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CATH Superfamily 3.40.1020.10

Biosynthetic Threonine Deaminase; Domain 3

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:

"
Biosynthetic Threonine Deaminase; Domain 3
".

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 288: L-threonine dehydratase

There are 1 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
Threonine ammonia-lyase. [EC: 4.3.1.19]
L-threonine = 2-oxobutanoate + NH(3).
  • The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16), followed by tautomerization to an imine form and hydrolysis of the C-N bond.
  • The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10.
  • The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17.
  • Formerly EC 4.2.1.16.
 15 A0A0A8R9M9 A0A0C6EKD3 A0A0E1AQR8 A0A0H2ZL26 A0A0H3QUC2 A0A0P1D5Y7 A0A0V3SPV1 A0A157W258 A0A1C7BGD4 A0A1D5BW87
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