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:

"
P-loop containing nucleotide triphosphate hydrolases
".

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 630802: Dynein heavy chain, axonemal

There are 6 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
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.
115 A0A0B4K614 A0A0B4K648 A0A0B4KHJ4 A0A0B4KI48 A0A0B4LH20 A0A0D2LN34 A0A0D2NT62 A0A0J9R382 A0A0J9RP14 A0A0J9RP19
(105 more...)
Minus-end-directed kinesin ATPase. [EC: 3.6.4.5]
ATP + H(2)O = ADP + phosphate.
  • Structurally almost identical to EC 3.6.4.3 but the movement it catalyzes is toward the minus end of microtubules.
10 A8Y5B7 M9PBQ0 M9PBQ3 M9PE73 M9PEC8 M9PEN4 M9PHG8 Q5LJP0 Q7KVA7 Q9VZ77
Glycerol-3-phosphate dehydrogenase. [EC: 1.1.5.3]
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
  • An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis.
  • In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane.
  • In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain.
  • This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix.
  • Insect flight muscle uses only CoQ(10) as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ(9).
  • The enzyme is activated by calcium.
  • Formerly EC 1.1.2.1 and EC 1.1.99.5.
4 A0A0R3NTG7 B3MMG9 B5DJ47 Q9VJC6
Dynein ATPase. [EC: 3.6.4.2]
ATP + H(2)O = ADP + phosphate.
  • A multisubunit protein complex associated with microtubules.
  • Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome toward the microtubule's minus end.
  • It also functions in the movement of eukaryotic flagella and cilia.
  • Formerly EC 3.6.1.33.
4 A0A0B7F7W3 A0A0F4YV18 A2RAF2 B6HJQ7
Acid phosphatase. [EC: 3.1.3.2]
A phosphate monoester + H(2)O = an alcohol + phosphate.
  • Wide specificity.
  • Also catalyzes transphosphorylations.
2 A0A182VZ21 A0A1A9TNA0
Nucleoside-triphosphate phosphatase. [EC: 3.6.1.15]
NTP + H(2)O = NDP + phosphate.
  • The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria.
  • Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD.
  • The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
2 A0A060T9B0 A0A161M7B3
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