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CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like 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:

"
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 80: Thiazole biosynthesis adenylyltransferase ThiF

There are 3 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
Sulfur carrier protein ThiS adenylyltransferase. [EC: 2.7.7.73]
ATP + [ThiS] = diphosphate + adenylyl-[ThiS].
  • The enzyme catalyzes the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.
  • The enzyme shows significant structural similarity to ubiquitin- activating enzyme.
  • In Escherichia coli, but not in Bacillus subtilis, the enzyme forms a cross link from Cys-184 to the ThiS carboxy terminus (the position that is also thiolated) via an acyldisulfide.
  • Formerly EC 2.7.7.n3.
 3228 A0A024L9Q8 A0A024L9Q8 A0A024L9Q8 A0A024L9Q8 A0A024L9Q8 A0A024L9Q8 A0A024L9Q8 A0A024L9Q8 A0A024L9Q8 A0A024L9Q8
(3218 more...)
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.
 38 A0A0A1MCB6 A0A0A1MCB6 A0A0A1MCB6 A0A0A1MCB6 A0A0A1MCB6 A0A0A1MCB6 A0A1B2BBI3 A0A1B2BBI3 A0A1B2BBI3 A0A1B2BBI3
(28 more...)
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.
 2 A8WRE3 O44510