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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 63395: Alanine aminotransferase 2, mitochondrial

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
1-aminocyclopropane-1-carboxylate synthase. [EC: 4.4.1.14]
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine.
  • Catalyzes an alpha,gamma-elimination.
 163 A0A0A0LKW1 A0A0B2NRY0 A0A0B2NS63 A0A0B2NXG2 A0A0B2PZA9 A0A0B2Q5Y5 A0A0B2Q9U8 A0A0B2QC61 A0A0B2QGJ9 A0A0B2QX87
(153 more...)
Alanine transaminase. [EC: 2.6.1.2]
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.
  • 2-aminobutanoate acts slowly instead of alanine.
 101 A0A024R6R2 A0A061IBG9 A0A074SRQ0 A0A086JF45 A0A086JR66 A0A086L6L9 A0A086LKQ0 A0A086QC13 A0A086QN34 A0A088S4I3
(91 more...)
Glycine transaminase. [EC: 2.6.1.4]
Glycine + 2-oxoglutarate = glyoxylate + L-glutamate.
    		 7 A0A084FWL0 A0A178WFM8 A0A178WG36 A0A1D8RJ21 A0A1D8RJ35 Q9LR30 Q9S7E9
    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.
    		 5 A0A084FWL0 A0A178WFM8 A0A178WG36 Q9LR30 Q9S7E9
    Alanine--oxo-acid transaminase. [EC: 2.6.1.12]
    L-alanine + a 2-oxo acid = pyruvate + an L-amino acid.
      		 1 A0A171B308
      Cystathionine gamma-lyase. [EC: 4.4.1.1]
      L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate.
      • The enzyme cleaves a carbon-sulfur bond, releasing L-cysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia.
      • The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10.
      • Also catalyzes the conversion of L-homoserine to 2-oxobutanoate and ammonia, of L-cystine to thiocysteine, pyruvate and ammonia, and of L-cysteine to pyruvate, hydrogen sulfide and ammonia.
      • Formerly EC 4.2.1.15.
      		 1 O23788
      3-methyl-2-oxobutanoate hydroxymethyltransferase. [EC: 2.1.2.11]
      5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate + H(2)O = tetrahydrofolate + 2-dehydropantoate.
        		 1 A0A178VE54
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