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CATH Superfamily 3.30.1300.10

Pantoate-beta-alanine ligase, C-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:

"
Pantoate-beta-alanine ligase, C-terminal 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 1: Pantothenate synthetase

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
Pantoate--beta-alanine ligase (AMP-forming). [EC: 6.3.2.1]
ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.
    		 6076 A0A023X919 A0A023X919 A0A023X919 A0A023X919 A0A023X919 A0A024L7V5 A0A024L7V5 A0A024L7V5 A0A024L7V5 A0A024L7V5
    (6066 more...)
    (d)CMP kinase. [EC: 2.7.4.25]
    ATP + (d)CMP = ADP + (d)CDP.
    • The prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor.
    • Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalyzed in prokaryotes by EC 2.7.4.22.
    • The enzyme phosphorylates dCMP nearly as well as it does CMP.
    		 4 L8AKD2 L8AKD2 Q55074 Q55074
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