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CATH Superfamily 1.20.210.10

Cytochrome c oxidase-like, subunit I domain

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:

"
Cytochrome c oxidase-like, subunit I domain
".

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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 3 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
Cytochrome-c oxidase. [EC: 1.9.3.1]
4 ferrocytochrome c + O(2) + 4 H(+) = 4 ferricytochrome c + 2 H(2)O.
  • The reduction of O(2) to water is accompanied by the extrusion of four protons from the intramitochondrial compartment.
  • Several bacteria appear to contain analogous oxidases.
 467 A0A023J6G7 A0A023VVZ3 A0A045IAT1 A0A049DHA5 A0A068BBI0 A0A075E6K7 A0A088BEW7 A0A0A0VG02 A0A0A1G1J6 A0A0A7ALM5
(457 more...)
Ubiquinol oxidase (H(+)-transporting). [EC: 7.1.1.3]
2 ubiquinol + O(2) + n H(+)(Side 1) = 2 ubiquinone + 2 H(2)O + n H(+)(Side 2).
  • This terminal oxidase enzyme generates proton motive force by two mechanisms: (1) transmembrane charge separation resulting from utilizing protons and electrons originating from opposite sides of the membrane to generate water, and (2) active pumping of protons across the membrane.
  • The bioenergetic efficiency (the number of charges driven across the membrane per electron used to reduce oxygen to water) depends on the enzyme; for example, for the bo(3) oxidase it is 2, while for the bd-II oxidase it is 1.
  • Cf. EC 7.1.1.7.
  • Formerly EC 1.10.3.10.
 167 A0A023YT60 A0A025CAN2 A0A026UGU4 A0A028AID9 A0A028DMF9 A0A029IC72 A0A029J0X3 A0A059URU4 A0A069XN08 A0A070F9R0
(157 more...)
Nitric-oxide reductase (cytochrome c). [EC: 1.7.2.5]
Nitrous oxide + 2 ferricytochrome c + H(2)O = 2 nitric oxide + 2 ferrocytochrome c + 2 H(+).
  • The enzyme from Pseudomonas aeruginosa contains a dinuclear center comprising a non-heme iron center and heme b3, plus heme c, heme b and calcium; the acceptor is cytochrome c551.
  • Formerly EC 1.7.99.7.
 5 A0A0T6V6P5 A0A2N8RD21 A0A454M1Q7 P98008 Q59647