Information on EC 3.6.3.21 - polar-amino-acid-transporting ATPase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.6.3.21
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RECOMMENDED NAME
GeneOntology No.
polar-amino-acid-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + polar amino acid/out = ADP + phosphate + polar amino acid/in
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroloysis of phosphoric ester
hydrolysis of phosphoric ester
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transmembrane transport
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polar-amino-acid-importing)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. Comprises bacterial enzymes that import His, Arg, Lys, Glu, Gln, Asp, ornithine, octopine and nopaline.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC 7120 and different bgtA, bgtB, natF, natG, and natH knockout mutants
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Manually annotated by BRENDA team
six genes CaGap1-CaGap6
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
MG1361 derivates
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Manually annotated by BRENDA team
MG1361 derivates
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Manually annotated by BRENDA team
strain Wisconsin 54-1255
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Manually annotated by BRENDA team
strain Wisconsin 54-1255
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Manually annotated by BRENDA team
gene TcAAP7
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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trafficking of Gap1p mutants with altered substrate specificity and transport activity, overview
metabolism
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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
physiological function
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + acidic amino acid/out
ADP + phosphate + acidic amino acid/in
show the reaction diagram
-
crucial role for the uptake of amino acids into the endosperm and supplying the developing embryo with amino acids during early embryogenesis
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-
?
ATP + H2O + alpha-aminoisobutyric acid/out
ADP + phosphate + alpha-aminoisobutyric acid/in
show the reaction diagram
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-
-
-
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
show the reaction diagram
ATP + H2O + betaine/out
ADP + phosphate + betaine/in
show the reaction diagram
ATP + H2O + citrulline/out
ADP + phosphate + citrulline/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + glycine/out
ADP + phosphate + glycine/in
show the reaction diagram
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-
-
-
?
ATP + H2O + His/out
ADP + phosphate + His/in
show the reaction diagram
ATP + H2O + histidine/out
ADP + phosphate + histidine/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-alanine/out
ADP + phosphate + L-alanine/in
show the reaction diagram
ATP + H2O + L-Arg/out
ADP + phosphate + L-Arg/in
show the reaction diagram
ATP + H2O + L-arginine/out
ADP + phosphate + L-arginine/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-Asp/out
ADP + phosphate + L-Asp/in
show the reaction diagram
ATP + H2O + L-asparagine/out
ADP + phosphate + L-asparagine
show the reaction diagram
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-
-
-
?
ATP + H2O + L-aspartate/out
ADP + phosphate + L-aspartate/in
show the reaction diagram
ATP + H2O + L-citrulline/out
ADP + phosphate + L-citrulline/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-cysteine/out
ADP + phosphate + L-cysteine/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-Gln/out
ADP + phosphate + L-Gln/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-Glu/out
ADP + phosphate + L-Glu/in
show the reaction diagram
ATP + H2O + L-glutamate/out
ADP + phosphate + L-glutamate/in
show the reaction diagram
ATP + H2O + L-glutamine/out
ADP + phosphate + glutamine/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-glutamine/out
ADP + phosphate + L-glutamine/in
show the reaction diagram
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-
-
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?
ATP + H2O + L-histidine/out
ADP + phosphate + L-histidine/in
show the reaction diagram
ATP + H2O + L-Leu/out
ADP + phosphate + L-Leu/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-leucine/out
ADP + phosphate + L-leucine/in
show the reaction diagram
ATP + H2O + L-Lys/out
ADP + phosphate + L-Lys/in
show the reaction diagram
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
show the reaction diagram
ATP + H2O + L-methionine/out
ADP + phosphate + L-methionine/in
show the reaction diagram
ATP + H2O + L-Orn/out
ADP + phosphate + L-Orn/in
show the reaction diagram
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the histidine-binding protein HisJ binds L-His and L-Arg tightly and L-Lys and L-Orn less tightly
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?
ATP + H2O + L-phenylalanine/out
ADP + phosphate + L-phenylalanine/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-threonine/out
ADP + phosphate + L-threonine/in
show the reaction diagram
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-
-
-
?
ATP + H2O + neutral amino acid/out
ADP + phosphate + neutral amino acid/in
show the reaction diagram
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-
-
-
?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
show the reaction diagram
ATP + H2O + Pro/out
ADP + phosphate + Pro/in
show the reaction diagram
CTP + H2O + His/out
CDP + phosphate + His/in
show the reaction diagram
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dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 50% of the ATPase activity with ATP
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?
GTP + H2O + His/out
GDP + phosphate + His/in
show the reaction diagram
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dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 53% of the ATPase activity with ATP
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?
UTP + H2O + His/out
UDP + phosphate + His/in
show the reaction diagram
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dimeric HisP protein with a carboxy-terminal extension of 8 amino acids, 37% of the ATPase activity with ATP
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + acidic amino acid/out
ADP + phosphate + acidic amino acid/in
show the reaction diagram
-
crucial role for the uptake of amino acids into the endosperm and supplying the developing embryo with amino acids during early embryogenesis
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-
?
ATP + H2O + amino acid/out
ADP + phosphate + amino acid/in
show the reaction diagram
ATP + H2O + His/out
ADP + phosphate + His/in
show the reaction diagram
-
the histidine transport system Hut is also involved in proline and betaine uptake
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?
ATP + H2O + histidine/out
ADP + phosphate + histidine/in
show the reaction diagram
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-
-
-
?
ATP + H2O + L-Arg/out
ADP + phosphate + L-Arg/in
show the reaction diagram
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-
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?
ATP + H2O + L-Asp/out
ADP + phosphate + L-Asp/in
show the reaction diagram
ATP + H2O + L-Gln/out
ADP + phosphate + L-Gln/in
show the reaction diagram
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-
-
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?
ATP + H2O + L-Glu/out
ADP + phosphate + L-Glu/in
show the reaction diagram
ATP + H2O + L-Lys/out
ADP + phosphate + L-Lys/in
show the reaction diagram
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-
-
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?
ATP + H2O + L-lysine/out
ADP + phosphate + L-lysine/in
show the reaction diagram
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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poor stimulatory activity on ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
Co2+
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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
Mn2+
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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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-O-(trinitrophenyl)adenosine 5'-triphosphate
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
3'-O-(trinitrophenyl)adenosine 5'-triphosphate
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
5'-adenylyl-beta,gamma-imidotriphosphate
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inhibits ATPase activity
adenosine 5'(beta,gamma-imino)triphosphate
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inhibits ATPase activity
adenosine 5'-O-(3-thio)triphosphate
adenylyl (beta,gamma-methylene)-diphosphate
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
adenylyl (beta,gamma-methylene)-diphosphonate
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
Arg-Phe-Phe
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noncompetitive
betaine
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competitive inhibitor of His uptake
cardiolipin
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
L-arginine
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8% cell growth, 25% viability of cells
L-Asp-gamma-L-Phe
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competitive
L-asparagine
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35% cell growth, 70% viability of cells
L-aspartate
slight inhibition
L-citrulline
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1% cell growth, 1% viability of cells
L-cysteine
L-glutamate
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2% cell growth, 4% viability of cells
L-glutamine
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18% cell growth, 70% viability of cells
L-Glycine
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1% cell growth, 1% viability of cells
L-histidine
L-isoleucine
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2% cell growth, 1% viability of cells
L-Leu-Gly
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competitive
L-leucine
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34% cell growth, 35% viability of cells
L-lysine
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1% cell growth, 1% viability of cells
L-methionine
L-proline
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9% cell growth, 701% viability of cells
L-serine
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20% cell growth, 25% viability of cells
L-threonine
L-tryptophan
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4% cell growth, 25% viability of cells
L-tyrosine
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20% cell growth, 35% viability of cells
L-valine
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13% cell growth, 10% viability of cells
leucine
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inhibits alpha-aminoadipic acid transport via PcGap1
lysophosphatidic acid
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
NEM
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
orthovanadate
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inhibits ATPase activity
phosphatidic acid
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
phosphatidylglycerol
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
phosphatidylserine
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
Pro
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competitive inhibitor of His uptake
vanadate
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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
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
histidine-binding protein
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L-asparagine
slight activation
L-cysteine
slight activation
L-threonine
slight activation
additional information
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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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
alpha-aminoadipic acid
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0.000807
alpha-aminoisobutyric acid
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0.046 - 8
ATP
0.0127 - 0.02
glycine/out
0.000509
L-alanine
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0.0002
L-glutamate
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0.041
L-glutamine/out
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wild-type LHT1, pH 5.8, temperature not specified in the publication
0.0002
L-histidine
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-
0.000515
L-leucine
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-
0.00736
L-lysine/out
pH 4.5, 30°C, recombinant enzyme
additional information
additional information
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Michaelis-Menten kinetics
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.105
L-Asp-gamma-L-Phe
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0.19
L-Leu-Gly
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.027 - 0.0309
citrulline
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004 - 0.0387
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activities of diverse mutant enzymes, overview, pH and temperature not specified in the publication
0.0332
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wild-type Gap1 amino acid uptake activity, pH and temperature not specified in the publication
additional information
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ATP-binding subunit HisP with a carboxy-terminal extension of 8 amino acids
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
recombinant enzyme
5.8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.5
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about 30% of maximal activity at pH 6.0 and at pH 9.5
6.3 - 8
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
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30°C: about 40% of maximal activity, 55°C: about 80% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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up-regulation very early during rust development
Manually annotated by BRENDA team
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up-regulation very early during rust development
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49600
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predicted
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 1.5 A resolution
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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
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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; nucleotide-binding subunit HisP
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21
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expression in Pisum sativum and Vicia narbonensis seeds under control of the legumin B4 promoter
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expression in Saccharomyces cerevisiae mutant M4276
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expression in Spodoptera frugiperda 21
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expression of Gap1 mutants and of GFP-tagged Gap1p in a gap1DELTA car1DELTA sec6-4 strain that shows temperature sensitivity at 36°C
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expression of mutant enzymes in strains EK008 and EN121
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gene gap1, DNA and amino acid sequence analysis, expression analysis of wild-type and mutant enzymes in strain QA23
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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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into AT vector
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the Hut transport system is encoded by three genes, hutXWV
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UfAAT3 expression in Xenopus oocytes
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
W653C
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decreased ATP-dependent LTC4 transport
W653Y
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higher transport activity than wild-type enzyme
Y1302C
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decreased ATP-dependent LTC4 transport
Y1302W
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no effect of ATP binding and hydrolysis
A297V
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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
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site-directed mutagenesis, the mutation strongly affects both transport and signaling with citrulline and other amino acids
K9R/K16R
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site-directed mutagenesis, the mutant shows reduced activity with altered specificity compared to the wild-type enzyme
K9R/K16R/A297V
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site-directed mutagenesis, the mutant shows reduced activity with altered specificity compared to the wild-type enzyme
S392C
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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
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site-directed mutagenesis, the mutation strongly affects both transport and signaling with citrulline and other amino acids
Y395C
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site-directed mutagenesis, the mutation strongly affects both transport and signaling with citrulline and other amino acids
D149A
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mutation in histidine binding subunit HisJ, mutant protein is capable of interacting with HisQMP2 although at a much reduced level
D149N
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mutation in histidine binding subunit HisJ, mutant protein is capable of interacting with HisQMP2 although at a much reduced level
D61N
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mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis
E191K
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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
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mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme. Increased intrinsic ATPase activity without HisJ
H211R
-
mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis
K45P
-
mutation in the ATP-binding subunit HisP*, defective in ATP hydrolysis
R154D
-
mutation in histidine binding subunit HisJ, binds His as well as the wild type, defective in transport
R154S
-
mutation in histidine binding subunit HisJ, binds His as well as the wild type, defective in transport
T205A
-
mutation in the ATP-binding subunit HisP*, greater ease of HisP release from HisQM than in wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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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
additional information
Show AA Sequence (768 entries)
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