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CATH Superfamily 3.40.50.880

Class I glutamine amidotransferase (GATase) domain

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: waiting to be named.

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 34169: Cobyrinate a,c-diamide synthase

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.

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EC Term Annotations Evidence
Cobyrinate a,c-diamide synthase (glutamine-hydrolyzing). [EC: 6.3.5.11]
2 ATP + cobyrinate + 2 L-glutamine + 2 H(2)O = 2 ADP + 2 phosphate + cobyrinate a,c-diamide + 2 L-glutamate.
  • This enzyme is the first glutamine amidotransferase that participates in the anaerobic (early cobalt insertion) biosynthetic pathway of adenosylcobalamin, and catalyzes the ATP-dependent synthesis of cobyrinate a,c-diamide from cobyrinate using either L-glutamine or ammonia as the nitrogen source.
  • It is proposed that the enzyme first catalyzes the amidation of the c-carboxylate, and then the intermediate is released into solution and binds to the same catalytic site for the amidation of the a-carboxylate.
  • The Km for ammonia is substantially higher than that for L-glutamine.
 2 B0R5X0 Q9HPL7