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CATH Superfamily 3.30.870.10

Endonuclease Chain A

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:

"
Endonuclease Chain A
".

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 12808: Phospholipase D, isoform G

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
Phospholipase D. [EC: 3.1.4.4]
A phosphatidylcholine + H(2)O = choline + a phosphatidate.
  • Also acts on other phosphatidyl esters.
 51 A0A0B2QFH9 A0A0B2QY87 A0A0F4Z5F1 A0A0F8DB25 A0A0J9R7R1 A0A0N8P0J4 A0A0Q9W3Q0 A0A0Q9XAC2 A2QY19 A2R689
(41 more...)
2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
  • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
  • Alk-2-enals of shorter chain have lower affinities.
  • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
  • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
  • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
 3 B9RFF1 B9RTA5 E0W3X3
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.
 1 G0R1A9
Peptidylprolyl isomerase. [EC: 5.2.1.8]
Peptidylproline (omega=180) = peptidylproline (omega=0).
  • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
  • Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
  • The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
 1 G0QMG5
Picornain 2A. [EC: 3.4.22.29]
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
  • From entero- and rhinoviruses.
  • Smaller than the homologous virus picornain 3C.
  • Belongs to peptidase family C3.
 1 G0R1A9
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