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CATH Superfamily 3.40.350.10

Creatinase/prolidase N-terminal 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 named:

"
Creatinase/prolidase N-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 6430: Xaa-Pro dipeptidase (M24 family)

There are 3 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
Xaa-Pro aminopeptidase. [EC: 3.4.11.9]
Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
  • Generally membrane bound enzyme present in both mammalian and bacterial cells.
  • Belongs to peptidase family M24B.
 93 A0A0F4YM87 A0A0F4Z2P2 A0A0F8AYN2 A0A0F8DM05 A0A0J6FU39 A0A167XFW3 A0A179UMV8 A0A179V168 A0A1D9Q6L2 A0A1E2Y041
(83 more...)
Xaa-Pro dipeptidase. [EC: 3.4.13.9]
Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
  • Possibly thiol dependent.
  • Cytosolic from most animal tissues.
  • Belongs to peptidase family M24A.
  • Formerly EC 3.4.3.7.
 13 A0A0B2NWK5 A0A140VJR2 A2RS23 A3LWP2 B9RKB6 E0VMG1 I1K635 K0KSD0 P12955 Q11136
(3 more...)
NAD(+) ADP-ribosyltransferase. [EC: 2.4.2.30]
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D- ribosyl)(n+1)-acceptor.
  • The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP- ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
 3 A0A0L1HI18 A0A178EJX9 E5A7J5