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:

"
NAD(P)-binding Rossmann-like 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 252465: Adenylyltransferase and sulfurtransferase MOCS3

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
Molybdopterin-synthase adenylyltransferase. [EC: 2.7.7.80]
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly- Gly-AMP.
  • Adenylates the C-terminus of the small subunit of the molybdopterin synthase.
  • This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit.
  • The reaction occurs in prokaryotes and eukaryotes.
  • In the human, the reaction is catalyzed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain.
  • Formerly EC 2.7.7.n4.
3 A0A0D3FBS0 A2XAQ6 A3ACF3
Molybdopterin synthase sulfurtransferase. [EC: 2.8.1.11]
[Molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine + reduced acceptor = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + [cysteine desulfurase] + oxidized acceptor.
  • The enzyme transfers sulfur to form a thiocarboxylate moiety on the C-terminal glycine of the small subunit of EC 2.8.1.12.
  • In the human, the reaction is catalyzed by the rhodanese-like C-terminal domain (cf. EC 2.8.1.1) of the MOCS3 protein, a bifunctional protein that also contains EC 2.7.7.80 at the N-terminal domain.
  • Formerly EC 2.8.1.n1.
3 A0A0D3FBS0 A2XAQ6 A3ACF3