View in Gene3D

CATH Superfamily 3.30.420.40

ATPase, nucleotide binding domain

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: waiting to be named.

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.
« Back to all FunFams

FunFam 63863: Heat shock protein 70

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
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.
 62 A0A074T3M7 A0A074T3M7 A0A074TXD1 A0A074TXD1 A0A086J942 A0A086J942 A0A086KIT4 A0A086KIT4 A0A086KXI2 A0A086KXI2
(52 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).
 58 A0A0B2NWM9 A0A0B2NWM9 A0A0B2NX74 A0A0B2NX74 A0A0B2Q5A6 A0A0B2Q5A6 A0A0B2Q9R1 A0A0B2Q9R1 A0A0F4YKA3 A0A0F4YKA3
(48 more...)
Non-chaperonin molecular chaperone ATPase. [EC: 3.6.4.10]
ATP + H(2)O = ADP + phosphate.
  • This is a highly diverse group of enzymes that perform many functions that are similar to those of chaperonins.
  • They comprise a number of heat-shock-cognate proteins.
  • They are also active in clathrin uncoating and in the oligomerization of actin.
 46 A0A0K1W3I4 A0A0K1W3I4 A0A0L8VS46 A0A0L8VS46 A6ZXA5 A6ZXA5 B3LHA5 B3LHA5 C8Z6P0 C8Z6P0
(36 more...)
Porphobilinogen synthase. [EC: 4.2.1.24]
2 5-aminolevulinate = porphobilinogen + 2 H(2)O.
  • The enzyme catalyzes the asymmetric condensation and cyclization of two 5-aminolevulinate molecules, which is the first common step in the biosynthesis of tetrapyrrole pigments such as porphyrin, chlorophyll, vitamin B12, siroheme, phycobilin, and cofactor F430.
  • The enzyme is widespread, being essential in organisms that carry out respiration, photosynthesis, or methanogenesis.
  • In humans, the enzyme is a primary target for the environmental toxin Pb.
  • The enzymes from some organisms utilize a dynamic equilibrium between architecturally distinct multimeric assemblies as a means for allosteric regulation.
 6 A0A158P200 A0A158P200 A0A161MIJ3 A0A161MIJ3 G6CYQ3 G6CYQ3
DNA ligase (ATP). [EC: 6.5.1.1]
ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.
  • The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA.
  • Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue.
  • The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA).
  • Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
  • RNA can also act as substrate, to some extent.
  • Cf. EC 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7.
 2 A0A1J8QGX6 A0A1J8QGX6