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CATH Superfamily 3.40.50.300

P-loop containing nucleotide triphosphate hydrolases

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 635115: DEAD/DEAH box RNA helicase

There are 11 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
RNA helicase. [EC: 3.6.4.13]
ATP + H(2)O = ADP + phosphate.
  • RNA helicases utilize the energy from ATP hydrolysis to unwind RNA.
  • Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity.
  • Some helicases unwind DNA as well as RNA.
  • May be identical with EC 3.6.4.12 (DNA helicase).
 103 A0A024W9L6 A0A061ICN7 A0A075ATZ5 A0A076JCS2 A0A076JJG9 A0A077TGQ3 A0A077X5G2 A0A078K256 A0A080N5Y9 A0A083WY77
(93 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.
 4 A0A151SZE2 A0A161MNT5 A7AUA6 Q9Y134
Pectate lyase. [EC: 4.2.2.2]
Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
  • Favors pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10).
  • Formerly EC 4.2.99.3.
 1 B0E7S8
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.
 1 A0A161MNT5
Pyruvate dehydrogenase (acetyl-transferring). [EC: 1.2.4.1]
Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
  • It is a component (in multiple copies) of the multienzyme pyruvate dehydrogenase complex in which it is bound to a core of molecules of EC 2.3.1.12, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.12.
 1 A0A084G772
DNA-directed DNA polymerase. [EC: 2.7.7.7]
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
  • Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
  • Cannot initiate a chain de novo.
  • Requires a primer which may be DNA or RNA.
  • See also EC 2.7.7.49.
 1 A3LY83
Type II site-specific deoxyribonuclease. [EC: 3.1.21.4]
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.
  • Large group of enzymes which recognize specific short DNA sequences and cleave either within, or at a short specific distance from, the recognition site.
  • See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
 1 G0QXV5
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring). [EC: 1.2.4.4]
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine- residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO(2).
  • It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2- oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine.
  • It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, which also binds multiple copies of EC 1.8.1.4.
  • It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
  • Formerly EC 1.2.4.3.
 1 A0A084G772
DNA topoisomerase (ATP-hydrolyzing). [EC: 5.99.1.3]
ATP-dependent breakage, passage and rejoining of double-stranded DNA.
  • Can introduce negative superhelical turns into double-stranded circular DNA.
  • One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.99.1.2).
 1 B0EG54
Glycerol-3-phosphate 1-O-acyltransferase. [EC: 2.3.1.15]
Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
  • Acyl-[acyl-carrier-protein] can also act as acyl donor.
  • Acts only with derivatives of fatty acids of chain length above C(10).
 1 B0EG54
Phosphate acetyltransferase. [EC: 2.3.1.8]
Acetyl-CoA + phosphate = CoA + acetyl phosphate.
  • Also acts with other short-chain acyl-CoAs.
 1 B0EG54
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