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CATH Superfamily 2.60.40.420

Cupredoxins - blue copper proteins

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:

"
Cupredoxins - blue copper proteins
".

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 24116: Iron transport multicopper oxidase FET3

There are 7 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
Laccase. [EC: 1.10.3.2]
4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.
  • A group of multi-copper proteins of low specificity.
  • Acts on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine.
  • The semiquinone may react further either enzymically or non- enzymically.
 154 A0A022Q819 A0A022Q819 A0A059U466 A0A059U466 A0A059U7S4 A0A059U7S4 A0A059UAZ0 A0A059UAZ0 A0A059UBJ3 A0A059UBJ3
(144 more...)
L-ascorbate oxidase. [EC: 1.10.3.3]
4 L-ascorbate + O(2) = 4 monodehydroascorbate + 2 H(2)O.
    		 56 A0A084FV90 A0A084FV90 A0A0A0LXB9 A0A0A0LXB9 A0A0B2PJR4 A0A0B2PJR4 A0A0B2QWJ4 A0A0B2QWJ4 A0A0B2RAC3 A0A0B2RAC3
    (46 more...)
    Acetate kinase. [EC: 2.7.2.1]
    ATP + acetate = ADP + acetyl phosphate.
    • While purified enzyme from Escherichia coli is specific for acetate, others have found that the enzyme can also use propanoate as a substrate, but more slowly.
    • Acetate can be converted into the key metabolic intermediate acetyl- CoA by coupling acetate kinase with EC 2.3.1.8.
    • Both this enzyme and EC 2.7.2.15 play important roles in the production of propanoate.
    		 2 A0A168CDI7 A0A168CDI7
    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.
    		 2 A0A084GGS2 A0A084GGS2
    Ferroxidase. [EC: 1.16.3.1]
    4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
      		 2 A2R3T0 A2R3T0
      Peroxidase. [EC: 1.11.1.7]
      2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
        		 2 A0A0N7Z1T5 A0A0N7Z1T5
        Endo-alpha-N-acetylgalactosaminidase. [EC: 3.2.1.97]
        3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H(2)O = 3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein].
        • The enzyme catalyzes the liberation of Gal-(1->3)-beta-GalNAc alpha- linked to serine or threonine residues of mucin-type glycoproteins.
        • EngBF from Bifidobacterium longum specifically acts on core 1-type O-glycan to release the disaccharide Gal-(1->3)-beta-GalNAc.
        • The enzymes from Clostridium perfringens, Enterococcus faecalis, Propionibacterium acnes and Alcaligenes faecalis show broader specificity (e.g. release of the core 2 trisaccharide Gal-(1->3)- beta-(GlcNAc-(1->6)-beta)-GalNAc or the core 3 disaccharide GlcNAc- (1->3)-beta-GalNAc).
        • The enzyme may play an important role in the degradation and utilization of mucins having core 1 O-glycan.
        • Formerly EC 3.2.1.110.
        		 2 A0A084GH29 A0A084GH29
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