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CATH Superfamily 2.60.40.1730

tricorn interacting facor f3 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 named:

"
tricorn interacting facor f3 domain
".

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 4176: Leukotriene A-4 hydrolase homolog

There are 5 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
Leukotriene-A(4) hydrolase. [EC: 3.3.2.6]
(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.
  • A bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities.
  • It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates.
  • It also converts leukotriene A(4) into leukotriene B(4), unlike EC 3.2.2.10 which converts leukotriene A(4) into 5,6-dihydroxy- 7,9,11,14-eicosatetraenoic acid.
 581 A0A010R5R8 A0A015IZ30 A0A017SKL0 A0A023EVM8 A0A024S6Z6 A0A026WSW2 A0A034VLU1 A0A060T0L8 A0A060WBS5 A0A060WJD0
(571 more...)
Aminopeptidase B. [EC: 3.4.11.6]
Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.
  • Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds.
  • One of the activities of the bifunctional enzyme EC 3.3.2.6.
  • Belongs to peptidase family M1.
 4 O09175 Q7RU04 Q8VCT3 Q9H4A4
Membrane alanyl aminopeptidase. [EC: 3.4.11.2]
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
  • Is not activated by heavy metal ions.
  • Belongs to peptidase family M1.
  • Formerly EC 3.4.1.2, EC 3.4.3.5 and EC 3.4.13.6.
 4 A0A1B2TXR3 A0A1C9W6A9 M7P180 Q26F87
TRNA dimethylallyltransferase. [EC: 2.5.1.75]
Dimethylallyl diphosphate + adenine(37) in tRNA = diphosphate + N(6)- dimethylallyladenine(37) in tRNA.
  • Formerly known as tRNA isopentenyltransferase (EC 2.5.1.8), but it is now known that dimethylallyl diphosphate, rather than isopentenyl diphosphate, is the substrate.
  • Formerly EC 1.8.6.1 and EC 2.5.1.8.
 1 A0A0F7S1E7
Soluble epoxide hydrolase. [EC: 3.3.2.10]
An epoxide + H(2)O = a glycol.
  • Catalyzes the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism.
  • It is involved in the metabolism of arachidonic epoxides (epoxyeicosatrienoic acids; EETs) and linoleic acid epoxides.
  • The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76.
  • Like EC 3.3.2.9, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate.
  • The enzyme can also use leukotriene A(4), the substrate of EC 3.3.2.6, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B(4) as the product.
  • Formerly EC 3.3.2.3, EC 4.2.1.63 and EC 4.2.1.64.
 1 A0A0L1I061