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:

"
NAD(P)-binding Rossmann-like Domain
".

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 285373: Putative aspartate kinase, homoserine dehydrogenas...

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
Homoserine dehydrogenase. [EC: 1.1.1.3]
L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H.
  • The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+).
  • The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4.
16 A0A0E0IAK1 A0A1D6ENN2 A0A1D6Q023 A0A1J3E4C2 A0A1J3H5C5 A0A1J3IZD4 B8A1Q6 B9SHP2 K7TVF1 O63067
(6 more...)
Aspartate kinase. [EC: 2.7.2.4]
ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
  • The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 1.1.1.3.
  • This is also the case for two of the four isoenzymes in Arabidopsis thaliana.
  • The equilibrium constant strongly favors the reaction from right to left, i.e. the non-physiological direction of reaction.
10 A0A067JLN5 A0A0B2PX90 B9SHP2 O63067 O81852 P37142 P49079 P49080 Q0WRP9 Q9SA18
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