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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_4_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 353: Lipopolysaccharide biosynthesis protein RfbH

There are 1 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
GDP-4-dehydro-6-deoxy-alpha-D-mannose 3-dehydratase. [EC: 4.2.1.168]
GDP-4-dehydro-alpha-D-rhamnose + L-glutamate = GDP-4-dehydro-3,6-dideoxy- alpha-D-mannose + 2-oxoglutarate + ammonia.
  • This enzyme, involved in beta-L-colitose biosynthesis, is a unique vitamin-B6-dependent enzyme.
  • In the first step of catalysis, the bound pyridoxal phosphate (PLP) cafactor is transaminated to the pyridoxamine 5'-phosphate (PMP) form of vitamin B(6), using L-glutamate as the amino group donor.
  • The PMP cofactor then forms a Schiff base with the sugar substrate and the resulting adduct undergoes a 1,4-dehydration to eliminate the 3-OH group.
  • Hydrolysis of the product from the enzyme restores the PLP cofactor and results in the release of an unstable enamine intermediate.
  • This intermediate tautomerizes to form an imine form, which hydrolyzes spontaneously, releasing ammonia and forming the final product.
 1 G4WJD4
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