif of Gap1p is involved in amino acid binding
Products: -
?
additional information
?
-
-
Substrates: broad specificity for polar amino acids
Products: -
?
additional information
?
-
Substrates: specificity of L-lysine transport in wild-type cells, overview
Products: -
?
additional information
?
-
-
Substrates: specificity of L-lysine transport in wild-type cells, overview
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + acidic amino acid/out
ADP + phosphate + acidic amino acid/in
-
Substrates: crucial role for the uptake of amino acids into the endosperm and supplying the developing embryo with amino acids during early embryogenesis
Products: -
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
ATP + H2O + His/out
ADP + phosphate + His/in
-
Substrates: the histidine transport system Hut is also involved in proline and betaine uptake
Products: -
?
ATP + H2O + histidine/out
ADP + phosphate + histidine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Arg/out
ADP + phosphate + L-Arg/in
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine -binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
ATP + H2O + L-Asp/out
ADP + phosphate + L-Asp/in
ATP + H2O + L-asparagine-[L-asparagine-binding protein][side 1]
ADP + phosphate + L-asparagine[side 2] + [L-asparagine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-Gln/out
ADP + phosphate + L-Gln/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Glu/out
ADP + phosphate + L-Glu/in
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
ATP + H2O + L-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
ATP + H2O + L-Lys/out
ADP + phosphate + L-Lys/in
-
Substrates: -
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
ATP + H2O + polar amino acid-[polar amino acid-binding protein][side 1]
ADP + phosphate + polar amino acid[side 2] + [polar amino acid-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
additional information
?
-
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
Substrates: acidic and neutral polar amino acid uptake, essential for diazotropic physiology of the bacterium, transports Asp, Glu, Asn, Gln, Met, Thr, Ala, Ser, Gly, and His
Products: -
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
Substrates: essential for basic amino acid uptake, transports Lys, Arg, Orn, His, and Gln
Products: -
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
Substrates: amino acid uptake, catalyzes the transport of all the D- and L-isomers of the amino acids normally found in proteins
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-Asp/out
ADP + phosphate + L-Asp/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Asp/out
ADP + phosphate + L-Asp/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Glu/out
ADP + phosphate + L-Glu/in
-
Substrates: -
Products: -
?
ATP + H2O + L-Glu/out
ADP + phosphate + L-Glu/in
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamate-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
Substrates: the enzyme is specific for glutamine
Products: -
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
-
Substrates: -
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
-
Substrates: -
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
Substrates: -
Products: -
?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
Substrates: -
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
Substrates: -
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
Substrates: -
Products: -
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: 1H, 13C, and 15N backbone resonance assignments for apo HisJ and holo HisJ from Escherichia coli. Structural information about the interactions between HisJ and HisQM and to clarify the mechanism of the histidine transfer from the periplasm to the cytoplasm
Products: -
?
additional information
?
-
-
Substrates: Gap1 is a transporting amino acid transceptor that triggers the activation of the protein kinase A pathway
Products: -
?
additional information
?
-
-
Substrates: Gap1p transports all naturally occurring amino acids
Products: -
?
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
W653C
-
decreased ATP-dependent LTC4 transport
W653Y
-
higher transport activity than wild-type enzyme
Y1302C
-
decreased ATP-dependent LTC4 transport
Y1302W
-
no effect of ATP binding and hydrolysis
A297V
-
site-directed mutagenesis, the catalytically inactive mutant does not respond to complex amino acid mixtures and constitutively sorts Gap1p to the plasma membrane. The mutant shows reduced activity with altered specificity compared to the wild-type enzyme and does not transport basic amino acids, its trafficking is also not regulated by these amino acids. The mutant has a specific defect in transport of positively charged amino acids
I394
-
site-directed mutagenesis, the mutation strongly affects both transport and signaling with citrulline and other amino acids
K9R/K16R
-
site-directed mutagenesis, the mutant shows reduced activity with altered specificity compared to the wild-type enzyme
K9R/K16R/A297V
-
site-directed mutagenesis, the mutant shows reduced activity with altered specificity compared to the wild-type enzyme
S392C
-
site-directed mutagenesis, the mutation strongly affects both transport and signaling with citrulline and other amino acids
T106K
-
site-directed mutagenesis, the GTG motif mutant enzyme localized to the plasma membrane normally
V386C
-
site-directed mutagenesis, the mutation strongly affects both transport and signaling with citrulline and other amino acids
V402C
-
site-directed mutagenesis, the mutation strongly affects both transport and signaling with citrulline and other amino acids
Y395C
-
site-directed mutagenesis, the mutation strongly affects both transport and signaling with citrulline and other amino acids
D149A
-
mutation in histidine binding subunit HisJ, mutant protein is capable of interacting with HisQMP2 although at a much reduced level
D149N
-
mutation in histidine binding subunit HisJ, mutant protein is capable of interacting with HisQMP2 although at a much reduced level
D61N
-
mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis
E191K
-
mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme. Increased intrinsic ATPase activity without HisJ
E202K
-
mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme. Increased intrinsic ATPase activity without HisJ
H211R
-
mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis
K45P
-
mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis
R154D
-
mutation in histidine binding subunit HisJ, binds His as well as the wild type, defective in transport
R154S
-
mutation in histidine binding subunit HisJ, binds His as well as the wild type, defective in transport
T205A
-
mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme
P172T
-
-
P172T
-
mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme
P172T
-
increased intrinsic ATPase activity without HisJ
T205M
-
mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme
T205M
-
increased intrinsic ATPase activity without HisJ
additional information
-
overexpression of LHT1 in Arabidopsis thaliana results in increased uptake, with uptake rates of between 219 and 456% of wild-type uptake, and saturating kinetics for L-Gln and increased but linear kinetics for L-Ala, L-Asp and L-Glu, in comparison to the wild-type plant. In the LHT1 mutant, uptake of L-Gln, L-Ala, L-Glu and L-Asp is greatly reduced by on average 61-85% over the entire concentration range, while the uptake of L-Arg and L-Lys is unaffected. AAP1 mutants do not display any major differences in the uptake of any of the amino acids tested
additional information
-
overexpression of LHT1 in Arabidopsis thaliana results in increased uptake, with uptake rates of between 219 and 456% of wild-type uptake, and saturating kinetics for L-Gln and increased but linear kinetics for L-Ala, L-Asp and L-Glu, in comparison to the wild-type plant. In the LHT1 mutant, uptake of L-Gln, L-Ala, L-Glu and L-Asp is greatly reduced by on average 61-85% over the entire concentration range, while the uptake of L-Arg and L-Lys is unaffected. AAP1 mutants do not display any major differences in the uptake of any of the amino acids tested
-
additional information
-
deletion of BcaP results in the loss of most of the branched-chain amino acids uptake acitivity, and predominantely affects genes belonging to the regulons of the transcriptional regulator CodY, which is involved in global nitrogen metabolism, and of CmbR, which is involved in sulfur amino acid metabolism
additional information
-
deletion of BcaP results in the loss of most of the branched-chain amino acids uptake acitivity, and predominantely affects genes belonging to the regulons of the transcriptional regulator CodY, which is involved in global nitrogen metabolism, and of CmbR, which is involved in sulfur amino acid metabolism
-
additional information
-
deletion of gap1delta and agp1delta from the wild-type strain does not alter carbon catabolite repression induced increase in L-leucine uptake, deletion of further amino acid permeases reduces the increase in L-leucine uptake 36% in gnp1delta, 62% in bap2delta and 83% in deltabap2-tat1, deletion of TOR1, which regulates cellular response to changes in nitrogen availibility, from the wild-type abolishes the carbon catabolite repression-induced amino acid uptake
additional information
-
Gap1p mutants, deficient in transport of a subset of amino acids, show that Gap1p inactivation at the plasma membrane does not depend on the presence of either extracellular or intracellular amino acids, but does require active amino acid transport by Gap1p
additional information
-
mutants defective in Gap1p polyubiquitination and class E vps mutants show highly increased levels of active Gap1p, but only class E vps mutants can respond normally to high external and internal amino acid concentrations by redirecting Gap1p away from the plasma membrane to the vacuolar targeting pathway, LST4 or LST7 mutations block Gap1p traffic to the plasma membrane
additional information
-
construction of a gap1 mutant of a wine strain, fermentation rate, biomass production and nitrogen consumption of the gap1 mutant compared to its parental strain during fermentations with different nitrogen concentrations shows that the fermentation capacity of the gap1 mutant strain is impaired in the nitrogen-limited and -excessive conditions. The nitrogen consumption rates of wild-type strain and mutant are different for some amino acids, especially those affected by nitrogen catabolite repression, NCR. The deletion of GAP1 gene also modifies the gene expression of other permeases, phenotype, overview
additional information
-
mutation of each of the amino acid residues V381, I382, L383, I384, A385, L387, S388, V389, G390, N391, A393, A396, S398, R399, T400, M401, A403, l404, and A405 to cysteine does not affect transport or signaling by the enzyme
additional information
-
generation of 47 mutant proteins reaching the plasma membrane normally, of two that are unstable and rapidly down-regulated even when the nitrogen source is poor. Six other mutants are totally inactive and another four, altered in a 16-amino-acid sequence in the N-terminal tail, are resistant to ammonium-induced down-regulation. Finally, a mutation in L6 causes missorting of Gap1 from the secretory pathway to the vacuole. Detailed overview
additional information
-
mutations in the ATP-binding subunit that allow ligand translocation and ATP hydrolysis in the absence of the binding protein
additional information
-
binding protein-independent mutants
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hobson, A.C.; Weatherwax, R.; Ferru-Luzzi Ames, G.
ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system
Proc. Natl. Acad. Sci. USA
81
7333-7337
1984
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Liu, C.E.; Liu, P.Q.; Ames, G.F.
Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter)
J. Biol. Chem.
272
21883-21891
1997
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Boncompagni, E.; Dupont, L.; Mignot, T.; Osteraes, M.; Lambert, A.; Poggi, M.C.; Le Rudulier, D.
Characterization of a Sinorhizobium meliloti ATP-binding cassette histidine transporter also involved in betaine and proline uptake
J. Bacteriol.
182
3717-3725
2000
Sinorhizobium meliloti
brenda
Liu, P.Q.; Ferro-Luzzi Ames, G.
In vitro disassembly and reassembly by an ABC transporter, the histidine permease
Proc. Natl. Acad. Sci. USA
95
3495-3500
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Liu, P.Q.; Liu, C.E.; Ferro-Luzzi Ames, G.
Modulation of ATPase activity by physical disengagement of the ATP-binding domains of an ABC transporter, the histidine permease
J. Biol. Chem.
274
18310-18318
1999
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Liu, C.E.; Liu, P.Q.; Wolf, A.; Lin, E.; Ferro-Luzzi Ames, G.
Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex
J. Biol. Chem.
274
739-747
1999
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Nikaido, K.; Liu, P.Q.; Ferro-Luzzi Ames, G.
Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium
J. Biol. Chem.
272
27745-27752
1997
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Liu, C.E.; Ferro-Luzzi Ames, G.
Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis
J. Biol. Chem.
272
859-866
1997
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Petronilli, V.; Ferro-Luzzi Ames, G.
Binding protein-independent histidine permease mutants
J. Biol. Chem.
266
16293-16296
1991
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kreimer, D.I.; Malak, H.; Lakowicz, J.R.; Trakhanov, S.; Villar, E.; Shnyrov, V.L.
Thermodynamics and dynamics of histidine-binding protein, the water-soluble receptor of histidine permease
Eur. J. Biochem.
267
4242-4252
2000
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Walshaw, D.L.; Lowthorpe, S.; East, A.; Poole, P.S.
Distribution of a sub-class of bacterial ABC polar amino acid transporter and identification of an N-terminal region involved in solute specificity
FEBS Lett.
414
397-401
1997
Citrobacter freundii, Escherichia coli, Pectobacterium carotovorum, Pseudomonas fluorescens, Rhizobium leguminosarum, Sinorhizobium meliloti, Rhodobacter capsulatus
brenda
Hung, L.W.; Wang, I.X.; Nikaido, K.; Liu, P.Q.; Ferro-Luzzi, G.; Kim, S.H.
Crystal structure of the ATP-binding subunit of an ABC transporter
Nature
396
703-707
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Hosie, A.H.F.; Allaway, D.; Galloway, C.S.; Dunsby, H.A.; Poole, P.S.
Rhizobium leguminosarum has a second general amino acid permease with unusually broad substrate specificity and high similarity to branched-chain amino acid transporters (Bra/LIV) of the ABC family
J. Bacteriol.
184
4071-4080
2002
Rhizobium leguminosarum
brenda
Zhao, Q.; Chang, X-b.
Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein MRP1
J. Biol. Chem.
279
48505-48512
2004
Homo sapiens
brenda
Trip, H.; Evers, M.E.; Kiel, J.A.; Driessen, A.J.
Uptake of the b-lactam precursor a-aminoadipic acid in Penicillium chrysogenum is mediated by the acidic and the general amino acid permease
Appl. Environ. Microbiol.
70
4775-4783
2004
Penicillium chrysogenum, Penicillium chrysogenum Wisconsin 54-1255
brenda
Akerman, M.; Shaked-Mishan, P.; Mazareb, S.; Volpin, H.; Zilberstein, D.
Novel motifs in amino acid permease genes from Leishmania
Biochem. Biophys. Res. Commun.
325
353-366
2004
Leishmania donovani
brenda
Trip, H.; Evers, M.E.; Driessen, A.J.
PcMtr, an aromatic and neutral aliphatic amino acid permease of Penicillium chrysogenum
Biochim. Biophys. Acta
1667
167-173
2004
Penicillium chrysogenum, Penicillium chrysogenum Wisconsin 54-1255
brenda
Campbell, J.D.; Deol, S.S.; Ashcroft, F.M.; Kerr, I.D.; Sansom, M.S.
Nucleotide-dependent conformational changes in HisP: Molecular dynamics simulations of an ABC transporter nucleotide-binding domain
Biophys. J.
87
3703-3715
2004
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
den Hengst, C.D.; Groeneveld, M.; Kuipers, O.P.; Kok, J.
Identification and functional characterization of the Lactococcus lactis CodY-regulated branched-chain amino acid permease BcaP (CtrA)
J. Bacteriol.
188
3280-3289
2006
Lactococcus lactis, Lactococcus lactis MG1361 derivates
brenda
Peter, G.J.; Duering, L.; Ahmed, A.
Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway
J. Biol. Chem.
281
5546-5552
2006
Saccharomyces cerevisiae
brenda
Rubio-Texeira, M.; Kaiser, C.A.
Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway
Mol. Biol. Cell
17
3031-3050
2006
Saccharomyces cerevisiae
brenda
Risinger, A.L.; Cain, N.E.; Chen, E.J.; Kaiser, C.A.
Activity-dependent reversible inactivation of the general amino acid permease
Mol. Biol. Cell
17
4411-4419
2006
Saccharomyces cerevisiae
brenda
Struck, C.; Mueller, E.; Martin, H.; Lohaus, G.
The Uromyces fabae UfAAT3 gene encodes a general amino acid permease that prefers uptake of in planta scarce amino acids
Mol. Plant Pathol.
5
183-189
2004
Uromyces viciae-fabae
brenda
Gao, M.; Kaiser, C.A.
A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast
Nat. Cell Biol.
8
657-667
2006
Saccharomyces cerevisiae
brenda
Rolletschek, H.; Hosein, F.; Miranda, M.; Heim, U.; Goetz, K.; Schlereth, A.; Borisjuk, L.; Saalbach, I.; Wobus, U.; Weber, H.
Ectopic expression of an amino acid transporter (VfAAP1) in seeds of Vicia narbonensis and pea increases storage proteins
Plant Physiol.
137
1236-1249
2005
Vicia faba
brenda
Alonso, M.; Burgos, H.I.; Pannunzio, V.; Hughes, A.M.; Mattoon, J.R.; Stella, C.A.
Brefeldin A decreases the activity of the general amino acid permease (GAP1) and the more specific systems for L-leucine uptake in Saccharomyces cerevisiae
Cell. Mol. Biol. Lett.
11
256-263
2006
Saccharomyces cerevisiae
brenda
Pernil, R.; Picossi, S.; Mariscal, V.; Herrero, A.; Flores, E.
ABC-type amino acid uptake transporters Bgt and N-II of Anabaena sp. strain PCC 7120 share an ATPase subunit and are expressed in vegetative cells and heterocysts
Mol. Microbiol.
67
1067-1080
2008
Anabaena sp.
brenda
Schmidt, R.; Stransky, H.; Koch, W.
The amino acid permease AAP8 is important for early seed development in Arabidopsis thaliana
Planta
226
805-813
2007
Arabidopsis thaliana
brenda
Chiva, R.; Baiges, I.; Mas, A.; Guillamon, J.M.
The role of GAP1 gene in the nitrogen metabolism of Saccharomyces cerevisiae during wine fermentation
J. Appl. Microbiol.
107
235-244
2009
Saccharomyces cerevisiae
brenda
Van Zeebroeck, G.; Bonini, B.M.; Versele, M.; Thevelein, J.M.
Transport and signaling via the amino acid binding site of the yeast Gap1 amino acid transceptor
Nat. Chem. Biol.
5
45-52
2009
Saccharomyces cerevisiae
brenda
Igarashi, S.; Osawa, M.; Ozawa, S.; Shimada, I.
Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states
Biomol. NMR Assign.
4
17-20
2010
Escherichia coli
brenda
Inbar, E.; Canepa, G.E.; Carrillo, C.; Glaser, F.; Suter Grotemeyer, M.; Rentsch, D.; Zilberstein, D.; Pereira, C.A.
Lysine transporters in human trypanosomatid pathogens
Amino Acids
42
347-360
2012
Leishmania donovani (Q208R5), Leishmania donovani, Trypanosoma cruzi (Q4DMS3), Trypanosoma cruzi
brenda
Kraidlova, L.; Van Zeebroeck, G.; Van Dijck, P.; Sychrova, H.
The Candida albicans GAP gene family encodes permeases involved in general and specific amino acid uptake and sensing
Eukaryot. Cell
10
1219-1229
2011
Candida albicans
brenda
Ruiz, J.; Haneburger, I.; Jung, K.
Identification of ArgP and Lrp as transcriptional regulators of lysP, the gene encoding the specific lysine permease of Escherichia coli
J. Bacteriol.
193
2536-2548
2011
Escherichia coli
brenda
Cain, N.E.; Kaiser, C.A.
Transport activity-dependent intracellular sorting of the yeast general amino acid permease
Mol. Biol. Cell
22
1919-1929
2011
Saccharomyces cerevisiae
brenda
Svennerstam, H.; Jaemtgard, S.; Ahmad, I.; Huss-Danell, K.; Naesholm, T.; Ganeteg, U.
Transporters in Arabidopsis roots mediating uptake of amino acids at naturally occurring concentrations
New Phytol.
191
459-467
2011
Arabidopsis thaliana, Arabidopsis thaliana Col-0
brenda
Merhi, A.; Gerard, N.; Lauwers, E.; Prevost, M.; Andre, B.
Systematic mutational analysis of the intracellular regions of yeast Gap1 permease
PLoS ONE
6
e18457
2011
Saccharomyces cerevisiae
brenda
Huseinovic, A.; Dekker, S.J.; Boogaard, B.; Vermeulen, N.P.E.; Kooter, J.M.; Vos, J.C.
Acetaminophen reduces the protein levels of high affinity amino acid permeases and causes tryptophan depletion
Amino Acids
50
1377-1390
2018
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Price, D.R.; Wilson, A.C.; Luetje, C.W.
Proton-dependent glutamine uptake by aphid bacteriocyte amino acid transporter ApGLNT1
Biochim. Biophys. Acta
1848
2085-2091
2015
Acyrthosiphon pisum (F8RL01), Acyrthosiphon pisum
brenda
Li, Y.; Han, H.; Yin, J.; Zheng, J.; Zhu, X.; Li, T.; Yin, Y.
Effects of glutamate and aspartate on growth performance, serum amino acids, and amino acid transporters in piglets
Food Agric. Immunol.
29
675-687
2018
Sus scrofa (A8HG48), Sus scrofa (F1S025), Sus scrofa (Q5DT24)
-
brenda
Yang, H.; Stierhof, Y.D.; Ludewig, U.
The putative cationic amino acid transporter 9 is targeted to vesicles and may be involved in plant amino acid homeostasis
Front. Plant Sci.
6
212
2015
Arabidopsis thaliana
brenda
Xia, J.; Yang, Z.; Gong, C.; Xie, W.; Pan, H.; Guo, Z.; Zheng, H.; Yang, X.; Sun, X.; Kang, S.; Yang, F.; Wu, Q.; Wang, S.; Cong, B.; Teng, X.; Zhang, Y.
Genome-wide identification and expression analysis of amino acid transporters in the whitefly, Bemisia tabaci (Gennadius)
Int. J. Biol. Sci.
13
735-747
2017
Bemisia tabaci
brenda
Escudero, L.; Mariscal, V.; Flores, E.
Functional dependence between septal protein SepJ from Anabaena sp. strain PCC 7120 and an amino acid ABC-Type uptake transporter
J. Bacteriol.
197
2721-2730
2015
Synechococcus elongatus, Nostoc sp. PCC 7120 = FACHB-418, Synechococcus elongatus PCC 7942
brenda
Fulyani, F.; Schuurman-Wolters, G.; Slotboom, D.; Poolman, B.
Relative rates of amino acid import via the ABC transporter GlnPQ determine the growth performance of Lactococcus lactis
J. Bacteriol.
198
477-485
2015
Lactococcus lactis, Lactococcus lactis NZ9000
brenda
Garneau, M.G.; Tan, Q.; Tegeder, M.
Function of pea amino acid permease AAP6 in nodule nitrogen metabolism and export, and plant nutrition
J. Exp. Bot.
69
5205-5219
2018
Pisum sativum
brenda
Boudko, D.Y.; Tsujimoto, H.; Rodriguez, S.D.; Meleshkevitch, E.A.; Price, D.P.; Drake, L.L.; Hansen, I.A.
Substrate specificity and transport mechanism of amino-acid transceptor Slimfast from Aedes aegypti
Nat. Commun.
6
8546
2015
Aedes aegypti (Q16N01), Aedes aegypti
brenda
Mueller, K.E.; Zampieri, R.A.; Aoki, J.I.; Muxel, S.M.; Nerland, A.H.; Floeter-Winter, L.M.
Amino acid permease 3 (aap3) coding sequence as a target for Leishmania identification and diagnosis of leishmaniases using high resolution melting analysis
Parasit. Vectors
11
421
2018
Leishmania amazonensis, Leishmania braziliensis, Leishmania major, Leishmania mexicana, Leishmania tropica, Leishmania guyanensis, Leishmania lainsoni, Leishmania naiffi, Leishmania shawi, Leishmania infantum (A4I6I1), Leishmania donovani (Q86G79)
brenda
Ganeteg, U.; Ahmad, I.; Jaemtgard, S.; Aguetoni-Cambui, C.; Inselsbacher, E.; Svennerstam, H.; Schmidt, S.; Naesholm, T.
Amino acid transporter mutants of Arabidopsis provides evidence that a non-mycorrhizal plant acquires organic nitrogen from agricultural soil
Plant Cell Environ.
40
413-423
2017
Arabidopsis thaliana
brenda
Aoki, J.I.; Muxel, S.M.; Zampieri, R.A.; Acuna, S.M.; Fernandes, J.C.R.; Vanderlinde, R.H.; Sales, M.C.O.P.; Floeter-Winter, L.M.
L-arginine availability and arginase activity Characterization of amino acid permease 3 in Leishmania amazonensis
PLoS Negl. Trop. Dis.
11
e0006025
2017
Leishmania amazonensis, Leishmania amazonensis MHOM/BR/1973/2269
brenda
Pfannmueller, A.; Wagner, D.; Sieber, C.; Schoenig, B.; Boeckstaens, M.; Marini, A.M.; Tudzynski, B.
The general amino acid permease FfGap1 of Fusarium fujikuroi is sorted to the vacuole in a nitrogen-dependent, but Npr1 kinase-independent manner
PLoS ONE
10
e0125487
2015
Fusarium fujikuroi, Fusarium fujikuroi IMI58289
brenda