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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 462: 2'-deamino-2'-hydroxyneamine transaminase

There are 2 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
Neamine transaminase. [EC: 2.6.1.93]
Neamine + 2-oxoglutarate = 6'-dehydroparomamine + L-glutamate.
  • The reaction occurs in vivo in the opposite direction.
  • Involved in the biosynthetic pathways of several clinically important aminocyclitol antibiotics, including kanamycin B, butirosin, neomycin and ribostamycin.
  • Works in combination with EC 1.1.3.43 to replace the 6'-hydroxy group of paromamine with an amino group.
  • The enzyme from the bacterium Streptomyces kanamyceticus can also catalyze EC 2.6.1.94, which leads to production of kanamycin A.
  • The enzyme from the bacterium Streptomyces fradiae can also catalyze EC 2.6.1.95, leading to production of neomycin C.
 1 Q6L741
2'-deamino-2'-hydroxyneamine transaminase. [EC: 2.6.1.94]
2'-deamino-2'-hydroxyneamine + 2-oxoglutarate = 2'-deamino-2'-hydroxy- 6'-dehydroparomamine + L-glutamate.
  • The reaction occurs in vivo in the opposite direction.
  • Involved in the biosynthetic pathway of kanamycin A and kanamycin D.
  • The enzyme, characterized from the bacterium Streptomyces kanamyceticus, can also catalyze EC 2.6.1.93.
 1 Q6L741