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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 63096: Low specificity L-threonine aldolase

There are 2 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
Low-specificity L-threonine aldolase. [EC: 4.1.2.48]
(1) L-threonine = glycine + acetaldehyde. (2) L-allo-threonine = glycine + acetaldehyde.
  • The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine.
  • The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine.
  • The enzyme can also catalyze the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis.
  • Different from EC 4.1.2.5 and EC 4.1.2.49.
 823 A0A010T3E0 A0A011NVS8 A0A011P4R7 A0A011PUX3 A0A016XHX7 A0A022FVT2 A0A023C7Z6 A0A023D8E5 A0A023WT02 A0A024EEK0
(813 more...)
L-threonine aldolase. [EC: 4.1.2.5]
L-threonine = glycine + acetaldehyde.
  • This enzyme is specific for L-threonine and can not utilize L-allo- threonine.
  • Different from EC 4.1.2.49 and EC 4.1.2.48.
 8 A0A059FYW9 A0A089P7B9 A0A1L6YLL9 A0A1N7RTL6 A0A1N7SBK6 A3RUM8 E6PRU1 Q0C4Y8
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