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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 63220: Molybdenum cofactor sulfurase, putative

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
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.
 527 A0A010QXS5 A0A015KRC1 A0A017S5L0 A0A022QJW0 A0A022WAH6 A0A022Y1N7 A0A024SFH1 A0A024USG2 A0A034WQ45 A0A059BNC2
(517 more...)
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.
 14 A0A074STE4 A0A086J9M6 A0A086JRK5 A0A086KUC7 A0A086LK21 A0A086PH27 A0A086PVC0 A0A0A1UDC4 A0A125YJ19 A0A139XLI1
(4 more...)
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