Information on EC 3.6.3.3 - Cd2+-exporting ATPase

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

EC NUMBER
COMMENTARY hide
3.6.3.3
-
RECOMMENDED NAME
GeneOntology No.
Cd2+-exporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Cd2+/in = ADP + phosphate + Cd2+/out
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (Cd2+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme occurs in protozoa, fungi and plants.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
AtHMA3 gene
SwissProt
Manually annotated by BRENDA team
strain CU1065
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
soil isolate
UniProt
Manually annotated by BRENDA team
soil isolate
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain LV
SwissProt
Manually annotated by BRENDA team
strain LV
SwissProt
Manually annotated by BRENDA team
cultivars Cho-Ko-Koku, Akita 63, and IR24
-
-
Manually annotated by BRENDA team
gene cadA; 06909 strain
SwissProt
Manually annotated by BRENDA team
gene cadA; 06909 strain
SwissProt
Manually annotated by BRENDA team
BY4741 haploid strain
-
-
Manually annotated by BRENDA team
serovar Typhimurium, use of wild type and a cadmium senitive zntA-knockout mutant, expression of cadA gene from Geobacillus stearothermophilus LV in wild type yields a cadmium hypersensitive phenotype, when the zntA-knockout mutant is used cadmium sensitivity is reverted
SwissProt
Manually annotated by BRENDA team
strains 2011 and 1021
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
the root cell cytoplasm of Cd-overaccumulating rice plants has more Cd available for loading into the xylem as a result of the lack of HMA3-mediated transportation of Cd to the vacuoles
physiological function
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 + Cd2+/in
ADP + phosphate + Cd2+/out
show the reaction diagram
ATP + H2O + Cd2+/out
ADP + phosphate + Cd2+/in
show the reaction diagram
-
-
-
-
?
ATP + H2O + Pb2+/in
ADP + phosphate + Pb2+/out
show the reaction diagram
-
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
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 + Cd2+/in
ADP + phosphate + Cd2+/out
show the reaction diagram
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
enzyme can perform its cycle in the absence of Mg2+, using CdATP2- in the place of MgATP2-
Mg2+
-
uptake of Cd2+ is Mg-ATP-dependent
additional information
-
Cd2+ uptake is unaffected by Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bafilomycin
-
-
-
bafilomycin A
-
-
Fe2+
-
inhibits cellular Cd2+ uptake through a competitive interaction
N,N'-dicyclohexylcarbodiimide
-
-
N-ethylmaleimide
-
inhibits the formation of the phosphoenzyme, effect can be supressed in presence of Cd2+
nigericin
-
-
nitrate
-
-
orthovanadate
-
Cd2+ uptake by plasma membranes is almost completely reduced in the presence of 1 mM orthovanadate. The relevant process observed in the tonoplasts is strongly reduced by both, 0.1 mM (up to 40% in control and Cd-stressed plants) and 1 mM Na2VO4 (up to 25% and 20% in control plants and stressed plants, respectively)
Pb(OAc)2
-
inhibits transport of Pb(II)
Zn2+
-
inhibits cellular Cd2+ uptake through a competitive interaction
additional information
-
pre-exposure to either 0.01 or 0.1 mM orthovanadate does not affect the cellular Cd2+ uptake rate. After 60 min efflux, approximately 40% and 20% of accumulated Cd2+ in the enterocytes is lost in the absence and presence of orthovanadate, respectively, when compared to 0 min. Pre-exposure to verapamil or lanthanum does not exhibit any effects on the cellular Cd2+ uptake rate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
the inducing effect of cadmium on Pca1 expression is independent of epitope or its location
dithiothreitol
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170% increase of Cd2+ transport across plasma membranes at 5 mM. Cd transport across tonoplasts is stimulated up to 125% by 5 mM dithiothreitol
GSH
-
200% increase of Cd2+ transport across plasma membranes at 5 mM. Cd transport across tonoplasts is stimulated up to 160% by 5 mM GSH
HCO3-
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cellular Cd2+ uptake increases in the presence of HCO3-
L-cysteine
-
200% increase of Cd2+ transport across plasma membranes at 50 mM. Cd transport across tonoplasts is stimulated up to 120% by 50 mM L-cysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00086 - 0.00193
Cd2+/out
additional information
additional information
-
the range of 0.1-10 microM of added CdCl2 corresponds to Cd2+ binding at the transport site of unphosphorylated enzyme which induces the reaction of the enzyme with ATP and impairs the reaction with phosphate. The 0.1-1 mM range of added CdCl2 corresponds to Cd2+ binding to the transport site accessible from the extracellular medium
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
Fe2+
Oncorhynchus mykiss
-
pH and temperature not specified in the publication
0.0098
Zn2+
Oncorhynchus mykiss
-
pH and temperature not specified in the publication
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
found in all tissues, with highest levels in roots and cauline leaves
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme in Saccharomyces cerevisiae
Manually annotated by BRENDA team
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G970R mutation affects correct trafficking of the protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
-
x * 70000, SDS-PAGE
76000
x * 76000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
N-terminal binding-domain with bound metal ion
monomer
N-terminal binding-domain without bound metal ion
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structural analysis of N-terminal enzyme domain, soluble monomeric protein of 71 amino acids, by NMR and X-ray absorption spectroscopy
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminal binding-domain from Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complementation studies by expression in Saccharomyces cerevisiae; complementation studies by expression in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain BY4743
-
expression in Escherichia coli
expression in Saccharomyces cerevisiae for a complementation screening
expression in Saccharomyces cerevisiae, expression in the Cd-sensitive yeast strain Y04069 complements the mutation
expression in Sf9 cells of the native enzyme and a truncated peptide lacking the metal-binding domain
-
expression of a mutant protein in Bacillus subtilis, the resulting strain shows higher sensitivity to Cd2+, Zn2+ and Co2+ than the wild type
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expression of gene in Salmonella enterica serovar Typhimurium yields a cadmium hypersensitive phenotype, when a zntA-knockout mutant of Salmonella enterica (cadmium senitive) is used cadmium sensitivity is reverted
N-terminal binding-domain of 71 amino acids carrying a S71A mutation expressed in Escherichia coli M15
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C354A
-
transmembrane segment 6, participation in Cd2+ binding, inactive in transport of Cd2+, no ATPase activity
C356A
-
transmembrane segment 6, participation in Cd2+ binding, inactive in transport of Cd2+
D398A
-
no enzymic activity
D692A
-
transmembrane segment 8, participation in Cd2+ binding, inactive in transport of Cd2+, no ATPase activity
E164A
-
transmembrane segment 4, reduced ATPase activity
M149A
-
transmembrane segment 3, participation in Cd2+ binding, reduced ATPase activity
P355A
-
transmembrane segment 6, reduced ATPase activity
C298A/C300A
-
site-directed mutation of the CXC motif abolishes copper resistance but not cadmium resistance
C311A/C312A
-
site-directed mutation of the CC motif abolishes cadmium resistance yet retains the ability to confer copper resistance
G970R
-
naturally occurring missense mutation presented in a number of yeast laboratory strains, loss of function, mutation is not found in wild type strains
C298A/C300A
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site-directed mutation of the CXC motif abolishes copper resistance but not cadmium resistance
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C311A/C312A
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site-directed mutation of the CC motif abolishes cadmium resistance yet retains the ability to confer copper resistance
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
expression of enzyme in Saccharomyces cerevisiae strikingly decreases Cd2+ tolerance of yeast cells. Yeast expressing the non-functional mutant D398A can grow on selective medium containing up to 0.1 mM Cd2+, while those expressing the intact enzyme cannot grow in presence of 0.001 mM Cd2+. Enzyme is localized in the endoplasmic reticulum, so hypersensitivity to Cd2+ is due to Cd2+ accumulation in the reticulum lumen. Zn2+ does not protect cells against Cd2+ poisoning
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