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CATH Superfamily 1.10.1280.10

Di-copper center containing domain from catechol oxidase

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:

"
Di-copper center containing domain from catechol oxidase
".

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 2231: Related to tyrosinase (Monophenol monooxygenase)

There are 4 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
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.
 46 A0A024SJR1 A0A088TQS0 A0A088X6X5 A0A095KE59 A0A095T2Q1 A0A0D0H0L2 A0A0E1SGN2 A0A0E1UMR8 A0A0F6G789 A0A0F6L485
(36 more...)
DNA-directed RNA polymerase. [EC: 2.7.7.6]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
  • Can initiate a chain de novo.
  • In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized.
  • See also EC 2.7.7.19 and EC 2.7.7.48.
 2 A0A084GAD1 A0A0C2FH25
Molybdopterin-synthase adenylyltransferase. [EC: 2.7.7.80]
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly- Gly-AMP.
  • Adenylates the C-terminus of the small subunit of the molybdopterin synthase.
  • This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit.
  • The reaction occurs in prokaryotes and eukaryotes.
  • In the human, the reaction is catalyzed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.
  • Formerly EC 2.7.7.n4.
 1 A0A0L9T242
Molybdopterin synthase sulfurtransferase. [EC: 2.8.1.11]
[Molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine + reduced acceptor = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + [cysteine desulfurase] + oxidized acceptor.
  • The enzyme transfers sulfur to form a thiocarboxylate moiety on the C-terminal glycine of the small subunit of EC 2.8.1.12.
  • In the human, the reaction is catalyzed by the rhodanese-like C-terminal domain (cf. EC 2.8.1.1) of the MOCS3 protein, a bifunctional protein that also contains EC 2.7.7.80 at the N-terminal domain.
  • Formerly EC 2.8.1.n1.
 1 A0A0L9T242