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CATH Superfamily 2.140.10.30

Dipeptidylpeptidase IV, N-terminal domain

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:

"
Dipeptidylpeptidase IV, 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.

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 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
Dipeptidyl-peptidase IV. [EC: 3.4.14.5]
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
  • A membrane-bound serine-type peptidase in mammals.
  • EC 3.4.14.11 catalyzes a similar reaction.
  • Belongs to peptidase family S9B.
 92 A0A024R5Z6 A0A0A1V0X1 A0A167SE74 A0A1D9QFN3 A0A1S9DU52 A0A1S9DYN3 A0A2I3RVD3 A0A384K439 A0A480UDQ9 A0S5V9
(82 more...)
Prolyl oligopeptidase. [EC: 3.4.21.26]
Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.
  • Found in vertebrates, plants and Flavobacterium.
  • Generally cytosolic, commonly activated by thiol compounds.
  • Belongs to peptidase family S9A.
  • Formerly EC 3.4.22.18.
 5 A5D7B7 G3RGI5 H2QIW2 P97321 Q12884
Xaa-Xaa-Pro tripeptidyl-peptidase. [EC: 3.4.14.12]
Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline.
  • This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease.
  • The enzyme releases tripeptides from the free amino terminus of peptides and small proteins, such as interleukin-6.
  • The enzyme possesses an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1' position.
  • The size of the peptide does not affect the rate of reaction.
 3 A0A0K2J4F0 B2RJX3 Q7MUW6