IntEnz

EC 3.6.3.4 - Cu²⁺-exporting ATPase

IntEnz Enzyme Nomenclature
EC 3.6.3.4

Names

Reaction

• 10376 [IUBMB]
  ATP

  ATP

  Name origin: UniProt - CHECKED (C)

  CHEBI:30616

  Formula: C10H12N5O13P3
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  Cu²⁺

  Cu(2+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:29036

  Formula: Cu
  Charge: 2

  ChEBI compound status: CHECKED (C)

  

  IN

  +

  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  ADP

  ADP

  Name origin: UniProt - CHECKED (C)

  CHEBI:456216

  Formula: C10H12N5O10P2
  Charge: -3

  ChEBI compound status: CHECKED (C)

  

  +

  Cu²⁺

  Cu(2+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:29036

  Formula: Cu
  Charge: 2

  ChEBI compound status: CHECKED (C)

  

  OUT

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  phosphate

  phosphate

  Name origin: UniProt - CHECKED (C)

  CHEBI:43474

  Formula: HO4P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Cofactor

• Mg²⁺

Comments:

A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic bacterium Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].

Links to other databases

References

1. Mana-Capelli, S., Mandal, A. K., Arguello, J. M.
   Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain.
   J. Biol. Chem. 278: 40534-40541 (2003). [PMID: 12876283]
2. Jayakanthan, S., Roberts, S. A., Weichsel, A., Arguello, J. M., McEvoy, M. M.
   Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle.
   Biosci. Rep. 32: 443-453 (2012). [PMID: 22663904]

[EC 3.6.3.4 created 2000, modified 2013]