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CATH Superfamily 3.40.50.1820

Alpha/Beta hydrolase fold, catalytic 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 115381: Probable dipeptidyl peptidase 4

There are 6 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.
 482 A0A010QPU7 A0A010QPU7 A0A024R5Z6 A0A024R5Z6 A0A061I4W7 A0A061I4W7 A0A077XUS9 A0A077XUS9 A0A078SPS7 A0A078SPS7
(472 more...)
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.
 396 A0A015Q6M1 A0A015Q6M1 A0A015SAX5 A0A015SAX5 A0A015SIF2 A0A015SIF2 A0A015TNH9 A0A015TNH9 A0A015UUL7 A0A015UUL7
(386 more...)
Xaa-Pro dipeptidyl-peptidase. [EC: 3.4.14.11]
Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-|-p-nitroanilide and (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.
  • EC 3.4.14.5 catalyzes a similar reaction.
  • Belongs to peptidase family S15.
 28 A0A076P5I9 A0A076P5I9 A0A076P5K4 A0A076P5K4 A0A0H3CBJ5 A0A0H3CBJ5 A0A1M5XYX0 A0A1M5XYX0 A3LXS8 A3LXS8
(18 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.
 10 A0A1G4G5Y2 A0A1G4G5Y2 A5D7B7 A5D7B7 H2QIW2 H2QIW2 P97321 P97321 Q12884 Q12884
Succinate dehydrogenase (quinone). [EC: 1.3.5.1]
Succinate + a quinone = fumarate + a quinol.
  • The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria.
  • It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II).
  • In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone.
  • Cf. EC 1.3.5.4.
 2 A0A178F329 A0A178F329
DNA-directed RNA polymerase. [EC: 2.7.7.6]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
  • Catalyzes DNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time.
  • Can initiate a chain de novo.
  • In eukaryotes three forms of the enzyme have been distinguished on the basis of sensitivity of alpha-amanitin, and the type of RNA synthesized.
  • See also EC 2.7.7.19 and EC 2.7.7.48.
 2 A0A0L1HJF2 A0A0L1HJF2