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:

"
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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

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.
    1162 A0A009GIX5 A0A009IR61 A0A009KN41 A0A009PF93 A0A009S8V2 A0A009SGY6 A0A015QT68 A0A015Z4P3 A0A016ASP4 A0A016EJ18
    (1152 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.
    31 A0A1W5CKH2 A0A1Z4KHU1 A0A2G8PF90 A2BTH1 A2C536 A2CBX2 A3PF80 A5GIY5 A5GVR3 A8G795
    (21 more...)