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CATH Superfamily 1.10.760.10

Cytochrome c-like domain

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 named:

"
Cytochrome c-like 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.
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FunFam 19994: Cytochrome c, class I

There are 8 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
Sulfite dehydrogenase (cytochrome). [EC: 1.8.2.1]
Sulfite + 2 ferricytochrome c + H(2)O = sulfate + 2 ferrocytochrome c + 2 H(+).
  • Associated with cytochrome c-551.
  • Cf. EC 1.8.5.6.
 12 A0A076K5N0 A0A076K5N0 A0A0F9QND2 A0A0F9QND2 A0A0H4L0U3 A0A0H4L0U3 A0A0J5Q602 A0A0J5Q602 A0A109YLH7 A0A109YLH7
(2 more...)
Nitrite reductase (NO-forming). [EC: 1.7.2.1]
Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H(+).
  • The reaction is catalyzed by two types of enzymes, found in the perimplasm of denitrifying bacteria.
  • One type comprises proteins containing multiple copper centers, the other a heme protein, cytochrome cd1.
  • Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin.
  • Cytochrome cd1 also has oxidase and hydroxylamine reductase activities.
  • May also catalyze the reaction of EC 1.7.99.1 since this is a well- known activity of cytochrome cd1.
  • Formerly EC 1.6.6.5, EC 1.7.99.3 and EC 1.9.3.2.
 6 B6JIX6 B6JIX6 D6V7F6 D6V7F6 H0SHH5 H0SHH5
5-aminolevulinate synthase. [EC: 2.3.1.37]
Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2).
    		 2 A6FPZ9 A6FPZ9
    TRNA (guanine(46)-N(7))-methyltransferase. [EC: 2.1.1.33]
    S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.
    • The enzyme specifically methylates guanine(46) at N(7) in tRNA.
    		 2 A0A090KZ72 A0A090KZ72
    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.
    		 2 D5BTY2 D5BTY2
    Quinol--cytochrome-c reductase. [EC: 1.10.2.2]
    Quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H(+).
    • The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain.
    • It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria.
    • The mammalian enzyme contains cytochromes b-562, b-566 and C(1), and a 2-iron ferredoxin.
    • Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non- cytoplasmic compartment (cf. EC 1.6.99.3).
    		 2 D5BRT8 D5BRT8
    3-isopropylmalate dehydratase. [EC: 4.2.1.33]
    (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.
    • Forms part of the leucine-biosynthesis pathway.
    • Brings about the interconversion of the two isomers of isopropylmalate.
    		 2 A8TII4 A8TII4
    Transferred entry: 1.13.11.63. [EC: 1.14.99.36]
      		2 U2WTC3 U2WTC3
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