View in Gene3D

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.
« Back to all FunFams

FunFam 115041: Non-heme chloroperoxidase (Chloride peroxidase)

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
Chloride peroxidase. [EC: 1.11.1.10]
RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.
  • Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds.
  • Also oxidizes bromide and iodide.
  • Enzymes of this type are either heme-thiolate proteins, or contain vanadate.
  • A secreted enzyme produced by the ascomycetous fungus Caldariomyces fumago (Leptoxyphium fumago) is an example of the heme-thiolate type.
  • It catalyzes the production of hypochlorous acid by transferring one oxygen atom from H(2)O(2) to chloride.
  • At a separate site it catalyzes the chlorination of activated aliphatic and aromatic substrates, via HClO and derived chlorine species.
  • In the absence of halides, it shows peroxidase (e.g. phenol oxidation) and peroxygenase activities.
  • The latter inserts oxygen from H(2)O(2) into, for example, styrene (side chain epoxidation) and toluene (benzylic hydroxylation), however, these activities are less pronounced than its activity with halides.
  • Has little activity with non-activated substrates such as aromatic rings, ethers or saturated alkanes.
  • The chlorinating peroxidase produced by ascomycetous fungi (e.g. Curvularia inaequalis) is an example of a vanadium chloroperoxidase, and is related to bromide peroxidase (EC 1.11.1.18).
  • It contains vanadate and oxidizes chloride, bromide and iodide into hypohalous acids.
  • In the absence of halides, it peroxygenates organic sulfides and oxidizes ABTS (2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)) but no phenols.
 702 A0A009HD80 A0A009HRP4 A0A009HS00 A0A009KHG4 A0A009MY45 A0A009PFI1 A0A009QQ70 A0A009R8N0 A0A009RY68 A0A010HG70
(692 more...)
Arylesterase. [EC: 3.1.1.2]
A phenyl acetate + H(2)O = a phenol + acetate.
  • Acts on many phenolic esters.
  • It is likely that the three forms of human paraoxonase are lactonases rather than aromatic esterases.
  • The natural substrates of the paraoxonases are lactones, with (+-)-5- hydroxy-6E,8Z,11Z,4Z-eicostetraenoic-acid 1,5-lactone being the best substrate.
 66 A0A024HLZ1 A0A066P942 A0A085H7H3 A0A0B7DCV7 A0A0D0SZJ4 A0A0D9HIG3 A0A0E2M8P5 A0A0E9BQF3 A0A0F0Y9M6 A0A0F1D1I6
(56 more...)
Dihydrocoumarin hydrolase. [EC: 3.1.1.35]
Dihydrocoumarin + H(2)O = melilotate.
  • Also hydrolyzes some other benzenoid 1,4-lactones.
 4 A0A0D5YH31 A0A0J0ZNT6 B0V5B0 Q83WC8
Haloalkane dehalogenase. [EC: 3.8.1.5]
1-haloalkane + H(2)O = a primary alcohol + halide.
  • Acts on a wide range of 1-haloalkanes, haloalcohols, haloalkenes and some haloaromatic compounds.
 3 A0A0E3KHV4 A0A0Q8D0S8 A0A143GFC0
Pimeloyl-[acyl-carrier protein] methyl ester esterase. [EC: 3.1.1.85]
Pimeloyl-[acyl-carrier protein] methyl ester + H(2)O = pimeloyl-[acyl- carrier protein] + methanol.
  • Involved in biotin biosynthesis in Gram-negative bacteria.
  • The enzyme exhibits carboxylesterase activity, particularly toward substrates with short acyl chains.
  • Even though the enzyme can interact with coenzyme A thioesters, the in vivo role of the enzyme is to hydrolyze the methyl ester of pimeloyl-[acyl carrier protein], terminating the part of the biotin biosynthesis pathway that is catalyzed by the fatty acid elongation enzymes.
 2 W7PFR9 W7PI91
Calcium-transporting ATPase. [EC: 3.6.3.8]
ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate + Ca(2+)(Side 2).
  • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
  • This enzyme family comprises three types of Ca(2+)-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in Saccharomyces cerevisiae.
  • The first and third transport one ion per ATP hydrolyzed, whereas the second transports two ions.
  • Formerly EC 3.6.1.38.
 1 G8Q8K7
Peroxidase. [EC: 1.11.1.7]
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
    		 1 A0A060SYR9