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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+
Cu2+
-
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+
Pb2+
-
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)
Pb2+
-
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
Zn2+
-
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)
Zn2+
-
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. Wild-type ZntA binds two metal ions with high affinity, one in the N-terminal domain and another in the transmembrane domain
Zn2+
-
Zn2+ transport ATPase coordinates the metal via a tetrahedral coordination
Zn2+
activates at 0.00003 mM, the level of activation does not change much until a concentration of 0.0003 mM
Zn2+
-
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+
additional information
-
conserved aspartic acid 714 in transmembrane segment 8 of the ZntA Subgroup of P1B-type ATPases is as metal-binding residue
additional information
-
metal binding to the transmembrane site in ZntA or metal release from the transporter is the slow step in the reaction cycle. metal-binding to the N-terminal domain is not rate-limiting in the overall transport mechanism
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
vanadate
-
An inhibition of 30% of the total ATPase activity by 0.05 mM vanadate confirms the involvement of a P-type ATPase in the management of Zn2+.
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dimyristoyl-phosphatidylglycerol
-
solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol
1,2-dioleoyl-phosphatidylglycerol
-
solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol
1,2-dipalmitoyl-phosphatidylglycerol
-
solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol
1,2-distearoyl-phosphatidylglycerol
-
solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol
Phospholipid
-
solubilized ZntA is increased in the presence of negatively charged phospholipids and at slightly acidic pH. Among the most abundant naturally accuring phospholipids, only phosphatidyl-glycerol enhances the in vitro ATPase activity of TntA. Relipidation of detergent-purified ZntA with 1,2-dioleoylphosphatidyl-glycerol increases the ATPase activity 4fold compared to the purified state. Among the phosphatidylglycerol family, highest activity is observed for 1,2-dioleoyl-phosphatidylglycerol followed by 1,2-dimyristoyl-phosphatidylglycerol, 1,2-dipalmitoyl-phosphatidylglycerol and 1,2-distearoyl-phosphatidylglycerol
additional information
-
stimulated by an outwardly directed proton gradient
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.064
ATP
-
pH 7.0, 37°C, mutant lacking the N-terminal domain and both the CCCDXXC and GXXCXXC
0.004
Cd2+
-
pH 7.0, 37°C, mutant lacking the N-terminal domain and both the CCCDXXC and GXXCXXC
0.012
Pb2+
-
pH 7.0, 37°C, mutant lacking the N-terminal domain and both the CCCDXXC and GXXCXXC
0.009
Zn2+
-
pH 7.0, 37°C, mutant lacking the N-terminal domain and both the CCCDXXC and GXXCXXC
0.03589
Zn2+
-
carrier transport is stimulated by the addition of 1 mM ATP
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
300
ATP
in the presence of Zn2+ or Cd2+, in 0.6 M Tris, 2 M NaCl and 0.1 M MgCl2, pH 8.0, at 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
The activity with Ni2+, Co2+ and Cu2+ are extremely low, 10-20fold lower compared with the values obtained with Pb2+, Zn2+ and Cd2+.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
additional information
-
phosphorylation assays are carried out on ice and room temperature
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Salmonella enterica serovar typhimurium cells expressing the cadA gene of Geobacillus stearothermophilus
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
expression pattern of HMA1 invarious tissues of wild-type plants, HMA1 is expressed preferentially in shoots, including rosette leaves, cauline leaves, ?owers and stems, but little expression is observed in the roots, overview
brenda
-
AtHMA4 is expressed in tissues surrounding the root vascular vessels
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform ZntB is the main Zn2+ transporter of the endosome
brenda
-
isoform ZntB is the main Zn2+ transporter of the lysosome
brenda
-
isoform ZntA is the main Zn2+ transporter of the contractile vacuole
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
a prolonged accumulation of free zinc is observed in the DELTAzntA strain
malfunction
E7EC32
hma2 mutants have a significantly lower translocation ratio of Cd2+ and Zn2+ than the wild type enzyme
malfunction
-
enzyme deletion is associated with cytoplasmic Zn2+ accumulation, loss of secretory function and lactation failure. Enzyme deletion results in Zn2+-mediated degradation of phosphatase and tensin homolog, which impairs intercellular junction formation, prolactin receptor trafficking, and alveolar lumen development
malfunction
-
a prolonged accumulation of free zinc is observed in the DELTAzntA strain
-
physiological function
E7EC32
HMA2 is not responsible for the uptake of heavy metals but is a major transporter of zinc and cadmium from roots to shoots
physiological function
the enzyme is involved in Zn2+ and Cd2+ transport. Expression of HMA4 in tobacco (Nicotiana tabacum var. Xanthi) enhances Zn2+ translocation to the shoots only at 0.01 mM but not at 0.0005, 0.1 and 0.2 mM Zn2+. HMA4-expressing plants also show a decrease in cadmium uptake when exposed to 0.00025 and 0.005 mM Cd2+
physiological function
the protein is involved in xylem loading of zinc. Expression of P1B-ATPase HMA4 facilitates root-to-shoot zinc translocation and induces zinc uptake in a Zn2+ supply-dependent manner. Enzyme expression increases zinc excess, triggers iron deficiency in leaves and transcriptional activation of Fe-uptake systems in roots. Moreover, enzyme expression causes zinc overload of the apoplast, which may contribute to enhanced zinc sensitivity of transgenic tomato plants
physiological function
-
ZntA is up-regulated to efficiently lower the free zinc concentration
physiological function
disruption of transporter NpunR4017 results in a significant increase in zinc accumulation up to 24% greater than the wild-type, while cells overexpressing NpunR4107 accumulate 22% less than the wild-type. Accumulation of Zn2+ in ZntA-defective Escherichia coli overexpressing NpunR4017 is reduced by up to 21%
physiological function
-
transporter zntA and regulator zntR mutants are highly sensitive to CdCl2 and ZnCl2, and to a lesser extent to CoCl2. The inactivation of zntA increases the accumulation of intracellular cadmium and zinc, and confers hyperresistance to H2O2. The loss of either the zntA or zntR gene does not affect the virulence of Agrobacterium tumefaciens in Nicotiana benthamiana
physiological function
-
isoform HMA4 is mainly responsible for xylem loading of heavy metals for root to shoot transport
physiological function
-
isoform HMA4 is mainly responsible for xylem loading of heavy metals for root to shoot transport
physiological function
-
the enzyme is critical for appropriate mammary gland architecture. The interaction of the enzyme with V-ATPase critically mediates polarity establishment, alveolar development, and secretory function in the lactating mammary gland. The enzyme is required for the formation of acidified vesicles and secretion in mammary epithelial cells
physiological function
-
the enzyme is responsible for zinc and cadmium translocation from roots to shoots in Arabidopsis thaliana
physiological function
-
wheat heavy metal ATPase 2 can transport Zn2+ and Cd2+ across membranes and improves Zn2+ and Cd2+ tolerance in transgenic Arabidopsis thaliana
physiological function
Agrobacterium tumefaciens C58 / ATCC 33970
-
transporter zntA and regulator zntR mutants are highly sensitive to CdCl2 and ZnCl2, and to a lesser extent to CoCl2. The inactivation of zntA increases the accumulation of intracellular cadmium and zinc, and confers hyperresistance to H2O2. The loss of either the zntA or zntR gene does not affect the virulence of Agrobacterium tumefaciens in Nicotiana benthamiana
-
physiological function
-
ZntA is up-regulated to efficiently lower the free zinc concentration
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Show AA Sequence and Transmembrane Helices (2008 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
second subunit that contains the phosphorylation site, determined by SDS-PAGE and Western-blotting
60000
60000 - 70000
69000
-
the mutant lacking the N-terminal domain and both the CCCDXXC and GXXCXXC, SDS-PAGE
80000
92000
additional information
-
on PAA gels the protein is present in three forms, as a monomer with an apparent mass of 92 kDa, as a dimer of 190 kDa and as a proteolytic fragment of 67 kDa
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
additional information
dimer
-
on PAA gels the protein is present in three forms, as a monomer with an apparent mass of 92 kDa, as a dimer of 190 kDa and as a proteolytic fragment of 67 kDa
monomer
-
1 * 92000, also detection of a dimeric form of 190000 Da, SDS-PAGE
monomer
-
on PAA gels the protein is present in three forms, as a monomer with an apparent mass of 92 kDa, as a dimer of 190 kDa and as a proteolytic fragment of 67 kDa
additional information
-
HMA1 contains poly-His motifs that are commonly found in Zn(II)-binding proteins, but lacks some amino acids that are typical for this class of transporters
additional information
-
Lral transporter, lipoprotein, ATP-binding protein, integral membrane protein, encoded by operon mtsABC
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D149A
-
the mutant shows about 135% of wild type Zn2+-transporting activity
D313A
-
the mutant shows about 130% of wild type Zn2+-transporting activity
D688A
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the mutant shows about 20% of wild type Zn2+-transporting activity
DELTAN-HMA2
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mutant, lacking the N-terminal first 75 amino acids, 56% decrease in Vmax
DELTANC-HMA2
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mutant, lacking the N-terminal first 75 amino acids and the 244 C-terminal amino acids
E169A
-
the mutant shows about 25% of wild type Zn2+-transporting activity
F177A
-
the mutant shows about 95% of wild type Zn2+-transporting activity
F177L
-
the mutant shows about 40% of wild type Zn2+-transporting activity and reduced Cd2+-transporting activity (about 20%) compared to the wild type enzyme
G360A
-
the mutant shows about 75% of wild type Zn2+-transporting activity
K138A
-
the mutant shows about 110% of wild type Zn2+-transporting activity
K667A
-
the mutant shows about 30% of wild type Zn2+-transporting activity
N151A
-
the mutant shows about 70% of wild type Zn2+-transporting activity
P366L
-
the mutant shows about 15% of wild type Zn2+-transporting activity
V154A
-
the mutant shows about 60% of wild type Zn2+-transporting activity
V154S
-
the mutant shows about 60% of wild type Zn2+-transporting activity
A508F
-
at low ATP concentrations the mutant enzyme is poorly phosphorylated
C392A
-
mutant for evaluating the importance of the cysteine residue of the conserved 392CPC394 motif in metal ion binding
C392H
-
mutant for evaluating the importance of the cysteine residue of the conserved 392CPC394 motif in metal ion binding
C392H/C394H
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mutant for evaluating the importance of the cysteine residue of the conserved 392CPC394 motif in metal ion binding
C392S
-
mutant for evaluating the importance of the cysteine residue of the conserved 392CPC394 motif in metal ion binding
C392S/C394S
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mutant for evaluating the importance of the cysteine residue of the conserved 392CPC394 motif in metal ion binding
C394A
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mutant for evaluating the importance of the cysteine residue of the conserved 392CPC394 motif in metal ion binding
C394S
-
mutant for evaluating the importance of the cysteine residue of the conserved 392CPC394 motif in metal ion binding
C59A/C62A
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mutant enzyme in which the N-terminal metal-binding site is disabled by site-specific mutagenesis, can bind only one metal ion
D436N
-
the mutant is completely inactive with respect to both in vivo resistance and ATP hydrolysis activity
D714A
-
mutant enzyme is not able to confer resistance to Pb2+, Zn2+, and Cd2+ salts, large reduction in ATPase activity
D714E
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mutant enzyme is not able to confer resistance to Pb2+, Zn2+, and Cd2+ salts, large reduction in ATPase activity, retains the ability to bind metal ions with high affinity at the transmembrane site
D714H
-
mutant enzyme is not able to confer resistance to Pb2+, Zn2+, and Cd2+ salts, large reduction in ATPase activity, retains the ability to bind metal ions with high affinity at the transmembrane site
D714M
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significant metal-independent ATPase activity, poor phosphorylation by ATP and Pi
D714P
-
mutant enzyme is not able to confer resistance to Pb2+, Zn2+, and Cd2+ salts, large reduction in ATPase activity
E470A
-
metal ion-stimulated activity is reduced, about 30-40%. Mutant is phosphorylated more strongly in comparison to the wild type enzyme
G444V
-
mutation stabilizes the E2-P state. Gly144 might become close to P upon domain movements
G503S
-
at low ATP concentrations the mutant enzyme is poorly phosphorylated. The phosphorylation defect of the mutant enzyme can be partially compensated by using higher ATP concentrations
G505R
-
at low ATP concentrations the mutant enzymeis poorly phosphorylated. The phosphorylation defect of the mutant enzyme can be fully compensated by using higher ATP concentrations
H475A
-
mutant enzyme reacts poorly with ATP, mutation influences the binding of ATP and also other catalytic steps
H475D
-
mutant enzyme reacts poorly with ATP, mutation influences the binding of ATP and also other catalytic steps
H475L
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mutant enzyme reacts poorly with ATP, mutation influences the binding of ATP and also other catalytic steps
H475Q
-
metal ion-stimulated activity is reduced, about 30-40%. Mutant is phosphorylated more weakly in comparison to the wild type enzyme. Mutation affects the reaction with ATP and phosphate and stabilizes the enzyme in a dephosphorylated state
H475S
-
mutant enzyme reacts poorly with ATP, mutation influences the binding of ATP and also other catalytic steps
K693N
-
very low activity, no Cu2+-dependent phosphorylation with ATP, hyperphosphorylation by Pi, altered metal sensitivity of phosphorylation by Pi
K693N/D714M
-
very low activity and phosphorylation with ATP, almost normal phosphorylation with Pi, altered metal senstivity of Pi phosphorylation
P393A
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mutant, shows no activity and can not bind any metal ion at the transmembrane site
SAAS
-
mutation of two the two cysteines to serines in the CAAC motif near the N-terminus, ATPase activity 50%, diminished phosphorylation, faster dephosphorylation
SPS
-
mutation of two the two cysteines to serines in the CPC motif in transmembrane helix 6, inactive, very low phosphorylation
additional information
additional information
-
AtHMA4 and a truncated form lacking the last 457 amino acids both confer Cd and Zn resistance to yeast
additional information
-
expression of mutant derivatives, with and without a C-terminal GFP tag, from the HMA2 promoter in transgenic hma2,hma4, Zn-deficient plants. The deletion mutant lacking the C-terminal 244 amino acids rescues most of the hma2,hma4 Zn-deficiency phenotypes with the exception of embryo or seed development. Root-to-shoot Cd translocation is fully rescued. The GFP-tagged derivative is partially mislocalized in the root pericycle cells in which it is expressed. Deletion derivatives lacking the C-terminal 121 and 21 amino acids rescue all phenotypes and localize normally. N-terminal domain mutants localize normally but fail to complement the hma2,hma4 phenotypes, overview
additional information
-
sensitivity of Saccharomyces cerevisiae to high concentrations of Zn2+ is altered by the expression of AtHMA1 lacking its N-terminal chloroplast-targeting signal. Construction of HMA knockout plants showing as more pronounced sensitivity in the presence of high Zn2+ concentrations, and increased accumulation of Zn in the chloroplast of T-DNA insertional mutants of AtHMA1 compared to the wild-type, overview. The Zn2+-sensitive phenotype of AtHMA1 knock-out plants is complemented by the expression of AtHMA1 under the control of its own promoter. No organ-specific differences in the Zn content of hma1-1 mutants
additional information
-
in the plasmid-free strain AE104, single gene deletions of cadA or zntA have only a moderate effect on cadmium and zinc resistance, but zinc resistance decreases 6fold and cadmium resistance decreases 350fold in double deletion strains.
additional information
-
Construction of a mutant lacking the N-terminal domain and both the CCCDXXC and GXXCXXC. The activity of the mutant is similar to the wild-type. The Km for ATP is unchanged. The function of the amino-terminal domain may be to increase the overall catalytic rate by increasing the rate of binding of specific metal ions to the transporter.
additional information
-
DELTA-ZntA, in which the N-terminal domain is deleted can bind only one metal ion
additional information
-
N1-ZntA and N2-ZntA, containing residues 1-111 and 47-111 of ZntA, respectively, are characterized. N1-ZntA has both the CCCDGAC and GXXCXXC motifs, while N2-ZntA has only the GXXCXXC motif. N1-ZntA can bind both divalent metal ions such as Cd(II), Pb(II), and Zn(II) and monovalent metal ions such as Ag(I), with a stoichiometry of 1. N2-ZntA can bind Zn(II) and Cd(II) with a stoichiometry of 1 but not Pb(II). ZntA, which lacks the first 46 residues has the same activity as wild-type ZntA with respect to Cd(II) and Zn(II). Its activity with Pb(II) is similar to the mutant DELTAN-ZntA, which lacks the entire N-terminal domain
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme requires the presence of 20% (v/v) glycerol as stabilizing agent. The enzyme activity requires addition of lipids like soybean extract.
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 20% glycerol, 2 mM beta-mercaptoethanol, 0.5 mM PMSF
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-80°C, 100 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM Tris(2-carboxyethyl)phosphine hydrochoride
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
membranes from yeast are prepared, purification of the HMA2 C-terminal metal binding domain is performed using a Strep-Tactin Superflow column
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purification of the HMA2 N-terminal metal binding domain is performed using Strep-tag affinity chromatography, membranes from HMA2 expressing yeasts are prepared
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the recombinant mutant lacking the N-terminal domain and both the CCCDXXC and GXXCXXC
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Zn2+ affinity column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Arabidopsis thaliana HMA2 and truncated forms of the protein are prepared using the bacterial expression vector pPRIBA1 and the yeast expression vector pYES2/CT
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expression of wild-type HMA2 and mutant derivatives in transgenic hma2,hma4, Zn-deficient plants from the HMA2 promoter, quantitative realtime PCR expression analysis
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HMA1 DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative realtime RT-PCR expression analysis, expression in Saccharomyces cerevisiae
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identification of two independent mutant alleles for both genes, HMA2 and HMA4. The hma2-2 mutant is indistinguishable from the wild-type, whereas the hma4-1 and the double mutant hma2-2,hma4-1 accumulate approximately 2fold and 4fold less Zn, respectively, than the wild type.
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into the pBAD/Myc-Hic C or pBAD/Myc-His A vector for expression in the Escherichia coli strain LMG194(zntA::cat)
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into the pTRCHisA vector for expression in the Escherichia coli TOP 10 strain
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The cadA and zntA genes are located on the bacterial chromosome. Expression of zntA in Escherichia coli predominantly mediated resistance to zinc, and expression of cadA predominantly mediated resistance to cadmium.
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the PCR-amplified cadA gene from Geobacillus stearothermophilus is cloned into the expression vector pBAD-TOPO
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the yeast expression vector pYES2/CT carrying Arabidopsis thaliana HMA2 containing a C-terminal Strep-tag is prepared, the HMA2 N-terminal metal binding domain is cloned into the pPRIBA1 vector for expression in Escherichia coli BL21DE3pLysS cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after zinc shock (0.05 mM Zn2+), the mRNA level increases substantially in a zinc-dependent manner
expression of the zntA gene is inducible by CdCl2, ZnCl2 and CoCl2, of which CdCl2 is the most potent inducer. The metal-induced expression of zntA is controlled by the MerR-like regulator ZntR
in roots, isoform HMA4 is up-regulated in response to deficient Zn2+. In roots the isoform HMA4 expression is enhanced only in excess of metal (either Cd2+ orZn2+)
there is no significant difference in HMA2 expression after Cd2+ or Zn2+ treatment
E7EC32
treatment with 18 microM of zinc for 1 h, increases NpunR4017 mRNA levels by up to 1300% above basal levels
after zinc shock (0.05 mM Zn2+), the mRNA level increases substantially in a zinc-dependent manner
-
after zinc shock (0.05 mM Zn2+), the mRNA level increases substantially in a zinc-dependent manner
-
-
expression of the zntA gene is inducible by CdCl2, ZnCl2 and CoCl2, of which CdCl2 is the most potent inducer. The metal-induced expression of zntA is controlled by the MerR-like regulator ZntR
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expression of the zntA gene is inducible by CdCl2, ZnCl2 and CoCl2, of which CdCl2 is the most potent inducer. The metal-induced expression of zntA is controlled by the MerR-like regulator ZntR
Agrobacterium tumefaciens C58 / ATCC 33970
-
-
in roots, isoform HMA4 is up-regulated in response to deficient Zn2+. In roots the isoform HMA4 expression is enhanced only in excess of metal (either Cd2+ orZn2+)
-
in roots, isoform HMA4 is up-regulated in response to deficient Zn2+. In roots the isoform HMA4 expression is enhanced only in excess of metal (either Cd2+ orZn2+)
-
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IUBMB Life
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40
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Escherichia coli
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185
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Cupriavidus metallidurans
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J. Biol. Chem.
278
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Escherichia coli
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P-type ATPase heavy metal transporters with roles in essential zinc homeostasis in Arabidopsis
Plant Cell
16
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Arabidopsis thaliana
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Mechanism of zinc resistance in Pseudomonas putida strain S4
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17
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2001
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-
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The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP
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377
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2004
Escherichia coli
brenda
Dutta, S.J.; Liu, J.; Mitra, B.
Kinetic analysis of metal binding to the amino-terminal domain of ZntA by monitoring metal-thiolate charge-transfer complexes
Biochemistry
44
14268-14274
2005
Escherichia coli
brenda
Liu, J.; Stemmler, A.J.; Fatima, J.; Mitra, B.
Metal-binding characteristics of the aino-terminal domain of ZntA: binding of lead is different compared to cadmium and zinc
Biochemistry
44
5159-5167
2005
Escherichia coli
brenda
Dutta, S.J.; Liu, J.; Hou, Z.; Mitra, B.
Conserved aspartic acid 714 in transmembrane segment 8 of the ZntA Subgroup of P1B-type ATPases is as metal-binding residue
Biochemistry
45
5923-5931
2006
Escherichia coli
brenda
Liu, J.; Dutta, S.J.; Stemmler, A.J.; Mitra, B.
Metal-binding affinity of the transmembrane site in ZntA: implications for metal selectivity
Biochemistry
45
763-772
2006
Escherichia coli
brenda
Zimmer, J.; Doyle, D.A.
Phospholipid requirement and pH optimum for the in vitro enzymatic activity of the E. coli P-type ATPase ZntA
Biochim. Biophys. Acta
1758
645-652
2006
Escherichia coli
brenda
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Overexpression of AtHMA4 enhances root-to-shoot translocation of zinc and cadmium and plant metal tolerance
FEBS Lett.
576
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Arabidopsis thaliana
brenda
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The plant P1B-type ATPase AtHMA4 transports Zn and Cd and plays a role in detoxification of transition metals supplied at elevated levels
FEBS Lett.
579
783-791
2005
Arabidopsis thaliana
brenda
Eren, E.; Argueello, J.M.
Arabidopsis HMA2, a divalent heavy metal-transporting PIB-type ATPase, is involved in cytoplasmic Zn2+ homeostasis
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136
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Arabidopsis thaliana (Q9SZW4)
brenda
Parameswaran, A.; Leitenmaier, B.; Yang, M.; Kroneck, P.M.; Welte, W.; Lutz, G.; Papoyan, A.; Kochian, L.V.; Kuepper, H.
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363
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Noccaea caerulescens
brenda
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46
3692-3703
2007
Escherichia coli
brenda
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Novel Zn2+ coordination by the regulatory N-terminus metal binding domain of Arabidopsis thaliana Zn(2+)-ATPase HMA2
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46
7754-7764
2007
Arabidopsis thaliana
brenda
Okkeri, J.; Haltia, T.
The metal-binding sites of the zinc-transporting P-type ATPase of Escherichia coli. Lys693 and Asp714 in the seventh and eighth transmembrane segments of ZntA contribute to the coupling of metal binding and ATPase activity
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1757
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Escherichia coli
brenda
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281
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65Zn2+ transport by lobster hepatopancreatic lysosomal membrane vesicles
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-
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Arabidopsis thaliana
brenda
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Arabidopsis thaliana
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1818
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Escherichia coli
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Characterization of the PIB-type ATPases present in Thermus thermophilus
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194
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111
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Escherichia coli, Escherichia coli BW25113
brenda
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145
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Arabidopsis halleri (Q2I7E8)
brenda
Siemianowski, O.; Mills, R.F.; Williams, L.E.; Antosiewicz, D.M.
Expression of the P1B-type ATPase AtHMA4 in tobacco modifies Zn and Cd root to shoot partitioning and metal tolerance
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9
64-74
2011
Arabidopsis thaliana (P12265)
brenda
Satoh-Nagasawa, N.; Mori, M.; Nakazawa, N.; Kawamoto, T.; Nagato, Y.; Sakurai, K.; Takahashi, H.; Watanabe, A.; Akagi, H.
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53
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2012
Oryza sativa (E7EC32), Oryza sativa
brenda
Hudek, L.; Braeu, L.; Michalczyk, A.A.; Neilan, B.A.; Meeks, J.C.; Ackland, M.L.
The ZntA-like NpunR4017 plays a key role in maintaining homeostatic levels of zinc in Nostoc punctiforme
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99
10559-10574
2015
Nostoc punctiforme (B2J6J1), Nostoc punctiforme
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Chaoprasid, P.; Nookabkaew, S.; Sukchawalit, R.; Mongkolsuk, S.
Roles of Agrobacterium tumefaciens C58 ZntA and ZntB and the transcriptional regulator ZntR in controlling Cd2+/Zn2+/Co2+ resistance and the peroxide stress response
Microbiology
161
1730-1740
2015
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58 / ATCC 33970
brenda
Ravishankar, H.; Barth, A.; Andersson, M.
Probing the activity of a recombinant Zn2+-transporting P-type ATPase
Biopolymers
109
e23087
2018
Shigella sonnei (Q3YW59), Shigella sonnei Ss046 (Q3YW59)
brenda
Mishra, S.; Mishra, A.; Kpper, H.
Protein biochemistry and expression regulation of cadmium/zinc pumping ATPases in the hyperaccumulator plants Arabidopsis halleri and Noccaea caerulescens
Front. Plant Sci.
8
835
2017
Noccaea caerulescens, Arabidopsis halleri
brenda
Lee, S.; Rivera, O.; Kelleher, S.
Zinc transporter 2 interacts with vacuolar ATPase and is required for polarization, vesicle acidification, and secretion in mammary epithelial cells
J. Biol. Chem.
292
21598-21613
2017
Mus musculus
brenda
Barisch, C.; Kalinina, V.; Lefrancois, L.H.; Appiah, J.; Lopez-Jimenez, A.T.; Soldati, T.
Localization of all four ZnT zinc transporters in Dictyostelium and impact of ZntA and ZntB knockout on bacteria killing
J. Cell Sci.
131
222000
2018
Dictyostelium discoideum
brenda
Lekeux, G.; Crowet, J.M.; Nouet, C.; Joris, M.; Jadoul, A.; Bosman, B.; Carnol, M.; Motte, P.; Lins, L.; Galleni, M.; Hanikenne, M.
Homology modeling and in vivo functional characterization of the zinc permeation pathway in a heavy metal P-type ATPase
J. Exp. Bot.
70
329-341
2019
Arabidopsis thaliana
brenda
Qiao, K.; Gong, L.; Tian, Y.; Wang, H.; Chai, T.
The metal-binding domain of wheat heavy metal ATPase 2 (TaHMA2) is involved in zinc/cadmium tolerance and translocation in Arabidopsis
Plant Cell Rep.
37
1343-1352
2018
Triticum aestivum
brenda
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EXTERNAL LINKS (specific for EC-Number 7.2.2.12)
Transporter Classification Database (TCDB): 3.A.3.6.6, 3.A.3.6.7, 3.A.3.6.19, 3.A.3.6.20, 3.A.3.6.17, 3.A.3.6.18, 3.A.3.6.3, 3.A.3.6.2, 3.A.3.6.10
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Release 2023.1 (January 2023)
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