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CATH Superfamily 2.160.20.10

Single-stranded right-handed beta-helix, Pectin lyase-like

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:

"
Single-stranded right-handed beta-helix, Pectin lyase-like
".

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 22212: Probable pectate lyase C

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
Pectate lyase. [EC: 4.2.2.2]
Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
  • Favors pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10).
  • Formerly EC 4.2.99.3.
 1622 A0A022PR77 A0A022Q020 A0A022Q1L1 A0A022Q4U7 A0A022Q6X3 A0A022QJ11 A0A022QKF4 A0A022QTF7 A0A022QUT3 A0A022QXK5
(1612 more...)
Pectin lyase. [EC: 4.2.2.10]
Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
  • Favors pectin, the methyl ester, over pectate, the anion (which is the preferred substrate of EC 4.2.2.2).
 89 A0A068L4P0 A0A0A0Y6X2 A0A0B7FLC0 A0A0B7FTX0 A0A0B7FVN8 A0A0D9MLX6 A0A0D9MRY5 A0A0D9N9H5 A0A0F8D1G4 A0A0F8DBW8
(79 more...)
Elongation factor 4. [EC: 3.6.5.n1]
GTP + H(2)O = GDP + phosphate.
  • The enzyme is required for accurate and efficient protein synthesis under certain stress conditions.
  • May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes.
  • Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly.
  • Binds to ribosomes in a GTP-dependent manner.
 2 A0A0E0DWR2 A0A0E0DWR3
Pectate trisaccharide-lyase. [EC: 4.2.2.22]
Eliminative cleavage of unsaturated trigalacturonate as the major product from the reducing end of polygalacturonic acid/pectate.
  • Differs in specificity from EC 4.2.2.9 as the predominant action is removal of a trisaccharide rather than a disaccharide from the reducing end.
  • Disaccharides and tetrasaccharides may also be removed.
 2 A0A1M5UH95 A0A1M7YYK2
Non-reducing end alpha-L-arabinofuranosidase. [EC: 3.2.1.55]
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
  • Acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans.
  • Some EC 3.2.1.23 and EC 3.2.1.38 enzymes also hydrolyze alpha-L- arabinosides.
  • cf. EC 3.2.1.185.
  • Formerly EC 3.2.1.79.
 2 A0A1M7YTZ0 A0A1N6M2M8
Pyrroline-5-carboxylate reductase. [EC: 1.5.1.2]
L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H.
  • Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline.
 1 A0A0D9MP78
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