View in Gene3D

CATH Superfamily 3.40.640.10

Type I PLP-dependent aspartate aminotransferase-like (Major domain)

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Type I PLP-dependent aspartate aminotransferase-like (Major 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.
« Back to all FunFams

FunFam 24: Kynurenine--oxoglutarate transaminase 3

There are 4 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
Kynurenine--oxoglutarate transaminase. [EC: 2.6.1.7]
L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
  • Also acts on 3-hydroxykynurenine.
  • The product 4-(2-aminophenyl)-2,4-dioxobutanoate is converted into kynurenate by a spontaneous reaction.
 22 A8K563 A8K563 B4DW13 B4DW13 G2WGV6 G2WGV6 P47039 P47039 Q05CI8 Q05CI8
(12 more...)
Cysteine-S-conjugate beta-lyase. [EC: 4.4.1.13]
An L-cysteine-S-conjugate + H(2)O = RSH + NH(3) + pyruvate.
  • A pyridoxal 5'-phosphate protein.
  • The enzyme is promiscuous regarding the moiety conjugated to L-cysteine, and can accept both aliphatic and aromatic substitutions.
  • The enzyme cleaves a carbon-sulfur bond, releasing a thiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
  • While bacteria and plants have dedicated enzymes, all of the animal enzymes discovered thus far are bifunctional, most of which also act as aminotransferases.
  • Formerly EC 4.4.1.6 and EC 4.4.1.8.
 18 A8K563 A8K563 B4DW13 B4DW13 Q05CI8 Q05CI8 Q08415 Q0P5G4 Q16773 Q16773
(8 more...)
Glutamine--phenylpyruvate transaminase. [EC: 2.6.1.64]
L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine.
  • L-methionine, L-histidine and L-tyrosine can act as donors.
  • Has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15).
 10 A8K563 A8K563 Q05CI8 Q05CI8 Q08415 Q16773 Q16773 Q54KM6 Q8BTY1 Q8BTY1
Kynurenine--glyoxylate transaminase. [EC: 2.6.1.63]
L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine.
  • Acts, more slowly, on L-phenylalanine, L-histidine and L-tyrosine.
 8 B4DW13 B4DW13 Q0P5G4 Q58FK9 Q6YP21 Q6YP21 Q71RI9 Q7T3E5