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CATH Superfamily 3.30.420.40

ATPase, nucleotide binding 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 76983: Rhamnulokinase

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
Rhamnulokinase. [EC: 2.7.1.5]
ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate.
    		 1918 A0A014NST8 A0A014NST8 A0A017I4Q4 A0A017I4Q4 A0A023DD23 A0A023DD23 A0A023V5W7 A0A023V5W7 A0A023Z5Z4 A0A023Z5Z4
    (1908 more...)
    L-rhamnose isomerase. [EC: 5.3.1.14]
    L-rhamnopyranose = L-rhamnulose.
    • The enzyme binds the closed ring form of the substrate and catalyzes ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites.
    • Isomerization proceeds via a hydride-shift mechanism.
    • While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyzes the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose.
    		 2 Q5WL39 Q5WL39