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Information on EC 7.4.2.1 - ABC-type polar-amino-acid transporter
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7.4.2.1 ABC-type polar-amino-acid transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of polar amino acids. This entry comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
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Word Map
- 7.4.2.1
-
excitatory
-
l-type
- oocytes
- synaptic
- xenopus
- astrocyte
- l-arginine
- na+
-
neurotransmitter
- glial
-
glutamatergic
- vesicular
-
eaats
- rapamycin
- laevis
- slc7a5
-
blood-brain
-
basolateral
-
mtorc1
-
excitotoxicity
-
na+-independent
-
intolerance
- cystine
-
cotransporter
- l-glutamate
- l-leucine
-
gabaergic
- l-lysine
-
neurotransmission
-
ecotropic
-
sodium-coupled
- l-proline
-
sodium-independent
-
proton-coupled
-
monocarboxylate
-
dibasic
-
antiporter
-
electrogenic
-
two-electrode
-
symporter
-
transporter-1
-
transporter-mediated
-
na+-coupled
- proteinosis
-
vglut1
-
glycinergic
- medicine
- l-arg
-
inward-facing
-
microvillous
- rsp5
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
+
=
+
+
+
+
+
polar amino acid-[polar amino acid-binding protein][side 1]
=
+
+
polar amino acid[side 2]
+
[polar amino acid-binding protein][side 1]
Synonyms
amino acid transporter, slc7a7, amino acid permease, general amino acid permease, gap1p, slc7a1, slc6a19, histidine permease, glnpq, amino acid/auxin permease, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAP
AAP1
aap3
AAP7
ABC-type transporter for polar amino acids
amino acid permease
amino acid permease 1
amino acid permease 3
ATP phosphohydrolase (polar-amino-acid-importing
-
-
-
-
ATP-binding-cassette type transporter for polar amino acids
BcaP
branched-chain amino acid permease
CTRA
DmeA
EC 3.6.3.21
-
-
formerly
-
FFUJ_09118
GAP1
general amino acid permease
GlnPQ
Hip1
HisP
histidine permease
LHT1
lysine histidine transporter 1
lysine permease
lysine-specific permease
PcGap1
polar-amino-acid-transporting ATPase
-
-
-
-
additional information
-
displays also EC 3.6.3.21 /nonpolar-amino-acid-transporting ATPase activity
ATP-binding-cassette type transporter for polar amino acids
-
-
general amino acid permease
-
catalyzes the transport of all the D- and L-isomers of the amino acids normally found in proteins
HisP
-
-
-
-
histidine permease
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydroloysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, polar-amino-acid-importing)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. The enzyme, found in bacteria, interacts with an extracytoplasmic substrate binding protein and mediates the import of polar amino acids. This entry comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + acidic amino acid/out
ADP + phosphate + acidic amino acid/in
-
crucial role for the uptake of amino acids into the endosperm and supplying the developing embryo with amino acids during early embryogenesis
-
-
?
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
-
-
-
-
?
ATP + H2O + citrulline/out
ADP + phosphate + citrulline/in
-
-
-
-
?
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-[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
-
-
-
-
?
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-aspartate-[L-aspartate-binding protein][side 1]
ADP + phosphate + L-aspartate[side 2] + [L-aspartate-binding protein][side 1]
-
-
-
?
ATP + H2O + L-citrulline-[L-citrulline-binding protein][side 1]
ADP + phosphate + L-citrulline[side 2] + [L-citrulline-binding protein][side 1]
-
-
-
?
ATP + H2O + L-citrulline/out
ADP + phosphate + L-citrulline/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-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-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
ATP + H2O + L-lysine-[L-lysine-binding protein][side 1]
ADP + phosphate + L-lysine[side 2] + [L-lysine-binding protein][side 1]
-
-
-
?
ATP + H2O + L-Orn/out
ADP + phosphate + L-Orn/in
-
the histidine-binding protein HisJ binds L-His and L-Arg tightly and L-Lys and L-Orn less tightly
-
?
ATP + H2O + L-ornithine-[L-ornithine-binding protein][side 1]
ADP + phosphate + L-ornithine[side 2] + [L-ornithine-binding protein][side 1]
-
-
-
?
ATP + H2O + L-phenylalanine/out
ADP + phosphate + L-phenylalanine/in
-
-
-
-
?
ATP + H2O + L-threonine/out
ADP + phosphate + L-threonine/in
-
-
-
-
?
ATP + H2O + neutral amino acid/out
ADP + phosphate + neutral amino acid/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]
-
-
-
-
?
CTP + H2O + His/out
CDP + phosphate + His/in
-
dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 50% of the ATPase activity with ATP
-
?
GTP + H2O + His/out
GDP + phosphate + His/in
-
dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 53% of the ATPase activity with ATP
-
?
UTP + H2O + His/out
UDP + phosphate + His/in
-
dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 37% of the ATPase activity with ATP
-
?
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-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 + amino acid/out
ADP + phosphate + amino acid/in
-
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
-
-
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
essential for basic amino acid uptake, transports Lys, Arg, Orn, His, and Gln
-
-
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
amino acid uptake, catalyzes the transport of all the D- and L-isomers of the amino acids normally found in proteins
-
-
?
ATP + H2O + betaine/out
ADP + phosphate + betaine/in
-
the histidine transport system Hut is also involved in proline and betaine uptake
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
the histidine transport system Hut is also involved in proline and betaine uptake
-
?
ATP + H2O + L-alanine/out
ADP + phosphate + L-alanine/in
-
-
-
-
?
ATP + H2O + L-Arg/out
ADP + phosphate + L-Arg/in
-
the histidine-binding protein HisJ binds L-His and L-Arg tightly and L-Lys and L-Orn less tightly
-
?
ATP + H2O + L-arginine-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
preferred amino acid
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Leishmania amazonensis MHOM/BR/1973/2269
-
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
-
?
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-[L-asparagine-binding protein][side 1]
ADP + phosphate + L-asparagine[side 2] + [L-asparagine-binding protein][side 1]
-
-
-
-
?
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-aspartate/out
ADP + phosphate + L-aspartate/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-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
-
-
-
?
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-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
-
-
?
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-[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-glutamate/out
ADP + phosphate + L-glutamate/in
-
-
-
-
?
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-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]
the enzyme is specific for glutamine
-
-
?
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-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-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-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
-
the enzyme is the only transport system for L-glutamine but not for L-glutamic acid and L-asparagine
-
-
?
ATP + H2O + L-glutamine-[L-glutamine-binding protein][side 1]
ADP + phosphate + L-glutamine[side 2] + [L-glutamine-binding protein][side 1]
-
the enzyme is the only transport system for L-glutamine but not for L-glutamic acid and L-asparagine
-
-
?
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-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-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-histidine/out
ADP + phosphate + L-histidine/in
-
-
-
-
?
ATP + H2O + L-histidine/out
ADP + phosphate + L-histidine/in
-
-
-
-
?
ATP + H2O + L-Lys/out
ADP + phosphate + L-Lys/in
-
the histidine-binding protein HisJ binds L-His and L-Arg tightly and L-Lys and L-Orn less tightly
-
?
ATP + H2O + L-methionine/out
ADP + phosphate + L-methionine/in
-
transported to a lesser extent than branched-chain amino acids
-
-
?
ATP + H2O + L-methionine/out
ADP + phosphate + L-methionine/in
-
transported to a lesser extent than branched-chain amino acids
-
-
?
ATP + H2O + L-methionine/out
ADP + phosphate + L-methionine/in
-
-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
Ser388 and Val389 are exposed into the amino acid binding site for transport, also used by agonist action for signaling
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
?
ATP + H2O + Pro/out
ADP + phosphate + Pro/in
-
the histidine transport system Hut is also involved in proline and betaine uptake
-
?
additional information
?
-
no activity with betaine, gamma-aminobutyric acid, and taurine
-
-
?
additional information
?
-
-
no activity with betaine, gamma-aminobutyric acid, and taurine
-
-
?
additional information
?
-
the enzyme also generates significant inward currents for neutral aliphatic (Ile, Leu, Met), aromatic (Phe, Trp, Tyr) and even acidic amino acids
-
-
?
additional information
?
-
-
the enzyme also generates significant inward currents for neutral aliphatic (Ile, Leu, Met), aromatic (Phe, Trp, Tyr) and even acidic amino acids
-
-
?
additional information
?
-
the enzyme transports essential cationic and neutral amino acids with preference for L-arginine
-
-
?
additional information
?
-
-
the enzyme transports essential cationic and neutral amino acids with preference for L-arginine
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme catalyzes the transmembrane transport of single amino acid, multiple amino acids, auxin (indole-3-acetic acid) or gamma-aminobutyric acid
-
-
?
additional information
?
-
-
broad specificity for polar amino acids
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
specifically transports branched-chain amino acids
-
-
?
additional information
?
-
-
specifically transports branched-chain amino acids
-
-
?
additional information
?
-
specificity of L-lysine transport in wild-type cells and in recombinantly parasite AAP7 expressing yeast 22DELTA7AA cells, overview
-
-
?
additional information
?
-
-
specificity of L-lysine transport in wild-type cells and in recombinantly parasite AAP7 expressing yeast 22DELTA7AA cells, overview
-
-
?
additional information
?
-
-
broad specificity for polar amino acids
-
-
?
additional information
?
-
-
contributes to the alpha-aminoadipic acid flux
-
-
?
additional information
?
-
-
contributes to the alpha-aminoadipic acid flux
-
-
?
additional information
?
-
-
broad specificity for polar amino acids
-
-
?
additional information
?
-
-
broad specificity for polar amino acids
-
-
?
additional information
?
-
-
broad specificity for polar amino acids
-
-
?
additional information
?
-
-
Gap1 is a transporting amino acid transceptor that triggers the activation of the protein kinase A pathway
-
-
?
additional information
?
-
-
Gap1p transports all naturally occurring amino acids
-
-
?
additional information
?
-
-
the GTG motif of Gap1p is involved in amino acid binding
-
-
?
additional information
?
-
-
broad specificity for polar amino acids
-
-
?
additional information
?
-
specificity of L-lysine transport in wild-type cells, overview
-
-
?
additional information
?
-
-
specificity of L-lysine transport in wild-type cells, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + acidic amino acid/out
ADP + phosphate + acidic amino acid/in
-
crucial role for the uptake of amino acids into the endosperm and supplying the developing embryo with amino acids during early embryogenesis
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
-
the histidine transport system Hut is also involved in proline and betaine uptake
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
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-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 + polar amino acid-[polar amino acid-binding protein][side 1]
ADP + phosphate + polar amino acid[side 2] + [polar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
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
-
-
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
essential for basic amino acid uptake, transports Lys, Arg, Orn, His, and Gln
-
-
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
-
amino acid uptake, catalyzes the transport of all the D- and L-isomers of the amino acids normally found in proteins
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
Leishmania amazonensis MHOM/BR/1973/2269
-
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
-
?
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-[L-arginine-binding protein][side 1]
ADP + phosphate + L-arginine[side 2] + [L-arginine-binding protein][side 1]
-
-
-
-
?
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-[L-glutamate-binding protein][side 1]
ADP + phosphate + L-glutamate[side 2] + [L-glutamate-binding protein][side 1]
-
-
-
-
?
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]
the enzyme is specific for glutamine
-
-
?
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-histidine-[L-histidine-binding protein][side 1]
ADP + phosphate + L-histidine[side 2] + [L-histidine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Gap1 is a transporting amino acid transceptor that triggers the activation of the protein kinase A pathway
-
-
?
additional information
?
-
-
Gap1p transports all naturally occurring amino acids
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
poor stimulatory activity on ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
Co2+
-
dimeric ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids - Leu-Glu-His-His-His-His-His-His - under optimal conditions hydrolyzes ATP at a rate comparable to that of the intact complex HisQMP2, requires a cation for activity, Co2+ is the best stimulator at 1 mM
Mg2+
Mn2+
-
dimeric ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids - Leu-Glu-His-His-His-His-His-His - under optimal conditions hydrolyzes ATP at a rate comparable to that of the intact complex HisQMP2, requires a cation for activity, Mn2+ is the best stimulator at concentrations above 1.5 mM
Mg2+
-
dimeric ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids - Leu-Glu-His-His-His-His-His-His - under optimal conditions hydrolyzes ATP at a rate comparable to that of the intact complex HisQMP2, requires a cation for activity, Co2+ and Mn2+ are more effective than Mg2+
Mg2+
-
required for both transport and ATPase activity
Mg2+
-
conformational changes within HisP are sensitive to the presence/absence of Mg ions bound to the ATP
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-O-(trinitrophenyl)adenosine 5'-triphosphate
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
3'-O-(trinitrophenyl)adenosine 5'-triphosphate
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
5'-adenylyl-beta,gamma-imidotriphosphate
-
inhibits ATPase activity
adenosine 5'(beta,gamma-imino)triphosphate
-
inhibits ATPase activity
adenylyl (beta,gamma-methylene)-diphosphate
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
adenylyl (beta,gamma-methylene)-diphosphonate
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
cardiolipin
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
lysophosphatidic acid
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
NEM
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
orthovanadate
-
inhibits ATPase activity
phosphatidic acid
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
phosphatidylglycerol
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
phosphatidylserine
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
vanadate
-
in contrast to the intact enzyme complex HisQMP2 the ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids - Leu-Glu-His-His-His-His-His-His is not inhibited
adenosine 5'-O-(3-thio)triphosphate
-
inhibits ATPase activity
adenosine 5'-O-(3-thio)triphosphate
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
ADP
-
dimeric HisP protein with a carboxy-terminal extension of 8 amino acids
additional information
no or poor inhibition by L-alanine, L-asparagine, L-arginine, L-proline, L-serine, glycine, L-methionine, L-threonine, L-histidine, and L-cysteine
-
additional information
-
no or poor inhibition by L-alanine, L-asparagine, L-arginine, L-proline, L-serine, glycine, L-methionine, L-threonine, L-histidine, and L-cysteine
-
additional information
-
cycling of Gap1p-GFP to the plasma membrane is blocked by high amino acid concentrations
-
additional information
-
permease activity can be rapidly and reversibly inactivated by the presence of most amino acids, except alanine or phenylalanine, mixtures of amino acids are less toxic than single amino acids, the toxicity appears to be the consequence of uptake of unusually large quantities of a single amino acid
-
additional information
-
brefeldin A decreases uptake of L-Leu, substance probably acts via direct or indirect modification of the transporting protein, which affects the kinetic parameters
-
additional information
-
inhibition of agonist activity by the inhibitor molecules, overveiw
-
additional information
-
reversible inactivation of intrinsic Gap1p activity at the cell surface by amino acids requires active transport through Gap1p
-
additional information
no inhibition by L-aspartate, L-arginine, L-asparagine, L-alanine, and L-serine
-
additional information
-
no inhibition by L-aspartate, L-arginine, L-asparagine, L-alanine, and L-serine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
uptake of leucine 10fold and of arginine 25fold greater in wild-type yeast grown in galactose medium compared with those grown in glucose medium, increase in amino acid transport is due to carbon metabolite repression
-
histidine-binding protein
-
required
-
histidine-binding protein
-
Km: 0.008 mM
-
histidine-binding protein
-
the histidine-binding protein HisJ, interacts with the membrane-bound complex HisQMP2 and stimulates its ATPase activity, which results in histidine translocation. HisJ provides some additional essential function in translocation that is independent of the stimulation of ATP hydrolysis. HisJ has different optimal conformations for signaling and for translocation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
alpha-aminoadipic acid-[polar amino acid-binding protein][side 1]
-
-
-
5.4
L-glutamine-[L-glutamine-binding protein][side 1]
at pH 6.0 and 25°C
-
0.041
L-glutamine/out
-
wild-type LHT1, pH 5.8, temperature not specified in the publication
additional information
additional information
-
Michaelis-Menten kinetics
-
0.9
ATP
-
mutant P172T of the ATP-binding subunit HisP
1.2
ATP
-
mutant T205A of the ATP-binding subunit HisP
0.0127
glycine/out
-
Gap mutant K9R,K16R/A297V, pH and temperature not specified in the publication
0.02
glycine/out
-
Gap mutant K9R,K16R, pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.027
citrulline
Saccharomyces cerevisiae
-
Gap mutant K9R,K16R/A297V, pH and temperature not specified in the publication
0.0309
citrulline
Saccharomyces cerevisiae
-
Gap mutant K9R,K16R, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0004 - 0.0387
-
activities of diverse mutant enzymes, overview, pH and temperature not specified in the publication
0.0332
-
wild-type Gap1 amino acid uptake activity, pH and temperature not specified in the publication
additional information
-
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
maximum glutamine uptake occurs at extracellular pH 5.0, and is significantly reduced as extracellular pH increases to pH 8.0
7
-
dimeric HisP protein with a carboxy-terminal extension of 8 amino acids - Leu-Glu-His-His-His-His-His-His - under optimal conditions hydrolyzes ATP to a rate comparable to that by the intact complex HisQMP2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9.5
-
about 30% of maximal activity at pH 6.0 and at pH 9.5
6.3 - 8
-
pH 6.3: about 30% of maximal activity, pH 8.0: about 50% of maximal activity, dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, Leu-Glu-His-His-His-His-His-His
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
30°C: about 40% of maximal activity, 55°C: about 80% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC 7120 and different bgtA, bgtB, natF, natG, and natH knockout mutants
-
-
brenda
(L.) Heynh. plants (ecotype Col-0) and AAP8 deficiency mutant, deficiency mutant shows strongly affected seed development with reduced intracellular Asp and Glu and increased Pro content
-
-
brenda
strains S288C variant M3750, strain BY4741, strain EY0986, strain Bio101 and strain INVSc1
-
-
brenda
-
-
-
brenda
wild-type and mutant enzymes
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
very specific during early seed development 2-5 days after fertilization in young seeds, expressed in the veins of the mature siliques at later stages of development, not expressed in mature seeds
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
when amino acids are scarce Gap1p is sorted to the plasma membrane, whereas when amino acids are abundant Gap1p is sorted from the trans-Golgi through the multivesicular endosome and to the vacuole requiring direct recognition of transport substrates
brenda
-
bound to
brenda
-
the membrane-bound complex of the periplasmic histidine permease is composed of two integral membrane proteins, HisQ and HisM, and two copies of the ATP-binding subunit HisP
brenda
mainly to a membrane-bound structure or invagination close to the kinetoplast, the latter corresponding to the flagellar pocket or associated structures, such as the cytostome or contractile vacuole
brenda
-
the membrane-bound complex of the periplasmic histidine permease is composed of two integral membrane proteins, HisQ and HisM, and two copies of the ATP-binding subunit HisP
-
brenda
-
Gap1 comprises 12 transmembrane domains flanked by cytosol-facing N- and C-terminal tails
brenda
-
when amino acids are scarce Gap1p is sorted to the plasma membrane, whereas when amino acids are abundant Gap1p is sorted from the trans-Golgi through the multivesicular endosome and to the vacuole requiring direct recognition of transport substrates
brenda
-
at high amino acid concentrations, Gap1p-GFP is delivered to the vacuolar interior by the multivesicular endosome pathway in wild-type cells
brenda
-
when amino acids are scarce Gap1p is sorted to the plasma membrane, whereas when amino acids are abundant Gap1p is sorted from the trans-Golgi through the multivesicular endosome and to the vacuole requiring direct recognition of transport substrates
brenda
additional information
-
amino acids govern the propensity of Gap1p to recycle from the multivesicular endosome to the plasma membrane. Gap1p redistributes from the multivesicular endosome to the plasma membrane and that this recycling relies on the same machinery required for vesicular trafficking between the trans-Golgi and the plasma membrane
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
the enzyme belongs to the large amino acid/auxin permease family
malfunction
-
trafficking of Gap1p mutants with altered substrate specificity and transport activity, overview
malfunction
-
shoot and root nitrogen supply are strongly decreased in enzyme-silenced plants, while nitrogen fixation and nodule metabolism are up-regulated in these plants
malfunction
-
suppression of two enzyme genes (AAAP15 and AAAP21) significantly increases the mortality of adult whiteflies
metabolism
-
LysR-type ArgP and global regulator Lrp are transcriptional regulators of gene lysP, which is also regulated by the concentration of exogenous available lysine. Lysine-loaded ArgP and arginine-loaded ArgP compete at the lysP promoter. ArgP binds to the lysP promoter/control region at a T-N11-A motif in the presence and absence of lysine. Lysine-loaded ArgP prevents lysP transcription at the promoter clearance step and is a major regulator of lysP expression, Lrp modulates lysP transcription under lysine-limiting conditions by direct binding to its control region
metabolism
-
the enzyme catalyzes the transmembrane transport of single amino acid, multiple amino acids, auxin (indole-3-acetic acid) or gamma-aminobutyric acid
metabolism
-
the enzyme is a key player in nitrogen retrieval from the apoplasm into inner cortex cells for nodule export
physiological function
-
Candida albicans Gap2, CaGap2, is the true orthologue of Saccharomyces cerevisiae Gap1, which not only mediates the uptake of most amino acids but also functions as a receptor for the activation of protein kinase A, as it transports all tested amino acids. The other CaGap proteins have narrower substrate specificities though CaGap1 and CaGap6 transport several structurally unrelated amino acids. CaGap1, CaGap2, and CaGap6 also function as sensors, e.g. for methionine. CaGap permeases communicate to the intracellular signal transduction pathway
physiological function
the enzyme generates inward glutamine-dependent currents and regulates glutamine import into bacteriocytes
physiological function
-
the enzyme is crucial for plant uptake of organic nitrogen from soil
Show AA Sequence and Transmembrane Helices (878 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
ABC-type amino acid uptake transporter, composed of the ATPase subunit BgtA and a composite protein bearing periplasmic substrate-binding and transmembrane domains BgtB
additional information
-
ABC-type amino acid uptake transporter, composed of the ATPase subunit BgtA and the NatF, NatG, and NatH proteins
additional information
-
the membrane-bound enzyme complex contains four subunits and a soluble receptor
additional information
-
Gap1 comprises 12 transmembrane domains flanked by cytosol-facing N- and C-terminal tails. The N-terminal tail of Gap1 contains the acceptor lysines for ubiquitylation and its C-terminmal tail includes a sequence essential to exit from the endoplasmic reticulum
additional information
-
the P protein has a nucleotide-binding site, the M protein also might contain such a site
additional information
-
the membrane-bound enzyme complex contains four subunits and a soluble receptor
additional information
-
the histidine-binding protein HisJ, interacts with the membrane-bound complex HisQMP2 and stimulates its ATPase activity, which results in histidine translocation. HisJ provides some additional essential function in translocation that is independent of the stimulation of ATP hydrolysis. HisJ has different optimal conformations for signaling and for translocation
additional information
-
histidine permease is composed of a membrane bound complex HisQMP2 containing four subunits and of a soluble receptor, the histidine-binding protein HisJ
additional information
-
the membrane-bound complex of the periplasmic histidine permease is composed of two integral membrane proteins, HisQ and HisM, and two copies of the ATP-binding subunit HisP. HisP is absolutely required for ATP hydrolysis, HisQM regulates the ATPase activity of HisP
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 1.5 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
P172T
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
T205M
additional information
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids is stable to freezing and thawing
-
preparation diluted to 0.7 mg/ml protein and 4% glycerol is stable at 0°C for at least 1 h
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
5-10 mg/ml in storage buffer and in liquid nitrogen, ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids is stable for at least several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids, addition of a 6-histidine extension allows rapid and effective metal affinity purification
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Xenopus laevis oocytes
expression in Pisum sativum and Vicia narbonensis seeds under control of the legumin B4 promoter
-
expression of Gap1 mutants and of GFP-tagged Gap1p in a gap1DELTA car1DELTA sec6-4 strain that shows temperature sensitivity at 36°C
-
gene gap1, DNA and amino acid sequence analysis, expression analysis of wild-type and mutant enzymes in strain QA23
-
gene LdAAP7, phylogenetic analysis, functional expression in enzyme-deficient Saccharomyces cerevisiae mutant strain 22DELTA7AA
gene TcAAP7, phylogenetic analysis, functional expression in enzyme-deficient Saccharomyces cerevisiae mutant strain 22DELTA7AA. Functional overexpression of GFP-tagged TcAAP7
genes CaGap1-CaGap6, phylogenetic analysis, expression in Saccharomyces cerevisiae
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
an increase of temperature from 25 to 34C increases the enzyme level in plasma membrane, independently of pH and L-arginine availability
down-regulation of the mutant Gap1 permeases by ammonium, four gap1 mutants altered in the N-terminal tail resist ammonium-induced down-regulation, overview. Role of ubiquitin and acceptor lysines in constitutive down-regulation of mutant Gap1 proteins
-
an increase of temperature from 25 to 34C increases the enzyme level in plasma membrane, independently of pH and L-arginine availability
-
an increase of temperature from 25 to 34C increases the enzyme level in plasma membrane, independently of pH and L-arginine availability
Leishmania amazonensis MHOM/BR/1973/2269
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
medicine
-
identification of genus-specific motifs in amino acid permeases, which might be useful to better understand parasite physiology within its hosts, close relationship between the Leishmania donovani and Trypanosma brucei amino acid permeases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
medicine
-
the enzyme is used as a target for Leishmania identification and diagnosis of leishmaniases
additional information
-
BcaP is required for optimal growth in media containing free amino acids as the sole amino acid source
additional information
-
conformational changes within HisP that are dependent on the presence of ATP in the binding pocket of the protein, changes are predominantely confined to the alpha-helical subdomain, considerable conformational flexibility in a conserved glutamine-containing loop
additional information
-
identification of a GTPase-containing complex for Gap1p sorting in the endosomes, which has a key role in trafficking Gap1p out of the late endosome and may serve as coat proteins in this process, the complex contains the GTPases Gtr1p and Gtr2p, delivery of Gap1p to the plasma membrane depends on specific nucleotide-bound states of the GTPases, Gtr2p interacts with the C-terminal cytosolic domain of Gap1p, a tyrosine-containing motif in this domain is necessary both to bind Gtr2p and to direct sorting of Gap1p to the plasma membrane
additional information
-
role of ubiquitination appears to be a signal for delivery of Gap1p to the multivesicular endosome, whereas amino acid abundance appears to control the cycling of Gap1p from the multivesicular endosome to the plasma membrane, Gap1p recycling does not depend on other known pathways for recycling proteins from the endosome to Golgi compartments
additional information
-
the aromatic and neutral aliphatic amino acid permease PcMtr is unrelated to the amino acid permease family, which includes most amino acid permeases in fungi
additional information
-
UfAAT3 encodes a protein with a high degree of sequence similarity to fungal amino acid permeases
additional information
-
VfAAP1 expression increases seed sink strength for nitrogen, improves plant nitrogen status, and leads to higher seed protein
additional information
-
BcaP is required for optimal growth in media containing free amino acids as the sole amino acid source
-
additional information
-
the aromatic and neutral aliphatic amino acid permease PcMtr is unrelated to the amino acid permease family, which includes most amino acid permeases in fungi
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Rhodobacter capsulatus, Sinorhizobium meliloti
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
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