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CATH Superfamily 1.20.1690.10

V-type ATP synthase subunit C domain

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:

"
V-type ATP synthase subunit C domain
".

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 949: V-type ATPase, subunit C

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.
 264 A0A011QWP5 A0A017H4K6 A0A024VFQ4 A0A024W0I1 A0A024WZF4 A0A037Z7S9 A0A037Z7S9 A0A060HTY0 A0A060HTY0 A0A060S060
(254 more...)
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.
 10 A0A100I8S3 A0A146FBX4 A0A162CNX5 A0A1L9N804 A0A1M3TR14 A2QE37 B6H2L2 E3TEA9 G3Y0V9 G7XBI0
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.
 9 A0A090I164 C7HVT0 D5RFM9 G4L4R6 G4L4R6 K0IYD8 Q6L1S5 Q6L1S5 Q8RI75
Transferred entry: 3.6.3.14. [EC: 3.6.1.34]
    		2 Q8GUB0 Q8GUB0
    Branched-chain-amino-acid transaminase. [EC: 2.6.1.42]
    (1) L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. (2) L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate. (3) L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.
    • Also acts on L-isoleucine and L-valine.
    • Different from EC 2.6.1.66.
    		 1 A0A195FWC1