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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 2146: Heme oxygenase (staphylobilin-producing)

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
Heme oxygenase (staphylobilin-producing). [EC: 1.14.99.48]
(1) Protoheme + 5 reduced acceptor + 4 O(2) = 5-oxo-delta-bilirubin + Fe(2+) + formaldehyde + 5 acceptor + 4 H(2)O. (2) Protoheme + 5 reduced acceptor + 4 O(2) = 15-oxo-beta-bilirubin + Fe(2+) + formaldehyde + 5 acceptor + 4 H(2)O.
  • This enzyme, which is found in some pathogenic bacteria, is involved in an iron acquisition system that catabolizes the host's hemoglobin.
  • The two enzymes from the bacterium Staphylococcus aureus, encoded by the isdG and isdI genes, produce 67.5 % and 56.2 % 5-oxo-delta- bilirubin, respectively.
 76 A0A069AL92 A0A069AL92 A0A077UI71 A0A077UI71 A0A0D1JNV9 A0A0D1JNV9 A0A0E0VMZ5 A0A0E0VMZ5 A0A0E1AFU0 A0A0E1AFU0
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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.
 42 A0A069AL92 A0A069AL92 A0A0E1AFU0 A0A0E1AFU0 A0A0E1VKM8 A0A0E1VKM8 A0A0E1X8V2 A0A0E1X8V2 A0A1E8WQ49 A0A1E8WQ49
(32 more...)
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