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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 24179: 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.
 662 A0A059U6P5 A0A059U6P5 A0A059UBJ7 A0A059UBJ7 A0A067NGQ1 A0A067NGQ1 A0A067NRU7 A0A067NRU7 A0A0A0Q492 A0A0A0Q492
(652 more...)
Ferroxidase. [EC: 1.16.3.1]
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
    		 10 A2R3T0 A2R3T0 B0DLL7 B0DLL7 B0DRW0 B0DRW0 C0JRH1 C0JRH1 C0JRH2 C0JRH2
    Catechol oxidase. [EC: 1.10.3.1]
    2 catechol + O(2) = 2 1,2-benzoquinone + 2 H(2)O.
    • A type 3 copper protein that catalyzes exclusively the oxidation of catechols (i.e., o-diphenols) to the corresponding o-quinones.
    • The enzyme also acts on a variety of substituted catechols.
    • It is different from tyrosinase, EC 1.14.18.1, which can catalyze both the monooxygenation of monophenols and the oxidation of catechols.
    		 8 Q9HDS7 Q9HDS7 Q9HDS8 Q9HDS8 Q9HDS9 Q9HDS9 Q9UVU8 Q9UVU8
    Tyrosinase. [EC: 1.14.18.1]
    (1) 2 L-dopa + O(2) = 2 dopaquinone + 2 H(2)O. (2) L-tyrosine + O(2) = dopaquinone + H(2)O.
    • Found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin.
    • The enzyme, which is activated upon binding molecular oxygen, can catalyze both a monophenolase reaction cycle or a diphenolase reaction cycle.
    • During the monophenolase cycle, one of the bound oxygen atoms is transferred to a monophenol (such as L-tyrosine), generating an O-diphenol intermediate, which is subsequently oxidized to an o-quinone and released, along with a water molecule.
    • The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule.
    • During the diphenolase cycle the enzyme binds an external diphenol molecule (such as L-dopa) and oxidizes it to an O-quinone that is released along with a water molecule, leaving the enzyme in the intermediate met state.
    • The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state.
    • The second reaction is identical to that catalyzed by the related enzyme catechol oxidase (EC 1.10.3.1).
    • However, the latter can not catalyze the hydroxylation or monooxygenation of monophenols.
    • Formerly EC 1.14.17.2.
    		 2 B5B8U2 B5B8U2
    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
      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