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Information on EC 7.2.2.12 - P-type Zn2+ transporter
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7.2.2.12 P-type Zn2+ transporterIUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme, present in prokaryotes and photosynthetic eukaryotes, exports Zn2+ and the related cations Cd2+ and Pb2+.
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Word Map
- 7.2.2.12
- autoantibody
-
islet
- pancreatic
- metallothioneins
- synaptic
-
slc30a8
- children
- vesicular
- mellitus
- autoantigens
- shoot
-
micronutrient
- iaa
-
enteropathica
-
insulinoma-associated
-
zinc-dependent
- beta-cell
-
antigen-2
- c-peptide
-
mossy
- acrodermatitis
- atpases
-
zinc-induced
-
zinc-deficient
-
metal-responsive
- insulinoma
-
autoantibody-positive
-
diabetes-associated
- znuabc
-
hyperaccumulator
-
biofortification
- tpen
- ehlers-danlos
-
phytoremediation
-
root-to-shoot
- cu+
-
dyshomeostasis
-
radiobinding
-
ketoacidosis
-
autometallography
-
islet-specific
-
histidine-rich
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
zinc transporter, athma4, p1b-type atpase, p1b-atpase, tchma4, zinc transporter 2, npunr4017, heavy metal atpase 2, atpase znta, zn(2+)-atpase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CadA
Cd/Zn transporting ATPase
EC 3.6.3.5
-
-
formerly
-
heavy metal ATPase 2
HMA2
HMA4
P-type ATPase
zinc-cadmium transporter
Zn(II)-translocating P-type ATPase
-
-
-
-
Zn,Cd-transporting P-type ATPase
-
-
-
-
Zn2+ ATPase
Zn2+-ATPase
Zn2+-transporting type-I ATPase
Zn2+/Cd2+-ATPase
ZntA
additional information
additional information
-
HMA1 is a member of the heavy metal-transporting ATPase family
additional information
-
the enzyme is a member of the P1B subfamily of the ATPases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + Zn2+[side 1] = ADP + phosphate + Zn2+[side 2]
-
-
-
-
ATP + H2O + Zn2+[side 1] = ADP + phosphate + Zn2+[side 2]
cadmium and zinc are removed from cells by the CzcCBA efflux pump and by two soft-metal-transporting P-type ATPases, CadA and ZntA.
-
ATP + H2O + Zn2+[side 1] = ADP + phosphate + Zn2+[side 2]
HMA2 and HMA4 play essential roles in the homeostasis of Zn.
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Zn2+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme, present in prokaryotes and photosynthetic eukaryotes, exports Zn2+ and the related cations Cd2+ and Pb2+.
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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 + Cd(thiolate)2 [side 1]
ADP + phosphate + Cd(thiolate)2 [side 2]
-
-
-
-
?
ATP + H2O + Pb(thiolate)2 [side 1]
ADP + phosphate + Pb(thiolate)2 [side 2]
-
-
-
-
?
ATP + H2O + Zn(thiolate)2 [side 1]
ADP + phosphate + Zn(thiolate)2 [side 2]
-
-
-
-
?
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
-
AtHMA4 functions as an efflux pump conferring both Cd and Zn resistance
-
-
?
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
97% of the activity with Zn2+
-
-
?
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
-
highest activity when the metal is present as thiolate complex with Cys or glutathione
-
?
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
-
dephosphorylation with EDTA
-
-
r
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
-
ZntA confers resistance specifically to Pb2+, Zn2+, and Cd2+ in Escherichia coli
-
-
?
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
-
-
-
-
?
ATP + H2O + Co2+/in
ADP + phosphate + Co2+/out
45% of the activity with Zn2+
-
-
?
ATP + H2O + Cu2+/in
ADP + phosphate + Cu2+/out
about 40% of the activity with Zn2+
-
-
?
ATP + H2O + Ni2+/in
ADP + phosphate + Ni2+/out
45% of the activity with Zn2+
-
-
?
ATP + H2O + Pb2+/in
ADP + phosphate + Pb2+/out
about 50% of the activity with Zn2+
-
-
?
ATP + H2O + Pb2+/in
ADP + phosphate + Pb2+/out
-
highest activity when the metal is present as thiolate complex with Cys or glutathione
-
?
ATP + H2O + Pb2+/in
ADP + phosphate + Pb2+/out
-
dephosphorylation with EDTA
-
-
r
ATP + H2O + Pb2+/in
ADP + phosphate + Pb2+/out
-
ZntA confers resistance specifically to Pb2+, Zn2+, and Cd2+ in Escherichia coli
-
-
?
ATP + H2O + Pb2+/in
ADP + phosphate + Pb2+/out
-
-
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
AtHMA4 functions as an efflux pump conferring both Cd and Zn resistance
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
HMA2 is responsible for Zn2+ efflux from the cells and is required for maintaining low cytoplasmic Zn2+ levels and normal Zn2+ homeostasis
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
overexpression of AtHMA4 improves the root growth in the presence of toxic concentrations of Zn,Cd and Co. A null mutant exhibits a lower translocation of Zn and Cd from the roots to shoot. The AtHMA4 overexpressing lines display an increase in the zinc and cadmium shoot content. AtHMA4 plays a role in metal loading in the xylem
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis thaliana by reducing the Zn content of Arabidopsis thaliana plastids, regulation, overview
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
the N-terminal domain of HMA2 is essential for function in planta while the C-terminal domain, although not essential for function, may contain a signal important for the subcellular localization of the protein
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
HMA2 has N- and C-terminal domains that can bind Zn ions with high affinity
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
-
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
highest activity when the metal is present as thiolate complex with Cys or glutathione
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
identification of a gene zntR encoding a Zn(II)-responsive transcriptional regulator that regulates zntA. ZntR is a member of the growing family of MerR-like prokaryotic transcriptional regulators
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
expression of ZntA is specifically induced by cadmium and less efficiently by zinc
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
dephosphorylation with EDTA
-
-
r
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
ZntA confers resistance specifically to Pb2+, Zn2+, and Cd2+ in Escherichia coli
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
-
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
-
-
-
?
additional information
?
-
-
The enzyme mediates active extrusion of Zn2+, which occurred during the exponential phase of growth. The effluxed Zn2+ are not ejected out of the cell but stored in the outer membrane and periplasm.
-
-
?
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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
additional information
?
-
-
The enzyme mediates active extrusion of Zn2+, which occurred during the exponential phase of growth. The effluxed Zn2+ are not ejected out of the cell but stored in the outer membrane and periplasm.
-
-
?
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
-
AtHMA4 functions as an efflux pump conferring both Cd and Zn resistance
-
-
?
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
-
ZntA confers resistance specifically to Pb2+, Zn2+, and Cd2+ in Escherichia coli
-
-
?
ATP + H2O + Cd2+/in
ADP + phosphate + Cd2+/out
-
-
-
-
?
ATP + H2O + Pb2+/in
ADP + phosphate + Pb2+/out
-
ZntA confers resistance specifically to Pb2+, Zn2+, and Cd2+ in Escherichia coli
-
-
?
ATP + H2O + Pb2+/in
ADP + phosphate + Pb2+/out
-
-
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
AtHMA4 functions as an efflux pump conferring both Cd and Zn resistance
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
HMA2 is responsible for Zn2+ efflux from the cells and is required for maintaining low cytoplasmic Zn2+ levels and normal Zn2+ homeostasis
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
overexpression of AtHMA4 improves the root growth in the presence of toxic concentrations of Zn,Cd and Co. A null mutant exhibits a lower translocation of Zn and Cd from the roots to shoot. The AtHMA4 overexpressing lines display an increase in the zinc and cadmium shoot content. AtHMA4 plays a role in metal loading in the xylem
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
AtHMA1 contributes to the detoxification of excess Zn(II) in Arabidopsis thaliana by reducing the Zn content of Arabidopsis thaliana plastids, regulation, overview
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
the N-terminal domain of HMA2 is essential for function in planta while the C-terminal domain, although not essential for function, may contain a signal important for the subcellular localization of the protein
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
identification of a gene zntR encoding a Zn(II)-responsive transcriptional regulator that regulates zntA. ZntR is a member of the growing family of MerR-like prokaryotic transcriptional regulators
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
expression of ZntA is specifically induced by cadmium and less efficiently by zinc
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
ZntA confers resistance specifically to Pb2+, Zn2+, and Cd2+ in Escherichia coli
-
-
?
ATP + H2O + Zn2+/in
ADP + phosphate + Zn2+/out
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Cs2+
-
ZntA confers resistance specifically to Pb2+, Zn2+, and Cd2+ in Escherichia coli. Wild-type ZntA binds two metal ions with high affinity, one in the N-terminal domain and another in the transmembrane domain
Cu2+
Pb2+
Zn2+
additional information
Cd2+
-
isoform HMA4 reaches maximal ATPase activity when all internal high-affinity Cd2+ binding sites are occupied
Cd2+
-
ligands and perhaps binding geometry of Pb(II) at the N-terminal metal site in ZntA are different from that of Zn(II) and Cd(II)
Cd2+
activates at 0.00003 mM, the level of activation does not change much until a concentration of 0.001 mM
Cd2+
-
isoform HMA4 reaches maximal ATPase activity when all internal high-affinity Cd2+ binding sites are occupied
Cd2+
-
the putative Zn2+/Cd2+-ATPase is truncated at the N-terminus and is activated in vitro by copper but not by zinc or cadmium. When expressed in Escherichia coli, however, the putative enzyme can be isolated as a full-length protein and the ATPase activity is increased by the addition of Zn2+ and Cd2+ as well as by Cu2+