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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 22124: Polygalacturonase family protein, expressed

There are 7 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
Polygalacturonase. [EC: 3.2.1.15]
Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.
    		 504 A0A059SVB2 A0A059SVB2 A0A059SVE8 A0A059SVE8 A0A059SVJ2 A0A059SVJ2 A0A059SVT2 A0A059SVT2 A0A059SVT3 A0A059SVT3
    (494 more...)
    Galacturan 1,4-alpha-galacturonidase. [EC: 3.2.1.67]
    ((1->4)-alpha-D-galacturonide)(n) + H(2)O = ((1->4)-alpha-D- galacturonide)(n-1) + D-galacturonate.
      		 238 A0A0B2NYS2 A0A0B2NYS2 A0A0B2P5G8 A0A0B2P5G8 A0A0B2PCF3 A0A0B2PCF3 A0A0B2PHI4 A0A0B2PHI4 A0A0B2PS54 A0A0B2PS54
      (228 more...)
      Pectinesterase. [EC: 3.1.1.11]
      Pectin + n H(2)O = n methanol + pectate.
        		 32 A0A060A2E0 A0A060A2E0 A0A093ULN3 A0A093ULN3 A0A094EJM5 A0A094EJM5 A0A0C2J171 A0A0C2J171 A0A0F2MJY0 A0A0F2MJY0
        (22 more...)
        Alpha-L-rhamnosidase. [EC: 3.2.1.40]
        Hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L- rhamnosides.
        • The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing beta-L-rhamnose.
        • Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal alpha-L-rhamnose.
        		 4 A0A0F4Z261 A0A0F4Z261 A2QG68 A2QG68
        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.
        		 4 A0A087GTH9 A0A087GTH9 A0A178U9P2 A0A178U9P2
        Exo-poly-alpha-galacturonosidase. [EC: 3.2.1.82]
        Hydrolysis of pectic acid from the non-reducing end, releasing digalacturonate.
          		 2 Q9UUT3 Q9UUT3
          Cellulase. [EC: 3.2.1.4]
          Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
          • Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
          		 2 A0A164YZ28 A0A164YZ28
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