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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 630881: Small nuclear ribonucleoprotein helicase

There are 10 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).
 39 A0A060RP58 A0A077X9G1 A0A077XBQ5 A0A077Y5G3 A0A078K8D8 A0A0B2R3L5 A0A0F8CQ24 A0A0Y9V129 A0A1C3KPH6 A0A1C6WV57
(29 more...)
DNA helicase. [EC: 3.6.4.12]
ATP + H(2)O = ADP + phosphate.
  • DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA.
  • Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15).
  • Some helicases unwind DNA as well as RNA (4,9).
  • May be identical with EC 3.6.4.13 (RNA helicase).
 8 A0A061ICT3 A0A1N6LWJ3 E1BNG3 E7F8F4 E9PZJ8 F1LPQ2 F1NTD6 Q8N3C0
3-oxoacyl-[acyl-carrier-protein] reductase. [EC: 1.1.1.100]
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl- carrier-protein] + NADPH.
  • Exhibits a marked preference for [acyl-carrier-protein] derivatives over CoA derivatives as substrates.
 1 B0EGZ1
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 A0A060TE03
Arylesterase. [EC: 3.1.1.2]
A phenyl acetate + H(2)O = a phenol + acetate.
  • Acts on many phenolic esters.
  • It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases.
  • The natural substrates of the paraoxonases are lactones, with (+-)-5- hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate.
 1 B0EGZ1
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 A0A1L0B6U4
Beta-ketoacyl-[acyl-carrier-protein] synthase I. [EC: 2.3.1.41]
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) + [acyl-carrier-protein].
  • Responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain.
  • Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids.
  • Can use fatty acyl thioesters of ACP (C(2) to C(16)) as substrates, as well as fatty acyl thioesters of Co-A (C(4) to C(16)).
  • The substrate specificity is very similar to that of EC 2.3.1.179 with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C(16)-Delta(9)) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature.
 1 A0A023B4W0
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 B0EE60
Type I site-specific deoxyribonuclease. [EC: 3.1.21.3]
Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolyzed.
  • Large group of enzymes that have an absolute requirement for ATP (or dATP) and S-adenosyl-L-methionine.
  • They recognize specific short DNA sequences and cleave at sites remote from the recognition sequence.
  • Multifunctional proteins which also catalyze the reactions of EC 2.1.1.72 and EC 2.1.1.73, with similar site specificity.
  • Formerly EC 3.1.24.1 and EC 3.1.24.2.
  • See the REBASE database for a complete list of these enzymes: http://rebase.neb.com/rebase/
 1 B0EGZ1
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 A3LNR5