EC number:7.2.2.19

Enzyme

Download
EC Tree
     7. Translocases
        7.2 Catalysing the translocation of inorganic cations
            7.2.2 Linked to the hydrolysis of a nucleoside triphosphate
ID:7.2.2.19
Description:H(+)/K(+)-exchanging ATPase.
Alternative Name: Proton pump.
Potassium-transporting ATPase.
H(+)/K(+)-ATPase.
Gastric H(+)/K(+) ATPase.
Prosite: PDOC00139;
PDB:
PDBScop

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 7.2.2.19
BRENDA Enzyme Link: BRENDA 7.2.2.19
KEGG Enzyme Link: KEGG7.2.2.19
BioCyc Enzyme Link: BioCyc 7.2.2.19
ExPASy Enzyme Link: ExPASy7.2.2.19
EC2PDB Enzyme Link: EC2PDB 7.2.2.19
ExplorEnz Enzyme Link: ExplorEnz 7.2.2.19
PRIAM enzyme-specific profiles Link: PRIAM 7.2.2.19
IntEnz Enzyme Link: IntEnz 7.2.2.19
MEDLINE Enzyme Link: MEDLINE 7.2.2.19

EC number:7.2.2.19

MSA:

7.2.2.19;
Phylogenetic Tree:

7.2.2.19;
Uniprot:
M-CSA:
RHEA:22044 ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) + K(+)(in) + 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
Gastric H+-K+-ATPase in situ: evidence for compartmentalization.Hersey SJ, Perez A, Matheravidathu S, Sachs G1989 Oct2552824
The mechanism and structure of the gastric H,K-ATPase.Rabon EC, Reuben MA19902158765