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:

"
EF-hand
".

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 1412: Calmodulin 1 (Phosphorylase kinase, delta)

There are 4 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
NAD(P)H oxidase (H(2)O(2)-forming). [EC: 1.6.3.1]
NAD(P)H + O(2) = NAD(P)(+) + H(2)O(2).
  • When calcium is present, this transmembrane glycoprotein generates H(2)O(2) by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen.
  • The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups.
  • This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H(2)O(2) for the thyroid peroxidase-catalyzed biosynthesis of thyroid hormones.
12 A0A074T165 A0A086KQZ8 A0A086KUM3 A0A086LBG6 A0A086M6K9 A0A086QIE4 A0A086QU40 A0A125YHX6 A0A125YHX7 A0A139YA49
(2 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).
8 A0A0B2PBM0 A0A0B2Q8R4 A0A0B2RHK2 A0A0B2S914 C6T231 E0VSY4 I1LBL2 I1NC91
Ribonucleoside-diphosphate reductase. [EC: 1.17.4.1]
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.
  • This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair.
  • There are three types of this enzyme differing in their cofactors.
  • Class Ia enzymes contain a diferric-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin.
  • In all cases the cofactors are involved in generation of a transient thiyl radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl radical.
  • The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues.
  • A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position.
  • The disulfide bridge is reduced by the action of thioredoxin.
  • Cf. EC 1.1.98.6 and EC 1.17.4.2.
2 A0A099P9E1 A0A1B7SMA0
Calcium/calmodulin-dependent protein kinase. [EC: 2.7.11.17]
ATP + a protein = ADP + a phosphoprotein.
  • Requires calmodulin.
  • A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light-chains and the microtubule- associated tau protein.
  • Not identical with EC EC 2.7.11.18 or EC 2.7.11.26.
  • Formerly EC 2.7.1.120 and EC 2.7.1.123.
1 A0A0U3HLA8