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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_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.
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FunFam 2038: Antibiotic biosynthesis monooxygenase family prote...

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
Transferred entry: 1.14.14.18. [EC: 1.14.99.3]
    		36 A0A045KE53 A0A045KE53 A0A083VS97 A0A083VS97 A0A0G4DZ35 A0A0G4DZ35 A0A0H3LF70 A0A0H3LF70 A0A0H3MBJ7 A0A0H3MBJ7
    (26 more...)
    Heme oxygenase (biliverdin-producing). [EC: 1.14.14.18]
    Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O.
    • This mammalian enzyme participates in the degradation of heme.
    • The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules.
    • The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO.
    • The enzyme requires NAD(P)H and EC 1.6.2.4.
    • Cf. EC 1.14.15.20.
    • Formerly EC 1.14.99.3.
    		 32 A0A045KE53 A0A045KE53 A0A083VS97 A0A083VS97 A0A0G4DZ35 A0A0G4DZ35 A0A0H3LF70 A0A0H3LF70 A0A0H3MBJ7 A0A0H3MBJ7
    (22 more...)
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