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CATH Superfamily 3.90.1150.10

Aspartate Aminotransferase, domain 1

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Aspartate Aminotransferase, domain 1
".

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 205: Aminotransferase

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
LL-diaminopimelate aminotransferase. [EC: 2.6.1.83]
LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5- tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H(2)O.
  • In vivo, the reaction occurs in the opposite direction to that shown above.
  • This is one of the final steps in the lysine biosynthesis pathway of plants (ranging from mosses to flowering plants).
  • Meso-diaminoheptanedioate, an isomer of LL-2,6-diaminoheptanedioate, and the structurally related compounds lysine and ornithine are not substrates.
  • 2-oxoglutarate cannot be replaced by oxaloacetate or pyruvate.
  • It is not yet known if the substrate of the biosynthetic reaction is the cyclic or acyclic form of tetrahydropyridine-2,6-dicarboxylate.
 17 A0A2Z5PH27 A0A2Z5PH27 A0A2Z5PH27 A0A2Z5PH27 A0A2Z5PQC8 A0A2Z5PQC8 A0A2Z5PQC8 A0A2Z5PQC8 G0H302 G0H302
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