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 627923: ATP-dependent zinc metalloprotease FtsH

There are 22 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
Microtubule-severing ATPase. [EC: 3.6.4.3]
ATP + H(2)O = ADP + phosphate.
  • Another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
348 A0A074SNK4 A0A074SNM2 A0A074SNS3 A0A074SWI8 A0A074T3K5 A0A074T6A8 A0A074T7C3 A0A074TDD2 A0A074TVA0 A0A074TZ98
(338 more...)
Vesicle-fusing ATPase. [EC: 3.6.4.6]
ATP + H(2)O = ADP + phosphate.
  • A large family of ATP-hydrolyzing enzymes involved in the heterotypic fusion of membrane vesicles with target membranes and the homotypic fusion of various membrane compartments.
  • They belong to the AAA-type (ATPase associated with a variety of cell activities) ATPase superfamily.
  • They include peroxin, which apparently is involved in Zellweger's syndrome.
273 A0A060HGR4 A0A060HGR4 A0A060HI06 A0A060HP91 A0A060HPG6 A0A060HSK4 A0A060HU21 A0A060RQG5 A0A073CLB1 A0A073CLB1
(263 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.
211 A0A024R9G7 A0A060TEZ5 A0A061I0L1 A0A061I1C5 A0A074SNM2 A0A074T9E4 A0A074TDD2 A0A074TG53 A0A086J7E1 A0A086J7E1
(201 more...)
Proteasome ATPase. [EC: 3.6.4.8]
ATP + H(2)O = ADP + phosphate.
  • Belongs to the AAA-type superfamily and, like EC 3.6.4.5, is involved in channel gating and polypeptide unfolding before proteolysis in the proteasome.
  • Six ATPase subunits are present in the regulatory particle (RP) of 26S proteasome.
108 A0A024UYQ0 A0A024V2T0 A0A024V3D6 A0A024V4D2 A0A024VIT4 A0A024VMB1 A0A024VPK2 A0A024VYV2 A0A024W2K4 A0A024W2V3
(98 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).
65 A0A022SVU2 A0A098MYW0 A0A0C5X8M3 A0A0E2B9Q3 A0A0E2BBV3 A0A0E2CHV4 A0A0E2CP65 A0A0E2CZY3 A0A0E2E0V1 A0A0E2ICG5
(55 more...)
Proteasome endopeptidase complex. [EC: 3.4.25.1]
Cleavage of peptide bonds with very broad specificity.
  • A 20-S protein composed of 28 subunits arranged in four rings of seven.
  • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
  • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
  • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
  • Terminal apertures restrict access of substrates to the active sites.
  • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
  • Belongs to peptidase family T1.
  • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
27 A0A0F4YKC1 A0A0F4YY92 A0A0J5SYY7 A0A100INK1 A0A100IRG2 A0A146F6S4 A0A146FEC2 A0A1L9N9E0 A0A1L9NMQ3 A0A1L9UVK0
(17 more...)
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.
26 A0A060SYS4 A0A060TA07 A0A060TBW7 A0A060THA2 A0A0L1HEP1 A0A0L1HFS8 A0A0L1HJA9 A0A0L1HMB5 A0A0L1HR80 A0A0L1HR80
(16 more...)
Endopeptidase La. [EC: 3.4.21.53]
Hydrolysis of proteins in presence of ATP.
  • ATP hydrolysis is linked with peptide bond hydrolysis.
  • Vanadate inhibits both reactions.
  • A similar enzyme occurs in animal mitochondria.
  • Belongs to peptidase family S16.
4 B0E9H9 B0EE56 G0R0Q9 L1LBM1
Succinate dehydrogenase (quinone). [EC: 1.3.5.1]
Succinate + a quinone = fumarate + a quinol.
  • The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria.
  • It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II).
  • In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone.
  • Cf. EC 1.3.5.4.
4 A0A0E9NPU4 A0A0G2EH26 A0A178F329 A0A179U5S9
Diphosphate--fructose-6-phosphate 1-phosphotransferase. [EC: 2.7.1.90]
Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6- bisphosphate.
    1 A0A087STU7
    Acylphosphatase. [EC: 3.6.1.7]
    An acylphosphate + H(2)O = a carboxylate + phosphate.
      1 M4CNE5
      Protein-L-isoaspartate(D-aspartate) O-methyltransferase. [EC: 2.1.1.77]
      S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L- homocysteine + protein L-isoaspartate alpha-methyl ester.
      • D-aspartate (but not L-aspartate) residues in proteins can also act as acceptors.
      • Formerly EC 2.1.1.24.
      1 F9EDT5
      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 A0A1J1HXU4
      Stromelysin 1. [EC: 3.4.24.17]
      Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
      • Extracellular endopeptidase of vertebrate tissues.
      • Degradation of proteoglycans, fibronectin, collagen type III, IV, V and IX and activates procollagenase.
      • Belongs to peptidase family M10B.
      1 K9MN65
      Histone-lysine N-methyltransferase. [EC: 2.1.1.43]
      S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
        1 A0A1I7V8T8
        Lysine--tRNA ligase. [EC: 6.1.1.6]
        ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys).
          1 D9PGU0
          Receptor protein-tyrosine kinase. [EC: 2.7.10.1]
          ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
          • The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans.
          • In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies.
          • Formerly EC 2.7.1.112.
          1 A0A1B0GCP7
          Aminoacyl-tRNA hydrolase. [EC: 3.1.1.29]
          N-substituted aminoacyl-tRNA + H(2)O = N-substituted amino acid + tRNA.
            1 A5M914
            Cobaltochelatase. [EC: 6.6.1.2]
            ATP + hydrogenobyrinic acid a,c-diamide + Co(2+) + H(2)O = ADP + phosphate + cob(II)yrinic acid a,c-diamide + H(2).
            • This enzyme, which forms part of the aerobic cobalamin biosynthesis pathway, is a type I chelatase, being heterotrimeric and ATP- dependent.
            • It comprises two components, one of which corresponds to CobN and the other is composed of two polypeptides, specified by cobS and cobT in Pseudomonas denitrificans, and named CobST.
            • Hydrogenobyrinic acid is a very poor substrate.
            • ATP can be replaced by dATP or CTP but the reaction proceeds more slowly.
            • CobN exhibits a high affinity for hydrogenobyrinic acid a,c-diamide.
            • The oligomeric protein CobST possesses at least one sulfhydryl group that is essential for ATP-binding.
            • Once the Co(2+) is inserted, the next step in the pathway ensures that the cobalt is ligated securely by reducing Co(II) to Co(I); this step is carried out by EC 1.16.8.1.
            1 G0QW86
            Diacylglycerol kinase (ATP). [EC: 2.7.1.107]
            ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.
            • Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol.
            • Activity is stimulated by certain phospholipids.
            • In plants and animals the product 1,2-diacyl-sn-glycerol 3-phosphate is an important second messenger.
            • cf. EC 2.7.1.174.
            1 A0A0V1MLL1
            Type 1 galactoside alpha-(1,2)-fucosyltransferase. [EC: 2.4.1.69]
            GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D- glucosaminyl-R = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N- acetyl-beta-D-glucosaminyl-R.
            • The enzyme acts on a glycoconjugates where the substituent group is a glycoprotein or glycosphingolipid.
            • The recognized moiety of the substrate is known as a type 1 histo- blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen.
            • The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates (see EC 2.4.1.344).
            • Formerly EC 2.4.1.89.
            1 G0QW86
            Protein kinase C. [EC: 2.7.11.13]
            ATP + a protein = ADP + a phosphoprotein.
            • A family of serine- and threonine-specific protein kinases that depend on lipids for activity.
            • They can be activated by calcium but have a requirement for the second messenger diacylglycerol.
            • Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell- signaling pathways.
            • Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumor promoters.
            • Formerly EC 2.7.1.37.
            1 G0QXY3