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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_2_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.
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FunFam 63074: Alanine--glyoxylate aminotransferase 2, mitochondr...

There are 12 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
2,2-dialkylglycine decarboxylase (pyruvate). [EC: 4.1.1.64]
2,2-dialkylglycine + pyruvate = dialkyl ketone + CO(2) + L-alanine.
  • Acts on 2-amino-2-methylpropanoate (i.e. 2-methylalanine), 2-amino-2- methylbutanoate and 1-aminocyclopentanecarboxylate.
 46 A0A060V252 A0A0B7D566 A0A0D6I8C3 A0A0D6IWM5 A0A0F0KKZ9 A0A0H2M2R5 A0A0J6WQ85 A0A0J6Y2A5 A0A0J6Z619 A0A0M6ZJU9
(36 more...)
Alanine--glyoxylate transaminase. [EC: 2.6.1.44]
L-alanine + glyoxylate = pyruvate + glycine.
  • With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate.
  • A second component also catalyzes the reaction of EC 2.6.1.51.
 38 A0A076P2U1 A0A090EY00 A0A099KGH9 A0A099KQT9 A0A0B2RFE6 A0A0B2S254 A0A0B2S602 A0A0D2MH45 A0A0E0UG38 A0A0E0UGP3
(28 more...)
Ethanolamine-phosphate phospho-lyase. [EC: 4.2.3.2]
Ethanolamine phosphate + H(2)O = acetaldehyde + NH(3) + phosphate.
  • Also acts on D- (or L)-1-aminopropan-2-ol O-phosphate.
  • Formerly EC 4.2.99.7.
 16 A0A060V252 A0A061IK62 A0A061IMN5 A0A0B7G4Z1 A0A0E9B3A5 A0A0E9BG54 A0A0E9BRC0 A0A0H3L783 A0A192PJI0 A0A1C3R547
(6 more...)
4-aminobutyrate--2-oxoglutarate transaminase. [EC: 2.6.1.19]
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
  • Some preparations also act on beta-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate.
 10 A0A0A1HT87 A0A0P1EN50 A0A0P1IHM8 A0A1L3LEE4 D8ITP7 E0SL23 L7VAR3 M4MLF7 Q8YD29 Q92UM7
(R)-3-amino-2-methylpropionate--pyruvate transaminase. [EC: 2.6.1.40]
(R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + L-alanine.
  • The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.22, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
  • Formerly EC 2.6.1.61.
 8 B7RRZ5 C9D219 D5RP09 Q17QF0 Q3UEG6 Q5RFA3 Q64565 Q9BYV1
5-aminovalerate transaminase. [EC: 2.6.1.48]
5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate.
    		 8 A0A0F0KKZ8 A0A0F0KWR2 A0A0F0L052 A0A0F0L7A2 A0A0F0LVH1 A0A0M9EF43 A0A0S4HU31 A0A100JY02
    Diaminobutyrate--2-oxoglutarate transaminase. [EC: 2.6.1.76]
    L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate.
    • Differs from EC 2.6.1.46, which has pyruvate as the amino-group acceptor.
    • This is the first enzyme in the ectoine biosynthesis pathway, the other enzymes involved being EC 2.3.1.178 and EC 4.2.1.108.
    		 3 A0A0P1I0C8 A0A157QNF7 A0A1E3GNM6
    5-phosphonooxy-L-lysine phospho-lyase. [EC: 4.2.3.134]
    (5R)-5-phosphonooxy-L-lysine + H(2)O = (S)-2-amino-6-oxohexanoate + NH(3) + phosphate.
    • Has no activity with phosphoethanolamine (cf. EC 4.2.3.2).
    		 2 Q8IUZ5 Q8R1K4
    Taurine--pyruvate aminotransferase. [EC: 2.6.1.77]
    Taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde.
    • The enzyme from Bilophila wadsworthia catalyzes a reversible reaction that starts an anaerobic taurine degradation pathway.
    • beta-alanine is also a significant amino group donor.
    • The enzyme from the bacterium Pseudomonas denitrificans PD1222 can also use hypotaurine, producing 2-sulfinoacetaldehyde, which spontaneously hydrolyzes to sulfite and acetaldehyde.
    • Unlike EC 2.6.1.55, 2-oxoglutarate cannot serve as an acceptor for the amino group.
    		 2 A0A0H5D7S1 A0A0P1FWX5
    Acetylornithine transaminase. [EC: 2.6.1.11]
    N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
    • Also acts on L-ornithine and N(2)-succinyl-L-ornithine.
    		 1 S0G0N3
    Beta-alanine--pyruvate transaminase. [EC: 2.6.1.18]
    L-alanine + 3-oxopropanoate = pyruvate + beta-alanine.
      		 1 A0A081G382
      Glutamate-1-semialdehyde 2,1-aminomutase. [EC: 5.4.3.8]
      (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
        		 1 G8PLJ0
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