Information on EC 3.6.3.27 - phosphate-transporting ATPase

Word Map on EC 3.6.3.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
3.6.3.27
-
RECOMMENDED NAME
GeneOntology No.
phosphate-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + phosphate/out = ADP + phosphate + phosphate/in
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric acid anhydride
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (phosphate-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. A bacterial enzyme that imports phosphate anions.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Westar
-
-
Manually annotated by BRENDA team
cultivar Nannongyinshan
-
-
Manually annotated by BRENDA team
ATCC 824, four pst genes within the pst operon
-
-
Manually annotated by BRENDA team
opossum
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
duckweed
-
-
Manually annotated by BRENDA team
cv. Jemalong
-
-
Manually annotated by BRENDA team
strain SG34, genes pstS and phnD
-
-
Manually annotated by BRENDA team
strain H37Rv
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
wild-type strain W115, and mutator line W138 containing an active endogenous dTph1 transposable element system
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
alfalfa symbiont in root nodules, strain 1021, gene pstSCAB
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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 + arsenate/out
ADP + phosphate + arsenate/in
show the reaction diagram
ATP + H2O + phosphate/out
ADP + phosphate + phosphate/in
show the reaction diagram
CTP + H2O + phosphate/out
CDP + phosphate + phosphate/in
show the reaction diagram
GTP + H2O + phosphate/out
GDP + phosphate + phosphate/in
show the reaction diagram
additional information
?
-
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 + phosphate/out
ADP + phosphate + phosphate/in
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
stimulates 5fold
additional information
-
no activation with Ca2+, Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-p-fluorosulfonylbenzoyl adenosine
-
pH 7.4, 30 min at 30°C, 1-3 mM
arsenate
arsenic acid
carbonylcyanide 3-chlorophenylhydrazone
-
inhibits phosphate uptake in vivo
D-glucose 6-phosphate
37.5% inhibition at 2.5 mM
diphosphate
26% inhibition at 2.5 mM
glutamate
56% inhibition at 2.5 mM
guanidine hydrochloride
-
5 min at 100°C, 8000 mM, significant reduction in the activity
Li+
indirect inhibition
methylphosphonate
Mn2+
-
at room temperature
phosphate
substrate inhibition, 85.5% inhibition at 2.5 mM
phosphite
-
competitive, partial inhibition of phosphate transport activity, overview
phosphonate
-
competitive, partial inhibition of phosphate transport activity, overview
potassium dihydrogen phosphate
-
96% inhibition at 0.04 mM
Selenite
competitively inhibits phosphate uptake; competitively inhibits phosphate uptake; competitively inhibits phosphate uptake; competitively inhibits phosphate uptake
sulfate
21% inhibition at 2.5 mM
vanadate
26% inhibition at 2.5 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0239 - 0.654
ATP
0.13
CTP
-
at 37 °C, pH 7.5
0.211
GTP
-
at 37 °C, pH 7.5
0.0002 - 6.3
phosphate
0.0019 - 0.385
phosphate/out
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
5'-p-fluorosulfonylbenzoyl adenosine
-
pH 7.4, at 30°C
4.6 - 5.5
Selenite
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
assay at
7
-
assay at
additional information
-
expression of the pst genes is 8fold better at pH 5.8 compared to pH 4.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
PstS substrate-binding subunit, isoelectric focusing
7.1
sequence calculation, Pht1-4
7.6
sequence calculation, Pht1-1; sequence calculation, Pht1-2; sequence calculation, Pht1-3
8.2
sequence calculation, Pht1-6
8.6
-
calculated from amino acid sequence
8.8
sequence calculation, Pht1-5
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
localised to the external hyphae of Piriformospora indica colonized with maize plant root, which suggests that external hyphae are the initial site of phosphate uptake from the soil
Manually annotated by BRENDA team
endogenous PiT1 mRNA level is decreased in dense MC3T3-E1 cell cultures
Manually annotated by BRENDA team
-
PiT-2: expression analysis
Manually annotated by BRENDA team
-
PiT-2: expression analysis
Manually annotated by BRENDA team
-
proximal, PiT-2: expression analysis in younger and older rats
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
expression of Pit-1 and Pit-2, Pit-1 is not a component of matrix vesicles or apoptotic bodies, expression analysis, Pit-1 is the predominant sodium-dependent phosphate cotransporter, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
on the surface of the outer
Manually annotated by BRENDA team
-
PstS, PstBA, PstBB
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
x * 30000, SDS-PAGE
30500
-
PstB is the ATP-binding component, 2 * 30500, SDS-PAGE
35000
x * 35000, SDS-PAGE, x * 50500, about, processed enzyme, sequence calculation
45000
x * 45000, about, thylakoid membrane enzyme, SDS-PAGE, x * 56500, unprocessed enzyme containing the chloroplast transit peptide, SDS-PAGE, x * 50700, processed enzyme without transit peptide, SDS-PAGE
50500
x * 35000, SDS-PAGE, x * 50500, about, processed enzyme, sequence calculation
50700
x * 45000, about, thylakoid membrane enzyme, SDS-PAGE, x * 56500, unprocessed enzyme containing the chloroplast transit peptide, SDS-PAGE, x * 50700, processed enzyme without transit peptide, SDS-PAGE
54000
-
mutant lacking N-terminal SPX domain DELTA1-375
56100
x * 56100, sequence calculation, Pht1-5
56500
x * 45000, about, thylakoid membrane enzyme, SDS-PAGE, x * 56500, unprocessed enzyme containing the chloroplast transit peptide, SDS-PAGE, x * 50700, processed enzyme without transit peptide, SDS-PAGE
57700
calculated from cDNA
57970
-
x * 57970, calculated from amino acid sequence
58000
-
x * 58000, about, sequence calculation
58300
x * 58300, sequence calculation, Pht1-3
58400
x * 58400, sequence calculation, Pht1-4
58800
x * 58800, sequence calculation, Pht1-1; x * 58800, sequence calculation, Pht1-2
60600
x * 60600, sequence calculation, Pht1-6
69300
-
gel filtration chromatography
98000
-
wild-type
100000
-
x * 100000, green fluorescent protein-tagged enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
the periplasmic domain GP-56 is N-and O-glycosylated, identification of 6 predicted N-glycosylation sites and two predicted O-glycosylation sites, Thr273 and Thr306, overview
no modification
phosphoprotein
-
phosphory lation events occur at the C-end of PHT1 proteins when phosphate is abundant in the environment. Phosphorylation of other Arabidopsis thaliana members of the family, PHT1;4, PHT1;5; PHT1;7, and PHT1;9, at the C-end of the protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with phosphate, sitting drop vapor diffusion method, using 0.1 M sodium acetate, 0.2 M zinc acetate pH 4.5, and 10% (w/v) PEG 3000
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24 - 80
-
pH 7.5, for 5 min, enzyme is heat-resistant
37
-
pH 7.5, for 5 min, substantial loss in the enzyme activity at temperatures above 37°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by gel filtration chromatography using Superdex 200 column
-
by gel permeation chromatography using Superdex 200 column
-
HisTrap nickel affinity column chromatography and Superdex 75 gel filtration
native enzyme partially by preparation of chloroplasts and thylakoid membranes
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of genes pstS, pstC, pstA, and pstB from the pst operon, genetic architecture, DNA and amino acid sequence determination and analysis, expression analysis in cells
-
DNA and amino acid sequence determination and analysis, expression analysis, functional overexpression of the enzyme as His6-Xpress-ANTR1-FLAG fusion protein in Escherichia coli, the recombinantly expressed Arabidopsis ANTR1 facilitates Na+-dependent phosphate transport into Escherichia coli
DNA and amino acid sequence determination of the pst operon, genes pstS and pstA expression is regulated by the two-component regulatory system PhoBR and is repressed until times of phosphate starvation
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)-pGro7/GroEL cells
expressed in Glycine max cultivar Xinliaoxian
-
expressed in Saccharomyces cerevisiae and Nicotiana benthamiana leaves
-
expressed in Xenopus laevis oocytes
-
expressed in yeast MB192 strain and Xenopus laevis oocytes
-
expressed in yeast strain MB192
-
expressed in yeast strain MN192
expressed using the baculoviruses expression system
-
expression in transgenic Arabidopsis thaliana plants by Agrobacterium tumefaciens strain EHA105 transfection method, expression of recombinant GFP- and YFP-tagged Pht1;9 in Arabidopsis thaliana protoplasts via polyethylene glycol transformation
-
expression of a mycorrhiza-inducible bifunctional reporter transgene and insertional mutagenesis in Petunia hybrida strain W115, bidirectionalization of a mycorrhizal phosphate transporter promoter StPT3 controlling the expression of two reporter genes encoding firefly luciferase and GUS allows visualization of mycorrhiza-specific phosphate transporter expression
-
expression of HvPHT1;1 in Allium cepa epidermal cell plasma membranes from gateway-enabled pMDC83 vector with HvPHT1;1 being placed in-frame, upstream of the mGFP6 gene
gene PHO84, DNA and amino acid sequence determination and analysis, expression analysis
-
gene pht1-1, computational DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression pattern and regulation, overview; gene pht1-2, computational DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression pattern and regulation, overview; gene pht1-3, computational DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression pattern and regulation, overview; gene pht1-4, computational DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression pattern and regulation, overview; gene pht1-5, computational DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression pattern and regulation, overview; gene pht1-6, computational DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression pattern and regulation, overview
gene PHT1;1 mapped to locus to chromosome V, expression analysis, overview
-
gene pht4;2, DNA and amino acid sequence determination and analysis, genetic organization, PHT4;2 is located adjacent to DEETIOLATED2 (DET2) on chromosome 2 (loci At2g38060 and At2g38050, respectively), with 550 bp between the PHT4;2 stop codon and the DET2 translation start site, quantitative RT-PCR expression analysis, recombinant expression of the processed enzyme
gene pstSCAB, the expression is regulated by PhoB, which binds to the pstSCAB promoter at two binding sites
-
gene PT1, isolation of root-specific promoter sequence of gene PT1 by utilizing the gene-space sequence information, root-specific expression of GFP-tagged GUS-fusion enzymes in Arabidopsis thaliana and in transgenic roots of Medicago truncatula using the Agrobacterium tumefaciens transfection system, expression patterns, overview; gene PT2, isolation of root-specific promoter sequence of gene PT2 by screening of a genomic library, root-specific expression of GFP-tagged GUS-fusion enzymes in Arabidopsis thaliana and in transgenic roots of Medicago truncatula using the Agrobacterium tumefaciens transfection system, expression patterns, overview
genes pstA-2, pstC-1 and pstB
-
genes pstS-3 and pstC-2
-
GmPT1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in yeast MB192 mutant cells, expression as GFP-tagged protein in onion epidermal cells from chimeric gene CaMV35S-GmPT1 introduced into the cells by a particle bombardment system; GmPT2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in yeast MB192 mutant cells, expression as GFP-tagged protein in onion epidermal cells from chimeric gene CaMV35S-GmPT1 introduced into the cells by a particle bombardment system
MtPT4-GFP and MtPT1 expression from the MtPT4 and MtPT1 promoter, respectively, in Medicago truncatula plants in the periarbuscular membrane, and from the 35S promoter in roots and in the vacuole of vascular tissue cells. The plasma membrane GFP signal appears substantially weaker in cells harboring arbuscules than in other cortical cells. MtPT1-GFP fusions were expressed from the MtBcp1 promoter, which is active in cortical cells both before and during arbuscule formation. Phenotype of roots expressing pMtBcp1:MtPT4-GFP, overview
-
OsPT1 semi-quantitative RT-PCR and real time quantitative RT-PCR expression analyses
-
overexpression in Escherichia coli
-
overexpression of Pit-1 in immortalized human aortic smooth muscle cells
-
pst and phn operons, the Phn system is encoded by a three-gene operon, DNA and amino acid sequence determinations and analysis, genomic organization, expression analyis of pstS and phnD, overview
-
pstA is organized in the pst operon
-
pstS expression analysis in wild-type strain R6, R6 muant strains, and diverse clinical isolates, overview
-
PT4, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression analysis, expression and complementation in yeast mutant PAM2
PT4, single copy gene, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression analysis, expression and complementation in yeast mutant PAM2
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
1.3 kb promoter of TaPHT1.2 contains a number of phosphate-starvation responsive elements, including P1BS, WRKY-binding W-box, and helix-loop-helix-binding elements. Reporter gene expression analysis using this 1.3 kb promoter of TaPHT1.2 shows that the reporter gene is specifically induced by Pi-starvation and predominantly expressed in the roots
-
circadian expression of phosphate transporter gene pht4;1 is dependent on the protein circadian clock associated 1
-
enzyme expression is elevated in response to low phosphate
enzyme expression is specifically induced by phosphate starvation
-
enzyme expression is triggered in phosphate-starved mycorrhizal roots; enzyme expression is triggered in phosphate-starved mycorrhizal roots
expression of isoform PT13 is induced by 0.01 and 0.1 mM As(V) treatment, while isoforms PT5 and PT10 are induced only by 0.1 mM As(V)
-
in gametophytes, Pht1;3 transcript levels increase in response to phosphate deficiency and arsenate exposure
-
in roots, expression of isoform PT2 and PT3 is strongly inhibited by 0.01 and 0.1 mM As(V) treatment
-
OsPT1 expression is strongly enhanced by mutation of phosphate over-accumulator 2, OsPHO2, but not by phosphate starvation response 2, OsPHR2. OsPT8 and OsPT4 are significantly and moderately upregulated, respectively, in OsPT1 overexpressing plants
-
PHO84, encoding the high-affinity H+/phosphate symporter, expression is activated by the Pho4 transcription factor in phosphate-starved cells as part of the PHO signalling pathway
Pht1;9 is induced by phosphate starvation
the HvPHT1;1 gene is largely induced by phosphate starvation
the Pht1;4 induction by phosphate deficiency is dependent on the existence of sugar
-
transcription of PHO87 and PHO90, encoding the low-affinity H+/phosphate transport system, is independent of phosphate status
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D228E
-
drastic increase in expression compared to wild-type, mutant shows no transport activity
D382A
-
Km: (phosphate) 0.057 mM (in the presence of 25 mM NaCl), 0.49 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 156 nmol/mg of protein/h, results indicate that Arg-228 may participate in interactions associated with protein conformational changes required for full transport activity
D382E
-
Km: (phosphate) 0.046 mM (in the presence of 25 mM NaCl), 0.73 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 96 nmol/mg of protein/h, drastic increase in expression compared to wild-type, results indicate that Arg-228 may participate in interactions associated with protein conformational changes required for full transport activity
D382N
-
mutant shows no transport activity
R120K
-
Km: (phosphate) 0.161 mM (in the presence of 25 mM NaCl), 1.48 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 250 nmol/mg of protein/h, results indicate that Arg-120 may be important for binding and translocation of the substrate
R201K
-
Km: (phosphate) 0.214 mM (in the presence of 25 mM NaCl), 2.29 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 100 nmol/mg of protein/h, results indicate that Arg-201 may be important for binding and translocation of the substrate
R228K
-
drastic increase in expression compared to wild-type, Km: (phosphate) 0.103 mM (in the presence of 25 mM NaCl), 1.99 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 274 nmol/mg of protein/h, drastic increase in expression compared to wild-type, results indicate that Arg-228 may participate in interactions associated with protein conformational changes required for full transport activity
S124A
-
Km: (phosphate) 0.0448 mM (in the presence of 25 mM NaCl), 0.27 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 47 nmol/mg of protein/h, results indicate that Ser-124 may function as a transient binding site for Na+ ions in close proximity to the periplasmic side
S124T
-
Km: (phosphate) 0.109 mM (in the presence of 25 mM NaCl), 0.88 mM (in the presence of various concentrations of NaCl), Vmax (adjusted to the protein expression levels): 254 nmol/mg of protein/h, results indicate that Ser-124 may function as a transient binding site for Na+ ions in close proximity to the periplasmic side
E240Q
-
mutation in pstC, loss of phosphate transport through the pst system, alkaline phosphatase activity remains repressed
G48I
-
mutation in pstB, loss of phosphate transport through the Pst system and derepression of alkaline phosphatase activity
K49Q
-
mutation in pstB, loss of phosphate transport through the Pst system and derepression of alkaline phosphatase activity
P123L
-
mutation in pstC, loss of phosphate transport activity
P123L/P166L
-
mutation in pstA, complete loss of phosphate transport activity
P132L
-
mutation in pstA, partial loss of phosphate uptake activity
P166L
-
mutation in pstA, partial loss of phosphate uptake activity
P183L
-
mutation in pstC, loss of phosphate transport activity
R238Q
-
mutation in pstC, loss of phosphate transport through the pst system, alkaline phosphatase activity remains repressed
R238Q/E240Q
-
mutation in pstC, loss of phosphate transport through the pst system, alkaline phosphatase activity remains repressed
S115F
-
mutant MtPT4S115F is retained in the endomembrane system and colocalizes with endoplasmic reticulum and trans-Golgi network markers. Mutation of this residue disrupts a conserved process in phosphate transporter trafficking
S117F
-
mutant MtPT1S117F is retained in the endomembrane system and colocalizes with endoplasmic reticulum and trans-Golgi network markers. Mutation of this residue disrupts a conserved process in phosphate transporter trafficking
S115F
-
mutant MtPT4S115F is retained in the endomembrane system and colocalizes with endoplasmic reticulum and trans-Golgi network markers. Mutation of this residue disrupts a conserved process in phosphate transporter trafficking
-
S117F
-
mutant MtPT1S117F is retained in the endomembrane system and colocalizes with endoplasmic reticulum and trans-Golgi network markers. Mutation of this residue disrupts a conserved process in phosphate transporter trafficking
-
R138A
-
mutant possesses Na+/phosphate cotransport activity comparable to that of the wild type protein, but the DELTA PSI-dependent anion transport is inactive
DELTA1-375
-
mutant lacking the entire N-terminal SPX domain shows no differences in protein level or plasma membrane localisation compared to wild-type, phosphate uptake-rate is higher compared to wild-type, Km remains in the same range as wild-type, truncated mutant has increased catalytic activity
additional information
Show AA Sequence (15448 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.