Enzyme

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EC Tree
     7. Translocases
        7.2 Catalysing the translocation of inorganic cations
            7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
ID:7.2.2.8
Description:P-type Cu(+) transporter.
Alternative Name: Cu(+)-exporting ATPase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 7.2.2.8
BRENDA Enzyme Link: BRENDA 7.2.2.8
KEGG Enzyme Link: KEGG7.2.2.8
BioCyc Enzyme Link: BioCyc 7.2.2.8
ExPASy Enzyme Link: ExPASy7.2.2.8
EC2PDB Enzyme Link: EC2PDB 7.2.2.8
ExplorEnz Enzyme Link: ExplorEnz 7.2.2.8
PRIAM enzyme-specific profiles Link: PRIAM 7.2.2.8
IntEnz Enzyme Link: IntEnz 7.2.2.8
MEDLINE Enzyme Link: MEDLINE 7.2.2.8
MSA:

7.2.2.8;

Phylogenetic Tree:

7.2.2.8;

Uniprot:
M-CSA:
RHEA:25792 ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate
RULE(radius=1) [*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>[*:6]-[OH;+0:5].[*:1]=[P;H0;+0:2](-[*:3])(-[*:4])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA.Mandal AK, Argüello JM2003 Sep 2312974640
Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase.Fan B, Rosen BP2002 Dec 612351646
Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states.Banci L, Bertini I, Ciofi-Baffoni S, D'Onofrio M, Gonnelli L, Marhuenda-Egea FC, Ruiz-Dueñas FJ2002 Mar 2911922674