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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 20044: Gluconate dehydrogenase cytochrome c subunit

There are 9 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
Gluconate 2-dehydrogenase (acceptor). [EC: 1.1.99.3]
D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor.
    		 536 A0A024H9U6 A0A024H9U6 A0A031HKW0 A0A031HQK6 A0A060Q8Z1 A0A060QLL2 A0A060V268 A0A060V268 A0A063BGX5 A0A063BH53
    (526 more...)
    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.
    		 18 A0A0D0TBX6 A0A0H2M723 A0A0N7JWC4 A0A0S4IDT3 A0A0X2P2C6 A0A1A0D667 A0A1A0DE11 A0A1A0DE11 A0A1C3HDE7 A0A1E7W2K5
    (8 more...)
    Dehydrogluconate dehydrogenase. [EC: 1.1.99.4]
    2-dehydro-D-gluconate + acceptor = 2,5-didehydro-D-gluconate + reduced acceptor.
      		 7 A0A085GM70 A0A087PX78 A0A094YG46 A0A0H3NXJ5 A0A143GC18 A0A1B7KFJ3 W8FL89
      Transferred entry: 1.2.5.2. [EC: 1.2.99.3]
        		6 A0A0K0T8S5 C7JFA0 E6V0C6 G7ZDJ1 Q2IZI3 S6DAL9
        Isoquinoline 1-oxidoreductase. [EC: 1.3.99.16]
        Isoquinoline + acceptor + H(2)O = isoquinolin-1(2H)-one + reduced acceptor.
        • The enzyme from Pseudomonas diminuta is specific toward N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline.
        • Electron acceptors include 1,2-benzoquinone, cytochrome c, ferricyanide, iodonitrotetrazolium chloride (INT), nitroblue tetrazolium (NBT), Meldola blue and phenazine methosulfate.
        		 5 A0A0E3GXE4 A0A109B8G0 A0A143GH48 B2TF38 V4RIG5
        D-sorbitol dehydrogenase (acceptor). [EC: 1.1.99.21]
        D-sorbitol + acceptor = L-sorbose + reduced acceptor.
          		 2 D8MM43 Q3JFB3
          Xanthine dehydrogenase. [EC: 1.17.1.4]
          (1) Xanthine + NAD(+) + H(2)O = urate + NADH. (2) Hypoxanthine + NAD(+) + H(2)O = xanthine + NADH.
          • Acts on a variety of purines and aldehydes, including hypoxanthine.
          • The mammalian enzyme can also convert all-trans retinol to all-trans- retinoate, while the substrate is bound to a retinoid-binding protein.
          • The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum center.
          • The mammallian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4).
          • During purification the enzyme is largely converted to an O(2)- dependent form, EC 1.17.3.2.
          • The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds (which can be catalyzed by EC 1.8.4.7 in the presence of glutathione disulfide) or limited proteolysis, which results in irreversible conversion.
          • The conversion can also occur in vivo.
          • Formerly EC 1.2.1.37 and EC 1.1.1.204.
          		 2 A0A0C6P5Y7 A0A1M8X3J3
          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.
          		 2 A0A0U5B923 A0A0U5B923
          Aldehyde dehydrogenase (quinone). [EC: 1.2.5.2]
          An aldehyde + a quinone + H(2)O = a carboxylate + a quinol.
          • Wide specificity; acts on straight-chain aldehydes up to C(10), aromatic aldehydes, glyoxylate and glyceraldehyde.
          • Formerly EC 1.2.99.3.
          		 1 W6V6A8