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Information on EC 7.2.2.9 - P-type Cu2+ transporter and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SH30

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IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic archaeon Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9SH30
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
atp7b, atp7a, copper transporter, copper-transporting atpase, copper-transporting p-type atpase, menkes protein, cu-atpase, copper transporting p-type atpase, copper atpase, copper-transporting p-type, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu-transporting P1B-1-type ATPase
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moe
HMA5 belongs to a large family of genes encoding P1B-type cation-transporting ATPases
adenosine 5'-triphosphatase
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-
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ATP hydrolase
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ATP phosphohydrolase
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-
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ATP7B
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-
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ATPase
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-
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complex V
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-
-
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copper-transporting ATPase
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copper-transporting ATPase PAA1
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copper-transporting P-type ATPase
Cu2+-ATPase
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-
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CUA-1 ATPase
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-
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Menkes disease-associated protein
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-
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Menkes disease-associated protein homolog
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-
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Menkes P-type ATPase
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-
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MNK
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-
-
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Paa1 P-type ATPase
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Paa2 P-type ATPase
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Pinal night-specific ATPase
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-
-
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RAN1
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response to antagonist 1
WCBD
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-
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Wilson copper-transporting P-type ATPase
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-
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Wilson disease copper-transporting ATPase
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Wilson disease protein
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Wilson disease-associated protein
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Wilson disease-associated protein homolog
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Cu2+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic archaeon Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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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 + Cu2+/in
ADP + phosphate + Cu2+/out
show the reaction diagram
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-
-
?
ATP + H2O + Cu+/in
ADP + phosphate + Cu+/out
show the reaction diagram
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-
-
?
ATP + H2O + Cu2+/in
ADP + phosphate + Cu2+/out
show the reaction diagram
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-
-
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r
additional information
?
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the variation in Cu tolerance of Arabidopsis is regulated by the functional integrity of the Cu-translocating ATPase, HMA5, and in particular the amino acid sequence in several strictly conserved motifs, molecular mechanism of Cu tolerance, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + Cu2+/in
ADP + phosphate + Cu2+/out
show the reaction diagram
-
-
-
?
additional information
?
-
the variation in Cu tolerance of Arabidopsis is regulated by the functional integrity of the Cu-translocating ATPase, HMA5, and in particular the amino acid sequence in several strictly conserved motifs, molecular mechanism of Cu tolerance, overview
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
the enzyme is activated by silver ions with an apparent affinity in the micromolar range (40% activation at 0.005 mM compared to Cu+)
Cu+
the enzyme is preferentially activated by monovalent copper ions with an apparent affinity in the micromolar range (100% activation at 0.005 mM)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
inner membrane of the chloroplast envelope
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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ran1 mutants display ethylene-like responses to the ethylene antagonist trans-cyclooctene and have altered copper homeostasis
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HMA5_ARATH
995
8
108336
Swiss-Prot
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
PAA1 is phosphorylated from ATP in the presence of monovalent metals (only CuCl2 and AgNO3). The presence of EGTA does not affect the phosphorylation levels
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N923T
mutation in the Cvi allele in the tightly conserved domain N(x)6YN(x)4P, is a cause of dysfunction of the Cvi HMA5 allele
additional information
complementation assays of the ccc2 mutant of yeast using chimeric HMA5 proteins, a dysfunctional HMA5 allele is identified in Chisdra-2, which shows Cu sensitivity and low capacity of Cu translocation from roots to shoots, a unique amino acid substitution of Chisdra-2 occurs in another strictly conserved domain, CPC(x)6P, where the latter proline is replaced with leucine. The homozygous HMA5-KO line SALK_040252, carrying a T-DNA insertion at the first intron, shows hypersensitivity to Cu while showing similar growth to the wild type Col-0 in control solution
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genetic architecture of Cu tolerance, overview
expressed in Lactococcus lactis
expressed in Saccharomyces cerevisiae copper-transporting ATPase Ccc2-deficient cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform PAA2 protein abundance decreases significantly and specifically when Cu in the media is increased. Copper addition does not affect PAA2 transcript levels, but stability of the PAA2 protein is decreased in plants grown with elevated copper levels
PAA2 protein abundance is significantly increased in paa1 mutants, in which the copper content in the chloroplast is half of that of the wild-type, due to impaired copper import into the organelle. In a pc2 insertion mutant, which has strongly reduced plastocyanin expression, the PAA2 protein levels are low regardless of copper addition to the growth media
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shikanai, T.; Mueller-Moule, P.; Munekage, Y.; Niyogi, K.K.; Pilon, M.
PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in chloroplasts
Plant Cell
15
1333-1346
2003
Arabidopsis thaliana
Manually annotated by BRENDA team
Abdel-Ghany, S.E.; Mller-Moule, P.; Niyogi, K.K.; Pilon, M.; Shikanai, T.
Two P-type ATPases are required for copper delivery in Arabidopsis thaliana chloroplaszs
Plant Cell
17
1233-1251
2005
Arabidopsis thaliana (B9DFX7), Arabidopsis thaliana (Q9SZC9), Arabidopsis thaliana
Manually annotated by BRENDA team
Kobayashi, Y.; Kuroda, K.; Kimura, K.; Southron-Francis, J.L.; Furuzawa, A.; Kimura, K.; Iuchi, S.; Kobayashi, M.; Taylor, G.J.; Koyama, H.
Amino acid polymorphisms in strictly conserved domains of a P-type ATPase HMA5 are involved in the mechanism of copper tolerance variation in Arabidopsis
Plant Physiol.
148
969-980
2008
Arabidopsis thaliana (Q9SH30)
Manually annotated by BRENDA team
Binder, B.M.; Rodriguez, F.I.; Bleecker, A.B.
The copper transporter RAN1 is essential for biogenesis of ethylene receptors in Arabidopsis
J. Biol. Chem.
285
37263-37270
2010
Arabidopsis thaliana
Manually annotated by BRENDA team
Catty, P.; Boutigny, S.; Miras, R.; Joyard, J.; Rolland, N.; Seigneurin-Berny, D.
Biochemical characterization of AtHMA6/PAA1, a chloroplast envelope Cu(I)-ATPase
J. Biol. Chem.
286
36188-36197
2011
Arabidopsis thaliana (Q9SZC9), Arabidopsis thaliana
Manually annotated by BRENDA team
Tapken, W.; Ravet, K.; Pilon, M.
Plastocyanin controls the stabilization of the thylakoid Cu-transporting P-type ATPase PAA2/HMA8 in response to low copper in Arabidopsis
J. Biol. Chem.
287
18544-18550
2012
Arabidopsis thaliana (B9DFX7), Arabidopsis thaliana
Manually annotated by BRENDA team