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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 115703: Putative methylesterase 13, chloroplastic

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
Polyneuridine-aldehyde esterase. [EC: 3.1.1.78]
Polyneuridine aldehyde + H(2)O = 16-epivellosimine + CO(2) + methanol.
  • Following hydrolysis of this indole alkaloid ester, the carboxylic acid decarboxylates spontaneously giving the sarpagan skeleton.
  • Also acts on akuammidine aldehyde (the 16-epimer of polyneuridine aldehyde).
 74 A0A0B2NTY1 A0A0B2NTY1 A0A0B2NU46 A0A0B2NU46 A0A0B2NU51 A0A0B2NU51 A0A0B2NWT4 A0A0B2NWT4 A0A0B2NYM7 A0A0B2NYM7
(64 more...)
Pyrethroid hydrolase. [EC: 3.1.1.88]
Trans-permethrin + H(2)O = (3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2- dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate.
  • The enzyme is involved in degradation of pyrethroid pesticides.
  • The enzymes from Sphingobium sp., Klebsiella sp. and Aspergillus niger hydrolyze cis-permethrin at approximately equal rate to trans- permethrin.
  • The enzyme from mouse hydrolyzes trans-permethrin at a rate about 22-fold higher than cis-permethrin.
 26 A0A0A2HAD9 A0A0A2HAD9 A0A0M9EEP5 A0A0M9EEP5 A0A0Q9YPX1 A0A0Q9YPX1 A0A0Q9YSN7 A0A0Q9YSN7 A0A0W0YSL7 A0A0W0YSL7
(16 more...)
Carboxylesterase. [EC: 3.1.1.1]
A carboxylic ester + H(2)O = an alcohol + a carboxylate.
  • Wide specificity; also hydrolyzes vitamin A esters.
  • The enzymes from microsomes also catalyze the reactions of EC 3.1.1.2, EC 3.1.1.5, EC 3.1.1.6, EC 3.1.1.23, EC 3.1.1.28, EC 3.1.2.2, EC 3.5.1.4, and EC 3.5.1.13.
  • Formerly EC 3.1.1.12.
 26 A0A0B2QH22 A0A0B2QH22 A0A0B2QH78 A0A0B2QH78 A0A0B2R0L9 A0A0B2R0L9 A0A0B2SS52 A0A0B2SS52 B9R708 B9R708
(16 more...)
3-oxoadipate enol-lactonase. [EC: 3.1.1.24]
3-oxoadipate enol-lactone + H(2)O = 3-oxoadipate.
  • Acts on the product of EC 4.1.1.44.
  • Formerly EC 3.1.1.16.
 24 A0A098N126 A0A098N126 A0A0C5X4J7 A0A0C5X4J7 A0A0E2D300 A0A0E2D300 A0A0F6HF59 A0A0F6HF59 A0A0M4MRM3 A0A0M4MRM3
(14 more...)
Pheophorbidase. [EC: 3.1.1.82]
Pheophorbide a + H(2)O = pyropheophorbide a + methanol + CO(2).
  • Forms part of the chlorophyll degradation pathway, and is found in higher plants and in algae.
  • In higher plants it participates in de-greening processes such as fruit ripening, leaf senescence, and flowering.
  • Exists in two forms: type 1 is induced by senescence whereas type 2 is constitutively expressed.
  • Highly specific for pheophorbide as substrate (with a preference for pheophorbide a over pheophorbide b) as other chlorophyll derivatives such as protochlorophyllide a, pheophytin a and c, chlorophyll a and b, and chlorophyllide a cannot act as substrates.
  • Another enzyme, called pheophorbide demethoxycarbonylase (PDC), produces pyropheophorbide a from pheophorbide a without forming an intermediate although the precise reaction is not yet known.
 16 A0A0B2QH22 A0A0B2QH22 A0A0B2QH78 A0A0B2QH78 A0A0B2R0L9 A0A0B2R0L9 A0A0B2SS52 A0A0B2SS52 I1JZE9 I1JZE9
(6 more...)
(R)-mandelonitrile lyase. [EC: 4.1.2.10]
(R)-mandelonitrile = cyanide + benzaldehyde.
  • A variety of enzymes from different sources and with different properties.
  • Some are flavoproteins, others are not.
  • Active toward a number of aromatic and aliphatic hydroxynitriles (cyanohydrins).
 6 A0A178U928 A0A178U928 Q5S2C5 Q5S2C5 Q9LFT6 Q9LFT6
(S)-hydroxynitrile lyase. [EC: 4.1.2.47]
(1) An aliphatic (S)-hydroxynitrile = cyanide + an aliphatic aldehyde or ketone. (2) An aromatic (S)-hydroxynitrile = cyanide + an aromatic aldehyde.
  • Hydroxynitrile lyases catalyzes the the cleavage of hydroxynitriles into cyanide and the corresponding aldehyde or ketone.
  • In nature the liberation of cyanide serves as a defense mechanism against herbivores and microbial attack in plants.
  • In vitro the enzymes from Manihot esculenta and Hevea brasiliensis accept a broad range of aliphatic and aromatic carbonyl compounds as substrates and catalyze the formation of (S)-hydroxynitriles.
  • Formerly EC 4.1.2.37 and EC 4.1.2.39.
 4 P52704 P52704 P52705 P52705
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