The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Bovine Mitochondrial F1-atpase; Atp Synthase Beta Chain; Chain D, domain 3
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 2782: V-type ATPase subunit A

There are 5 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
H(+)-transporting two-sector ATPase. [EC: 3.6.3.14]
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
  • A multisubunit non-phosphorylated ATPase that is involved in the transport of ions.
  • Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)).
  • The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases.
  • All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits.
  • Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis.
  • This movement is driven by the H(+) electrochemical potential gradient.
  • The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP.
  • Formerly EC 3.6.1.34.
114 A0A023BDF6 A0A075B3T7 A0A088RRI4 A0A0B0E438 A0A0B2S1U3 A0A0B2S5B3 A0A0B7F5X5 A0A0D2VGB5 A0A0F8BNR3 A0A0J5SNI5
(104 more...)
Adenosinetriphosphatase. [EC: 3.6.1.3]
ATP + H(2)O = ADP + phosphate.
  • Many enzymes previously listed under this number are now listed separately as EC 3.6.1.32 to EC 3.6.1.39.
  • The remaining enzymes, not separately listed on the basis of some function coupled with hydrolyzes of ATP, include enzymes dependent on Ca(2+), Mg(2+), anions, H(+) or DNA.
  • Formerly EC 3.6.1.4.
5 A7L4W1 G8HI69 G8HI88 Q93XK8 Q946X7
Proton-exporting ATPase. [EC: 3.6.3.6]
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
  • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
  • Generates an electrochemical potential gradient of protons across the plasma membrane.
  • Formerly EC 3.6.1.35.
3 A5AAF1 B6HJ23 G3Y1B9
Sodium-transporting two-sector ATPase. [EC: 3.6.3.15]
ATP + H(2)O + Na(+)(In) = ADP + phosphate + Na(+)(Out).
  • A multisubunit non-phosphorylated ATPase that is involved in the transport of ions.
  • An enzyme found in alkaliphilic bacteria that is similar to EC 3.6.3.14.
3 B0ERI5 B9RHV0 E0VLH6
Transferred entry: 3.6.3.14. [EC: 3.6.1.34]
    2 Q9AVU8 Q9SM51
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