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CATH Superfamily 3.90.1150.10

Aspartate Aminotransferase, domain 1

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:

"
Aspartate Aminotransferase, domain 1
".

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 80712: Serine hydroxymethyltransferase (GlyA, SHMT)

There are 3 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
Glycine hydroxymethyltransferase. [EC: 2.1.2.1]
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine.
  • Also catalyzes the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- N(6),N(6),N(6)-trimethyl-L-lysine.
 38 A0A075G653 A0A075G653 A0A075H5H4 A0A075H5H4 A0A075I3S8 A0A075I3S8 A0A075IEJ7 A0A075IEJ7 A0A1E7IUF0 A0A1E7IUF0
(28 more...)
Fluorothreonine transaldolase. [EC: 2.2.1.8]
L-threonine + fluoroacetaldehyde = acetaldehyde + 4-fluoro-L-threonine.
  • Can also convert chloroacetaldehyde into 4-chloro-L-threonine.
  • Unlike EC 2.1.2.1 does not use glycine as a substrate.
 4 B6VP39 B6VP39 F8JMF0 F8JMF0
L-allo-threonine aldolase. [EC: 4.1.2.49]
L-allo-threonine = glycine + acetaldehyde.
  • This enzyme, characterized from the bacterium Aeromonas jandaei, is specific for L-allo-threonine and can not act on either L-threonine or L-serine.
  • Different from EC 4.1.2.5 and EC 4.1.2.48.
  • A previously listed enzyme with this name, EC 4.1.2.6, was deleted in 1971 after it was found to be identical to EC 2.1.2.1.
 4 A0A0A7LEA5 A0A0A7LEA5 Q58992 Q58992
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