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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 96: Molybdenum cofactor sulfurase

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
Molybdenum cofactor sulfurtransferase. [EC: 2.8.1.9]
Molybdenum cofactor + L-cysteine + reduced acceptor + 2 H(+) = thio- molybdenum cofactor + L-alanine + H(2)O + oxidized acceptor.
  • Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide.
  • The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes.
  • In prokaryotes the reaction is catalyzed by two enzymes: EC 2.8.1.7, which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein.
 4 A2VD33 Q14CH1 Q96EN8 Q9N0E7