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CATH Superfamily 3.30.70.100

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 48: Antibiotic biosynthesis monooxygenase

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
Heme oxygenase (mycobilin-producing). [EC: 1.14.99.57]
(1) Protoheme + 3 reduced acceptor + 3 O(2) = mycobilin a + Fe(2+) + 3 acceptor + 3 H(2)O. (2) Protoheme + 3 reduced acceptor + 3 O(2) = mycobilin b + Fe(2+) + 3 acceptor + 3 H(2)O.
  • The enzyme, characterized from the bacterium Mycobacterium tuberculosis, is involved in heme degradation and iron utilization.
  • The enzyme binds two stacked protoheme molecules per monomer.
  • Unlike the canonical heme oxygenases, the enzyme does not release carbon monoxide or formaldehyde; instead, it forms unique products, named mycobilins, that retain the alpha-meso-carbon at the ring cleavage site as an aldehyde group.
  • EC 1.6.2.4.
 110 A0A045KE53 A0A045KE53 A0A045KE53 A0A045KE53 A0A045KE53 A0A045KE53 A0A045KE53 A0A045KE53 A0A045KE53 A0A045KE53
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