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CATH Superfamily 1.20.1260.10

Ferritin, core subunit, four-helix bundle

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_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.
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FunFam 72: Dichlorochromopyrrolate synthase

There are 2 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
Catalase. [EC: 1.11.1.6]
2 H(2)O(2) = O(2) + 2 H(2)O.
  • A manganese protein containing Mn(III) in the resting state, which also belongs here, is often called pseudocatalase.
  • The enzymes from some organisms, such as Penicillium simplicissimum, can also act as a peroxidase (EC 1.11.1.7) for which several organic substances, especially ethanol, can act as a hydrogen donor.
  • Enzymes that exhibit both catalase and peroxidase activity belong under EC 1.11.1.21.
 1 Q8KHV6
Dichlorochromopyrrolate synthase. [EC: 1.21.98.2]
2 3-(7-chloroindol-3-yl)-2-iminopropanoate + H(2)O(2) = dichlorochromopyrrolate + NH(3) + 2 H(2)O.
  • This enzyme catalyzes a step in the biosynthesis of rebeccamycin, an indolocarbazole alkaloid produced by the bacterium Lechevalieria aerocolonigenes.
  • The enzyme is a dimeric heme-protein oxidase that catalyzes the oxidative dimerization of two L-tryptophan-derived molecules to form dichlorochromopyrrolic acid, the precursor for the fused six-ring indolocarbazole scaffold of rebeccamycin.
  • In vivo the enzyme uses hydrogen peroxide, formed by the enzyme upstream in the biosynthetic pathway (EC 1.4.3.23) as the electron acceptor.
  • However, the enzyme is also able to catalyze the reaction using molecular oxygen.
  • Formerly EC 1.21.3.9 and EC 4.3.1.26.
 1 Q8KHV6