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CATH Superfamily 3.20.20.70

Aldolase class I

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 named:

"
Aldolase class I
".

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 363: Oxygen-independent coproporphyrinogen III oxidase

There are 1 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
Coproporphyrinogen dehydrogenase. [EC: 1.3.98.3]
Coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO(2) + 2 L-methionine + 2 5'-deoxyadenosine.
  • Differs from EC 1.3.3.3 by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant.
  • Occurs mainly in bacteria, whereas eukaryotes use the oxygen- dependent oxidase.
  • The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl; this radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups.
  • This conversion, -.CH-CH(2)-COO- -> -CH=CH(2) + CO(2) + e(-) replaces the electron initially used.
  • Formerly EC 1.3.99.22.
 6 A0A2T5K0H7 A0A2T5K0H7 P33770 P51008 P95651 P95651