D
IPR044492

P-type ATPase, haloacid dehalogenase domain

InterPro entry
Short nameP_typ_ATPase_HD_dom
Overlapping
homologous
superfamilies
 
HAD superfamily (IPR023214)

Description

This entry represents the haloacid dehalogenase domain (the catalytic domain) of P-type ATPases
[2]
.

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.

P-ATPases (also known as E1-E2 ATPases) (
3.6.3.-
) are found in bacteria and in a number of eukaryotic plasma membranes and organelles
[1]
. P-ATPases function to transport a variety of different compounds, including ions and phospholipids, across a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases, which transport specific types of ion: H+, Na+, K+, Mg2+, Ca2+, Ag+and Ag2+, Zn2+, Co2+, Pb2+, Ni2+, Cd2+, Cu+and Cu2+. P-ATPases can be composed of one or two polypeptides, and can usually assume two main conformations called E1 and E2.

References

1.Evolution of substrate specificities in the P-type ATPase superfamily. Axelsen KB, Palmgren MG. J. Mol. Evol. 46, 84-101, (1998). View articlePMID: 9419228

2.The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Aravind L, Galperin MY, Koonin EV. Trends Biochem. Sci. 23, 127-9, (1998). View articlePMID: 9584613

Further reading

3. The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio. Cross RL, Muller V. FEBS Lett. 576, 1-4, (2004). View articlePMID: 15473999

4. Mechanisms of ATPases--a multi-disciplinary approach. Rappas M, Niwa H, Zhang X. Curr. Protein Pept. Sci. 5, 89-105, (2004). View articlePMID: 15078220

5. Regulation and isoform function of the V-ATPases. Toei M, Saum R, Forgac M. Biochemistry 49, 4715-23, (2010). View articlePMID: 20450191

6. New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). Gruber G, Marshansky V. Bioessays 30, 1096-109, (2008). View articlePMID: 18937357

7. F-type or V-type? The chimeric nature of the archaebacterial ATP synthase. Schafer G, Meyering-Vos M. Biochim. Biophys. Acta 1101, 232-5, (1992). PMID: 1385979

8. F-and V-ATPases in the genus Thermus and related species. Radax C, Sigurdsson O, Hreggvidsson GO, Aichinger N, Gruber C, Kristjansson JK, Stan-Lotter H. Syst. Appl. Microbiol. 21, 12-22, (1998). PMID: 9741106

Cross References

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