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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 24176: Laccase, multicopper oxidase, benzenediol:oxygen o...

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.
 4144 A0A022PRX8 A0A022PRX8 A0A022PYV8 A0A022PYV8 A0A022Q819 A0A022Q819 A0A022Q9N6 A0A022Q9N6 A0A022QCS2 A0A022QCS2
(4134 more...)
L-ascorbate oxidase. [EC: 1.10.3.3]
4 L-ascorbate + O(2) = 4 monodehydroascorbate + 2 H(2)O.
    		 14 A0A0B2PB55 A0A0B2PB55 A0A0B2PHW5 A0A0B2PHW5 A0A0B2Q4N7 A0A0B2Q4N7 A0A0B2QRP4 A0A0B2QRP4 A0A0B2SPC9 A0A0B2SPC9
    (4 more...)
    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
    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.
    		 4 A0A151QWJ3 A0A151QWJ3 A0A151UFI3 A0A151UFI3
    2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
    A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
    • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
    • Alk-2-enals of shorter chain have lower affinities.
    • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
    • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
    • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
    		 2 A0A0B2NUI1 A0A0B2NUI1
    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
    Receptor protein-tyrosine kinase. [EC: 2.7.10.1]
    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
    • The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans.
    • In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies.
    • Formerly EC 2.7.1.112.
    		 2 A0A0B2NUI1 A0A0B2NUI1
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