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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 112: Probable cysteine desulfurase

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
Cysteine desulfurase. [EC: 2.8.1.7]
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
  • The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors.
  • The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin).
  • In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation.
 136 A0A045IZN1 A0A045IZN1 A0A045IZN1 A0A045IZN1 A0A045IZN1 A0A045IZN1 A0A045IZN1 A0A045IZN1 A0A045IZN1 A0A045IZN1
(126 more...)
Selenocysteine lyase. [EC: 4.4.1.16]
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.
  • Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction.
  • The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7).
 4 A0A178WGK3 A0A178WGK3 Q93WX6 Q93WX6
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