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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_3_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 174: Probable hercynylcysteine sulfoxide lyase

Please note: GO 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.

There are 0 GO terms relating to "molecular function"

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.

There are 2 GO terms relating to "biological process"

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.
GO Term Annotations Evidence
Ergothioneine biosynthesis from histidine via N-alpha,N-alpha,N-alpha-trimethyl-L-histidine GO:0052704
The pathway resulting in the formation of ergothioneine from histidine. Histidine undergoes three methylations by a histidine-alpha-N-methyltransferase (EC:2.1.1.44) to form N-alpha,N-alpha,N-alpha-trimethyl-L-histidine (also known as hercynine or histidine betaine). N-alpha,N-alpha,N-alpha-trimethyl-L-histidine is modified by the ligation of gamma-glutamyl-cysteine and oxygen; this intermediate undergoes further modification by the removal of glutamate to produce hercynylcysteine sulfoxide. Finally, a beta-lyase acts on this compound, removing pyruvate, ammonia and oxygen to produce ergothioneine.
 7 O69668 (/ISS) O69668 (/ISS) O69668 (/ISS) O69668 (/ISS) O69668 (/ISS) O69668 (/ISS) O69668 (/ISS)
Ergothioneine biosynthesis from histidine via N-alpha,N-alpha,N-alpha-trimethyl-L-histidine GO:0052704
The pathway resulting in the formation of ergothioneine from histidine. Histidine undergoes three methylations by a histidine-alpha-N-methyltransferase (EC:2.1.1.44) to form N-alpha,N-alpha,N-alpha-trimethyl-L-histidine (also known as hercynine or histidine betaine). N-alpha,N-alpha,N-alpha-trimethyl-L-histidine is modified by the ligation of gamma-glutamyl-cysteine and oxygen; this intermediate undergoes further modification by the removal of glutamate to produce hercynylcysteine sulfoxide. Finally, a beta-lyase acts on this compound, removing pyruvate, ammonia and oxygen to produce ergothioneine.
 1 A0R5M7 (/IDA)

There are 0 GO terms relating to "cellular component"

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.