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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_3_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.

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 13 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 peroxidase. [EC: 1.11.1.5]
2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O.
    		 56 A0A024LA66 A0A024LA66 A0A069XK30 A0A069XK30 A0A070SM29 A0A070SM29 A0A072ZBZ0 A0A072ZBZ0 A0A0E0U4T9 A0A0E0U4T9
    (46 more...)
    Quinol--cytochrome-c reductase. [EC: 7.1.1.8]
    Quinol + 2 ferricytochrome c(Side 2) = quinone + 2 ferrocytochrome c(Side 2) + 2 H(+)(Side 2).
    • 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).
    • Formerly EC 1.10.2.2.
    		 34 A0A045HBG9 A0A045HBG9 A0A0H3M7Y6 A0A0H3M7Y6 A0A0H3MQ23 A0A0H3MQ23 A0A0Y1CWM8 A0A0Y1CWM8 A0A120IXB0 A0A120IXB0
    (24 more...)
    L-cysteine S-thiosulfotransferase. [EC: 2.8.5.2]
    (1) [SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H(+). (2) [SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H(+).
    • The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate.
    • It catalyzes two reactions in the pathway - early in the pathway it attaches a thiosulfate molecule to the sulfur atom of an L-cysteine of a SoxY protein; later it transfers a second thiosulfate molecule to a sulfane group that is already attached to the same cysteine residue.
    		 25 A0A1I5IP77 A0A1I5IP77 A0A2Z6DX80 A0A2Z6DX80 D3DJG4 D3DJG4 D3DJG5 D3RVS7 D3RVS7 D7A6E5
    (15 more...)
    Alcohol dehydrogenase (quinone). [EC: 1.1.5.5]
    Ethanol + ubiquinone = acetaldehyde + ubiquinol.
    • Only described in acetic acid bacteria where it is involved in acetic acid production.
    • Associated with membrane.
    • Electron acceptor is membrane ubiquinone.
    • A model structure suggests that, like all other quinoprotein alcohol dehydrogenases, the catalytic subunit has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ; the catalytic subunit also has a heme c in the C-terminal domain.
    • The enzyme has two additional subunits, one of which contains three molecules of heme c.
    • It does not require amines for activation.
    • It has a restricted substrate specificity, oxidizing a few primary alcohols (C2 to C6), but not methanol, secondary alcohols and some aldehydes.
    • It is assayed with phenazine methosulfate or with ferricyanide.
    		 15 A0A0D6PVY0 A0A0D6PVY0 A0A0D6PVY0 O05542 P0A388 P0A388 P0A388 P0A389 P0A389 P0A389
    (5 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.
    		 11 A0A0C7D2E8 A0A1F0IXV3 A0A1I5E511 A0A2V2TTC4 A0A335EPU8 A0A448BX27 P24040 P24474 P72181 Q51700
    (1 more...)
    Hydroxylamine reductase. [EC: 1.7.99.1]
    NH(3) + H(2)O + acceptor = hydroxylamine + reduced acceptor.
    • Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine.
    • May be identical to EC 1.7.2.1.
    		 11 A0A0C7D2E8 A0A1F0IXV3 A0A1I5E511 A0A2V2TTC4 A0A335EPU8 A0A448BX27 P24040 P24474 P72181 Q51700
    (1 more...)
    Thiosulfate dehydrogenase. [EC: 1.8.2.2]
    2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome c.
    • The enzyme catalyzes the reversible formation of a sulfur-sulfur bond between the sulfane atoms of two thiosulfate molecules, yielding tetrathionate and releasing two electrons.
    • In many bacterial species the enzyme is a diheme c-type cytochrome.
    • In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus, a second diheme cytochrome (TsdB) acts as the electron acceptor.
    • However, some organisms, such as Allochromatium vinosum, lack TsdB.
    • The electron acceptor in these organisms may be the high-potential iron-sulfur protein (HiPIP).
    		 10 A0A3B9TC57 A0A3B9TC57 A4VND8 A4VND8 D3RVD4 D3RVD4 D5WYQ5 D5WYQ5 Q4FQB7 Q4FQB7
    Alcohol dehydrogenase (azurin). [EC: 1.1.9.1]
    A primary alcohol + azurin = an aldehyde + reduced azurin.
    • Occurs in Comamonas and Pseudomonas.
    • Does not require an amine activator.
    • Oxidizes a wide range of primary and secondary alcohols, and also aldehydes and large substrates such as sterols; methanol is not a substrate.
    • Usually assayed with phenazine methosulfate or ferricyanide.
    • Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
    • Formerly EC 1.1.98.1.
    		 5 A0A1Y3KLH3 A0A2S6W5X4 Q46444 Q4W6G0 Q8GR64
    Nicotinate dehydrogenase (cytochrome). [EC: 1.17.2.1]
    Nicotinate + a ferricytochrome + H(2)O = 6-hydroxynicotinate + a ferrocytochrome + 2 H(+).
    • This two-component enzyme from Pseudomonas belongs to the family of xanthine dehydrogenases, but differs from most other members of this family.
    • While most members contain an FAD cofactor, the large subunit of this enzyme contains three c-type cytochromes, enabling it to interact with the electron transfer chain, probably by delivering the electrons to a cytochrome oxidase.
    		 4 A0A2V4F1A6 A0A2V4F1A6 Q88FX8 Q88FX8
    Gluconate 2-dehydrogenase (acceptor). [EC: 1.1.99.3]
    D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
      		 3 O34215 O34215 O34215
      Hydrazine synthase. [EC: 1.7.2.7]
      Hydrazine + H(2)O + 3 ferricytochrome c = nitric oxide + ammonium + 3 ferrocytochrome c.
      • The enzyme, characterized from anaerobic ammonia oxidizers (anammox bacteria), is one of only two enzymes that are known to form an N-N bond (the other being EC 1.7.1.14).
      • The enzyme from the bacterium Candidatus Kuenenia stuttgartiensis is heterotrimeric and contains multiple c-type cytochromes.
      		 2 Q1Q0T3 Q1Q0T3
      Lupanine 17-hydroxylase (cytochrome c). [EC: 1.17.2.2]
      Lupanine + 2 ferricytochrome c + H(2)O = 17-hydroxylupanine + 2 ferrocytochrome c + 2 H(+).
        		 1 Q934G0
        1-butanol dehydrogenase (cytochrome c). [EC: 1.1.2.9]
        Butan-1-ol + 2 ferricytochrome c = butanal + 2 ferrocytochrome c + 2 H(+).
        • This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation.
        • It contains both pyrroloquinoline quinone (PQQ) and heme c prosthetic groups.
        • Cf. EC 1.1.5.11.
        		 1 Q9AF95