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Information on EC 7.4.2.2 - ABC-type nonpolar-amino-acid transporter
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7.4.2.2 ABC-type nonpolar-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. This entry comprises enzymes that import Leu, Ile and Val.
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Word Map
- 7.4.2.2
- thyroid
-
sodium-coupled
-
blood-brain
-
l-type
- na+
-
monocarboxylate
- slc6a19
-
sodium-dependent
-
slc1a5
- rapamycin
-
mtorc1
-
na+-independent
-
slc38a2
- ace2
-
cotransporter
-
oatp1c1
-
bcaas
-
snats
-
deiodinase
- hartnup
-
meaib
-
microvillous
- collectrin
-
aminoaciduria
- gabapentin
-
iodothyronine
-
ascts
-
oatps
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
+
=
+
+
+
+
+
nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
=
+
+
nonpolar amino acid[side 2]
+
[nonpolar amino acid-binding protein][side 1]
Synonyms
neutral amino acid transporter, slc7a5, mct10, b0at1, brnq1, bcaa transporter, branched-chain amino acid transporter, pcdip5, high-affinity tryptophan permease, vacuolar amino acid transporter, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acidic amino acid permease
ATP phosphohydrolase (nonpolar-amino-acid-transporting)
-
-
-
-
BCAA permease
BCAA transporter
BcaP
BraB
branched-chain amino acid transporter
BrnQ
BrnQ1
BrnQ2
EC 3.6.3.22
-
-
formerly
-
neutral amino acid permease N-I
nonpolar-amino-acid-transporting ATPase
-
-
-
-
PcDIP5
additional information
-
the vacuolar amino acid transporters belong to the AVT family or the VBA family of enzymes
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1] = ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, nonpolar-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. This entry comprises enzymes that import Leu, Ile and Val.
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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 + 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 + L-alanine-[L-alanine-binding protein][side 1]
ADP + phosphate + L-alanine[side 2] + [L-alanine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-isoleucine-[L-isoleucine-binding protein][side 1]
ADP + phosphate + L-isoleucine[side 2] + [L-isoleucine-binding protein][side 1]
ATP + H2O + L-leucine-[L-leucine-binding protein][side 1]
ADP + phosphate + L-leucine[side 2] + [L-leucine-binding protein][side 1]
ATP + H2O + L-proline-[L-proline-binding protein][side 1]
ADP + phosphate + L-proline[side 2] + [L-proline-binding protein][side 1]
ATP + H2O + L-threonine-[L-threonine-binding protein][side 1]
ADP + phosphate + L-threonine[side 2] + [L-threonine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-tryptophan-[L-tryptophan-binding protein][side 1]
ADP + phosphate + L-tryptophan[side 2] + [L-tryptophan-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-valine-[L-valine-binding protein][side 1]
ADP + phosphate + L-valine[side 2] + [L-lvaline-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-valine-[L-valine-binding protein][side 1]
ADP + phosphate + L-valine[side 2] + [L-valine-binding protein][side 1]
ATP + H2O + L-valine/out
ADP + phosphate + L-valine/in
-
45fold less transport compared to leucine
-
-
?
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
ATP + H2O + unpolar amino acid-[unpolar amino acid-binding protein][side 1]
ADP + phosphate + unpolar amino acid[side 2] + [unpolar amino acid-binding protein][side 1]
ATP + H2O + alanine/out
ADP + phosphate + alanine/in
-
neutral Na-amino acid cotransport, e.g. Na-alanine cotransport, is differentially regulated by glucocorticoids in the normal and chronically inflamed rabbit small intestine, treatment with MP reverses the reduction in Na-alanine cotransport in villus cells from the chronically inflamed intestine, secondary to restoration in the affinity for the amino acid without a change in the Vmax, overview
-
-
?
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 + L-isoleucine-[L-isoleucine-binding protein][side 1]
ADP + phosphate + L-isoleucine[side 2] + [L-isoleucine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-isoleucine-[L-isoleucine-binding protein][side 1]
ADP + phosphate + L-isoleucine[side 2] + [L-isoleucine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-isoleucine-[L-isoleucine-binding protein][side 1]
ADP + phosphate + L-isoleucine[side 2] + [L-isoleucine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-isoleucine-[L-isoleucine-binding protein][side 1]
ADP + phosphate + L-isoleucine[side 2] + [L-isoleucine-binding protein][side 1]
-
substrate for isoforms BrnQ1 and BrnQ2
-
-
?
ATP + H2O + L-isoleucine-[L-isoleucine-binding protein][side 1]
ADP + phosphate + L-isoleucine[side 2] + [L-isoleucine-binding protein][side 1]
-
substrate for isoforms BrnQ1 and BrnQ2
-
-
?
ATP + H2O + L-isoleucine/out
ADP + phosphate + L-isoleucine/in
-
19fold less transport compared to leucine
-
-
?
ATP + H2O + L-isoleucine/out
ADP + phosphate + L-isoleucine/in
-
19fold less transport compared to leucine
-
-
?
ATP + H2O + L-leucine-[L-leucine-binding protein][side 1]
ADP + phosphate + L-leucine[side 2] + [L-leucine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-leucine-[L-leucine-binding protein][side 1]
ADP + phosphate + L-leucine[side 2] + [L-leucine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-leucine-[L-leucine-binding protein][side 1]
ADP + phosphate + L-leucine[side 2] + [L-leucine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-leucine-[L-leucine-binding protein][side 1]
ADP + phosphate + L-leucine[side 2] + [L-leucine-binding protein][side 1]
-
substrate for isoform BrnQ1
-
-
?
ATP + H2O + L-leucine-[L-leucine-binding protein][side 1]
ADP + phosphate + L-leucine[side 2] + [L-leucine-binding protein][side 1]
-
substrate for isoform BrnQ1
-
-
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
-
specificity of leucine-mediated transport by the LIV system of Campylobacter jejuni, overview. The LIV system is largely limited to leucine, isoleucine, and valine
-
-
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
-
-
-
-
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
-
specificity of leucine-mediated transport by the LIV system of Campylobacter jejuni, overview. The LIV system is largely limited to leucine, isoleucine, and valine
-
-
?
ATP + H2O + L-proline-[L-proline-binding protein][side 1]
ADP + phosphate + L-proline[side 2] + [L-proline-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-proline-[L-proline-binding protein][side 1]
ADP + phosphate + L-proline[side 2] + [L-proline-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-valine-[L-valine-binding protein][side 1]
ADP + phosphate + L-valine[side 2] + [L-valine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-valine-[L-valine-binding protein][side 1]
ADP + phosphate + L-valine[side 2] + [L-valine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-valine-[L-valine-binding protein][side 1]
ADP + phosphate + L-valine[side 2] + [L-valine-binding protein][side 1]
-
substrate for isoform BrnQ1
-
-
?
ATP + H2O + L-valine-[L-valine-binding protein][side 1]
ADP + phosphate + L-valine[side 2] + [L-valine-binding protein][side 1]
-
substrate for isoform BrnQ1
-
-
?
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
whereas Bgt is dispensable for diazotrophic growth, N-II appears to contribute together with N-I to the diazotrophic physiology of this cyanobacterium
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
AAP1 imports uncharged amino acids into roots of Arabidopsis thaliana, when these are supplied at ecologically relevant concentrations. Glutamate, histidine and neutral amino acids, including phenylalanine, are physiological substrates for AAP1, whereas aspartate, lysine and arginine are not
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
neutral Na-amino acid cotransport is differentially regulated by glucocorticoids in the normal and chronically inflamed rabbit small intestine, overview
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
vacuolar compartmentalization of amino acids: basic amino acids, e.g. tyrosine, leucine and isoleucine, accumulate preferentially into vacuoles but acidic amino acids are almost excluded from them, the enzyme acts as part of selective machineries to transport the amino acids operating at the vacuolar membrane
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
Arg, Lys, His, Phe, Trp, Tyr, Gln, Asn, Ile and Leu are actively transported into vacuoles by several different transporters, overview. VBA family enzymes transport basic amino acids, such as arginine, histidine and lysine, into yeast vacuoles
-
-
?
ATP + H2O + phenylalanine/out
ADP + phosphate + phenylalanine/in
-
-
-
-
?
ATP + H2O + unpolar amino acid-[unpolar amino acid-binding protein][side 1]
ADP + phosphate + unpolar amino acid[side 2] + [unpolar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + unpolar amino acid-[unpolar amino acid-binding protein][side 1]
ADP + phosphate + unpolar amino acid[side 2] + [unpolar amino acid-binding protein][side 1]
-
-
-
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant strains, overview
-
-
?
additional information
?
-
-
AAP1 plays an important role for efficient use of nitrogen sources present in the rhizosphere
-
-
?
additional information
?
-
-
the enzymes are responsible for the bulk of isoleucine and valine uptake and are also involved in leucine uptake
-
-
?
additional information
?
-
-
the enzymes are responsible for the bulk of isoleucine and valine uptake and are also involved in leucine uptake
-
-
?
additional information
?
-
-
LIV proteins are involved in transport of other branched-chain amino acids but at more modest levels than observed for leucine, comparison of activities of wild-type and mutant strains, overview
-
-
?
additional information
?
-
-
LIV proteins are involved in transport of other branched-chain amino acids but at more modest levels than observed for leucine, comparison of activities of wild-type and mutant strains, overview
-
-
?
additional information
?
-
-
the enzyme does not transport acidic amino acids like L-glutamate and L-aspartate
-
-
?
additional information
?
-
-
contributes to the alpha-aminoadipic acid flux
-
-
?
additional information
?
-
-
contributes to the alpha-aminoadipic acid flux
-
-
?
additional information
?
-
-
amino acid compartmentalization in vacuoles is dynamically linked with such a homeostatic function for the maintenance of the cytosolic amino acid concentration in yeast
-
-
?
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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 + L-leucine-[L-leucine-binding protein][side 1]
ADP + phosphate + L-leucine[side 2] + [L-leucine-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-proline-[L-proline-binding protein][side 1]
ADP + phosphate + L-proline[side 2] + [L-proline-binding protein][side 1]
-
-
-
-
?
ATP + H2O + L-tryptophan-[L-tryptophan-binding protein][side 1]
ADP + phosphate + L-tryptophan[side 2] + [L-tryptophan-binding protein][side 1]
-
-
-
-
?
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
ATP + H2O + unpolar amino acid-[unpolar amino acid-binding protein][side 1]
ADP + phosphate + unpolar amino acid[side 2] + [unpolar amino acid-binding protein][side 1]
ATP + H2O + alanine/out
ADP + phosphate + alanine/in
-
neutral Na-amino acid cotransport, e.g. Na-alanine cotransport, is differentially regulated by glucocorticoids in the normal and chronically inflamed rabbit small intestine, treatment with MP reverses the reduction in Na-alanine cotransport in villus cells from the chronically inflamed intestine, secondary to restoration in the affinity for the amino acid without a change in the Vmax, overview
-
-
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
-
specificity of leucine-mediated transport by the LIV system of Campylobacter jejuni, overview. The LIV system is largely limited to leucine, isoleucine, and valine
-
-
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
-
specificity of leucine-mediated transport by the LIV system of Campylobacter jejuni, overview. The LIV system is largely limited to leucine, isoleucine, and valine
-
-
?
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + nonpolar amino acid-[nonpolar amino acid-binding protein][side 1]
ADP + phosphate + nonpolar amino acid[side 2] + [nonpolar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
whereas Bgt is dispensable for diazotrophic growth, N-II appears to contribute together with N-I to the diazotrophic physiology of this cyanobacterium
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
AAP1 imports uncharged amino acids into roots of Arabidopsis thaliana, when these are supplied at ecologically relevant concentrations. Glutamate, histidine and neutral amino acids, including phenylalanine, are physiological substrates for AAP1, whereas aspartate, lysine and arginine are not
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
neutral Na-amino acid cotransport is differentially regulated by glucocorticoids in the normal and chronically inflamed rabbit small intestine, overview
-
-
?
ATP + H2O + nonpolar amino acid/out
ADP + phosphate + nonpolar amino acid/in
-
vacuolar compartmentalization of amino acids: basic amino acids, e.g. tyrosine, leucine and isoleucine, accumulate preferentially into vacuoles but acidic amino acids are almost excluded from them, the enzyme acts as part of selective machineries to transport the amino acids operating at the vacuolar membrane
-
-
?
ATP + H2O + phenylalanine/out
ADP + phosphate + phenylalanine/in
-
-
-
-
?
ATP + H2O + unpolar amino acid-[unpolar amino acid-binding protein][side 1]
ADP + phosphate + unpolar amino acid[side 2] + [unpolar amino acid-binding protein][side 1]
-
-
-
-
?
ATP + H2O + unpolar amino acid-[unpolar amino acid-binding protein][side 1]
ADP + phosphate + unpolar amino acid[side 2] + [unpolar amino acid-binding protein][side 1]
-
-
-
-
?
additional information
?
-
-
AAP1 plays an important role for efficient use of nitrogen sources present in the rhizosphere
-
-
?
additional information
?
-
-
amino acid compartmentalization in vacuoles is dynamically linked with such a homeostatic function for the maintenance of the cytosolic amino acid concentration in yeast
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
FTY720 (i.e. 2-amino-2-[2-(4-octylphenyl)]-1,3-propanediol hydrochloride or fingolimod) promotes endocytosis of the enzyme in HeLa cells, this is preceded by loss of its transport activity
-
additional information
-
leucine does not inhibit alpha-aminoadipic acid transport via PcDIP5
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methylprednisolone
-
stimulates Na-alanine cotransport in the normal intestine, mechanism of stimulation is secondary to an increase in cotransporter numbers without an alteration in the affinity for the amino acid. Treatment with MP reverses the reduction in Na-alanine cotransport in villus cells from the chronically inflamed intestine, secondary to restoration in the affinity for the amino acid without a change in the Vmax, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
alpha-aminoadipic acid-[polar amino acid-binding protein][side 1]
-
-
-
0.00162
L-leucine-[L-leucine-binding protein][side 1]
-
isoform BrnQ1, at 37°C, pH not specified in the publication
-
0.00179
L-valine-[L-valine-binding protein][side 1]
-
isoform BrnQ1, at 37°C, pH not specified in the publication
-
0.00093
L-isoleucine-[L-isoleucine-binding protein][side 1]
-
isoform BrnQ1, at 37°C, pH not specified in the publication
-
0.0041
L-isoleucine-[L-isoleucine-binding protein][side 1]
-
BcaP, at 26°C, pH not specified in the publication
-
0.00894
L-isoleucine-[L-isoleucine-binding protein][side 1]
-
isoform BrnQ2, at 37°C, pH not specified in the publication
-
0.016
L-isoleucine-[L-isoleucine-binding protein][side 1]
-
BraB, at 26°C, pH not specified in the publication
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
clinical isolate, live genes encoded in the liv operon
-
-
brenda
strain PCC 7120, ORFS salr4167 and alr3187 encoding BgtA and BgtB, and ORFs alr4167, alr4164, alr4165, and alr4166 encoding NatF, NatG, and NatH respectively
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
cellular and subcellular location of the Bgt and N-II transporters, N-I that is expressed only in vegetative cells, while the Bgt and N-II systems are present in both vegetative cells and heterocysts, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
cellular and subcellular location of the Bgt and N-II transporters, in nitrate-grown filaments, the recombinant GFP-tagged proteins are observed in all the cells of the filament, with a somewhat higher signal in the periphery than in the centre of the cells and, especially, in the intercellular septa, overview
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
deletion of isoform BrnQ2 results in increased virulence, including severe kidney pathology
malfunction
-
deletion of isoform BrnQ2 results in increased virulence, including severe kidney pathology
-
physiological function
-
LivJ and LivK are required for optimal commensal colonization of the chick ceca
physiological function
-
isoform BrnQ1 is required for Staphylococcus aureus strain USA300 fitness in vivo
physiological function
-
the enzyme contributes to salt stress-induced proline uptake from exogenous sources. In addition, proline uptake promotes salt tolerance in Arabidopsis seedlings
physiological function
-
isoform BrnQ1 is required for Staphylococcus aureus strain USA300 fitness in vivo
-
physiological function
-
LivJ and LivK are required for optimal commensal colonization of the chick ceca
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q0K9G8_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
284
0
30465
TrEMBL
-
Q0K9G9_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
246
0
26707
TrEMBL
-
Q0KBG5_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
237
0
26508
TrEMBL
-
Q0KBE7_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
255
0
26839
TrEMBL
-
Q0KCQ1_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
230
0
25155
TrEMBL
-
C9YDM9_CURXX
Curvibacter symbiont subsp. Hydra magnipapillata
231
0
25564
TrEMBL
-
G8S557_ACTS5
Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
237
0
24728
TrEMBL
-
Q0K3X5_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
245
0
26909
TrEMBL
-
Q0K5K3_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
241
0
26498
TrEMBL
-
A0A212KE23_9PROT
259
0
28012
TrEMBL
-
Q0KCQ2_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
282
0
30729
TrEMBL
-
Q0KEY0_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
272
0
30352
TrEMBL
-
C9Y9B9_CURXX
Curvibacter symbiont subsp. Hydra magnipapillata
284
0
30933
TrEMBL
-
Q0K5K2_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
258
0
28724
TrEMBL
-
Q0KEY4_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
326
0
35560
TrEMBL
-
Q0K5L2_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
247
0
26702
TrEMBL
-
Q0K8G6_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
255
0
28105
TrEMBL
-
C9Y9C0_CURXX
Curvibacter symbiont subsp. Hydra magnipapillata
239
0
25786
TrEMBL
-
F8GRQ2_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
237
0
25789
TrEMBL
-
Q0K3X6_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
257
0
28571
TrEMBL
-
Q0K7B9_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
258
0
28082
TrEMBL
-
D5ALW4_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
260
0
28084
TrEMBL
-
Q0KAY8_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
243
0
25780
TrEMBL
-
Q0K544_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
247
0
27265
TrEMBL
-
G0ERL1_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
263
0
29147
TrEMBL
-
Q0KBR8_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
241
0
26060
TrEMBL
-
Q0K7C0_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
238
0
25511
TrEMBL
-
Q0KC86_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
239
0
25662
TrEMBL
-
G0ERL0_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
233
0
25260
TrEMBL
-
D5ALW5_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
238
0
25337
TrEMBL
-
Q0KBE6_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
237
0
25501
TrEMBL
-
Q0JZN1_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
260
0
29420
TrEMBL
-
Q0KBG6_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
257
0
28304
TrEMBL
-
Q0JZN0_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
237
0
25787
TrEMBL
-
D5ASR5_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
273
0
30435
TrEMBL
-
F8GRQ1_CUPNN
Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)
260
0
29423
TrEMBL
-
Q0K325_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
268
0
29035
TrEMBL
-
Q0JZK3_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
254
0
27651
TrEMBL
-
Q0KBR9_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
256
0
27408
TrEMBL
-
D5AUG0_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
234
0
25365
TrEMBL
-
Q0K326_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
245
0
26776
TrEMBL
-
D5AUF9_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
262
0
28502
TrEMBL
-
Q0K8G7_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
233
0
25242
TrEMBL
-
Q0JZK2_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
235
0
25409
TrEMBL
-
Q0KC87_CUPNH
Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)
268
0
28737
TrEMBL
-
D5ASR0_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
272
0
30367
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ORFsalr4167 and alr3187 encode, respectively, an ATPase subunit, BgtA, and a composite protein bearing periplasmic substrate-binding and transmembrane domains, BgtB, of an ABC-type high-affinity basic amino acid uptake transporter Bgt. ORF alr4167 is clustered with ORFs alr4164, alr4165 and alr4166 that encode a periplasmic substrate-binding protein, NatF, and transmembrane proteins NatG and NatH respectively. The NatF, NatG, NatH and BgtA proteins constitute an ABC-type uptake transporter for acidic and neutral polar amino acids, N-II, Bgt and N-II transport systems thus share the ATPase subunit, BgtA
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N81K
-
the mutation completely abrogates tryptophan import without any abnormalities in the expression or localization
additional information
additional information
-
mutants of the open reading frames are strongly affected in the transport of Pro, Phe, Leu and Gly and also impaired in the transport of Ala and Ser
additional information
-
construction of deletion mutants of ORFs encoding BgtA, BgtB, NatF, NatG, and NatH, all showing altered substrate specificity compared to the wild-type enzyme, amino acid release and diazotrophy in the mutants, overview
additional information
-
mutants of the open reading frames are strongly affected in the transport of Pro, Phe, Leu and Gly and also impaired in the transport of Ala and Ser
-
additional information
-
identification of an Arabidopsis thaliana mutant that is deficient in the amino acid permease 1 and resistant to 10 mM phenylalanine and a range of other amino acids
additional information
-
generation of diverse liv gene deletion mutant strains, DELTAlivJ mutant shows a 10fold reduction in leucine transport, DELTAlivK mutant shows 43fold reduction compared to the wild-type activity, deletion of both livJ and livK reduces the transport of leucine to over 200fold lower than that for wild-type cells. Also deletion of other liv gene either individually, e.g., DELTAlivH, DELTAlivM, DELTAlivG, or DELTAlivF, or as paired double mutants essentially abolishes transport of leucine. Deletion of both livJ and livK as well as both permeases or ATPases results in abolishment of transport of isoleucine and valine
additional information
-
generation of diverse liv gene deletion mutant strains, DELTAlivJ mutant shows a 10fold reduction in leucine transport, DELTAlivK mutant shows 43fold reduction compared to the wild-type activity, deletion of both livJ and livK reduces the transport of leucine to over 200fold lower than that for wild-type cells. Also deletion of other liv gene either individually, e.g., DELTAlivH, DELTAlivM, DELTAlivG, or DELTAlivF, or as paired double mutants essentially abolishes transport of leucine. Deletion of both livJ and livK as well as both permeases or ATPases results in abolishment of transport of isoleucine and valine
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in a deletion mutant for the high-affinity tryptophan permease Tat2 in Saccharomyces cerevisiae
-
ORFsalr4167 and alr3187 encode, respectively, an ATPase subunit, BgtA, and a composite protein bearing periplasmic substrate-binding and transmembrane domains, BgtB, of an ABC-type high-affinity basic amino acid uptake transporter Bgt. ORF alr4167 is clustered with ORFs alr4164, alr4165 and alr4166 that encode a periplasmic substrate-binding protein, NatF, and transmembrane proteins NatG and NatH respectively. The NatF, NatG, NatH and BgtA proteins constitute an ABC-type uptake transporter for acidic and neutral polar amino acids, N-II, Bgt and N-II transport systems thus share the ATPase subunit, BgtA. Structure of the strain PCC 7120 genomic regions carrying the bgtB gene and the natF-natG-natH-bgtA gene cluster, overview, expression of the Bgt and N-II transporters as GFP-tagged proteins in strain PCC 7120
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by salt stress and abscisic acid, but not by L-proline
-
enzyme transcription is upregulated 1.44fold after rapamycin treatment for 6 h
-
livJ expression is not induced by leucine
the enzyme shows elevated transport activity of the neutral amino acid L-isoleucine during the nocturnal active phase compared to the inactive one. There is increased enzyme protein expression under amino acid-supplemented diet in the proximal section but not in the distal one of the small intestine
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
N-I permease is necessary for normal growth of Anabaena sp. on N2, plays a role in the diazotrophic filament specifically in vegetative cells, the products of Anabaena open reading frames all1046, all1047, all1284, alr1834 and all2912 are putative elements of the neutral amino acid permease
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
-
N-I permease is necessary for normal growth of Anabaena sp. on N2, plays a role in the diazotrophic filament specifically in vegetative cells, the products of Anabaena open reading frames all1046, all1047, all1284, alr1834 and all2912 are putative elements of the neutral amino acid permease
-
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
Kan, G.; Dassa, E.; Saurin, N.; Hofnung, M.; Saier, M.H.
Phylogenetic analyses of the ATP-binding constituents of bacterial extracytoplasmic receptor-dependent ABC-type nutrient uptake permeases
Res. Microbiol.
146
271-278
1995
Bacteria
brenda
Saier, M.H.
Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya
Adv. Microb. Physiol.
40
81-136
1998
Bacteria
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
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
Picossi, S.; Montesinos, M.L.; Pernil, R.; Lichtle, C.; Herrero, A.; Flores, E.
ABC-type neutral amino acid permease N-I is required for optimal diazotrophic growth and is repressed in the heterocysts of Anabaena sp. strain PCC 7120
Mol. Microbiol.
57
1582-1592
2005
Anabaena sp., Anabaena sp. PCC 7120
brenda
Sundaram, U.; Wisel, S.; Coon, S.
Neutral Na-amino acid cotransport is differentially regulated by glucocorticoids in the normal and chronically inflamed rabbit small intestine
Am. J. Physiol.
292
G467-G474
2007
Oryctolagus cuniculus
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
Lee, Y.H.; Foster, J.; Chen, J.; Voll, L.M.; Weber, A.P.; Tegeder, M.
AAP1 transports uncharged amino acids into roots of Arabidopsis
Plant J.
50
305-319
2007
Arabidopsis thaliana
brenda
Sekito, T.; Fujiki, Y.; Ohsumi, Y.; Kakinuma, Y.
Novel families of vacuolar amino acid transporters
IUBMB Life
60
519-525
2008
Saccharomyces cerevisiae
brenda
Ribardo, D.A.; Hendrixson, D.R.
Analysis of the LIV system of Campylobacter jejuni reveals alternative roles for LivJ and LivK in commensalism beyond branched-chain amino acid transport
J. Bacteriol.
193
6233-6243
2011
Campylobacter jejuni, Campylobacter jejuni 81-176
brenda
Uemura, S.; Mochizuki, T.; Kurosaka, G.; Hashimoto, T.; Masukawa, Y.; Abe, F.
Functional analysis of human aromatic amino acid transporter MCT10/TAT1 using the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1859
2076-2085
2017
Homo sapiens
brenda
Lunprom, S.; Pongcharoen, P.; Sekito, T.; Kawano-Kawada, M.; Kakinuma, Y.; Akiyama, K.
Characterization of vacuolar amino acid transporter from Fusarium oxysporum in Saccharomyces cerevisiae
Biosci. Biotechnol. Biochem.
79
1972-1979
2015
Fusarium oxysporum f. sp. cucumerinum
brenda
Wang, T.; Chen, Y.; Zhang, M.; Chen, J.; Liu, J.; Han, H.; Hua, X.
Arabidopsis amino acid permease1 contributes to salt stress-induced proline uptake from exogenous sources
Front. Plant Sci.
8
2182
2017
Arabidopsis thaliana
brenda
Kaiser, J.; Omer, S.; Sheldon, J.; Welch, I.; Heinrichs, D.
Role of BrnQ1 and BrnQ2 in branched-chain amino acid transport and virulence in Staphylococcus aureus
Infect. Immun.
83
1019-1029
2015
Staphylococcus aureus, Staphylococcus aureus USA300
brenda
Belitsky, B.R.
Role of branched-chain amino acid transport in Bacillus subtilis CodY activity
J. Bacteriol.
197
1330-1338
2015
Bacillus subtilis, Bacillus subtilis SMY
brenda
Jando, J.; Camargo, S.; Herzog, B.; Verrey, F.
Expression and regulation of the neutral amino acid transporter B0AT1 in rat small intestine
PLoS ONE
12
e0184845
2017
Rattus norvegicus
brenda
Barthelemy, C.; Barry, A.O.; Twyffels, L.; Andre, B.
FTY720-induced endocytosis of yeast and human amino acid transporters is preceded by reduction of their inherent activity and TORC1 inhibition
Sci. Rep.
7
13816
2017
Homo sapiens
brenda
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