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CATH Superfamily 3.40.980.10

MoaB/Mog-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:

"
MoaB/Mog-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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 5 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 molybdotransferase. [EC: 2.10.1.1]
Adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP.
  • Catalyzes the insertion of molybdenum into the ene-dithiol group of molybdopterin.
  • In eukaryotes this reaction is catalyzed by the N-terminal domain of a fusion protein whose C-terminal domain catalyzes EC 2.7.7.75.
 107 A0A024L551 A0A045IMK0 A0A069XWV4 A0A070VC88 A0A0D6H3Z2 A0A0E0VTB0 A0A0E1ANX8 A0A0E1LZJ2 A0A0E1XC31 A0A0F6AZ11
(97 more...)
Molybdopterin adenylyltransferase. [EC: 2.7.7.75]
ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.
  • Catalyzes the activation of molybdopterin for molybdenum insertion.
  • In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes molybdopterin molybdotransferase (EC 2.10.1.1).
  • The reaction requires a divalent cation such as Mg(2+) or Mn(2+).
  • Catalyzes the activation of molybdopterin for molybdenum insertion.
  • In eukaryotes, this reaction is catalyzed by the C-terminal domain of a fusion protein that also includes EC 2.10.1.1.
  • Formerly EC 2.7.7.n5.
 104 A0A070T3A7 A0A070UXV4 A0A080I285 A0A0E1T3Q0 A0A0F6BYK4 A0A0H3Q3R1 A0A0M1GMM5 A0A0M7NLF9 A0A127GFY2 A0A178U9Z9
(94 more...)
FAD synthetase. [EC: 2.7.7.2]
ATP + FMN = diphosphate + FAD.
  • Highly specific for ATP as phosphate donor.
  • The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates.
  • While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26.
 7 Q22017 Q5RCH4 Q626I0 Q68EH8 Q6ING7 Q8NFF5 Q8R123
Cyclic pyranopterin monophosphate synthase. [EC: 4.6.1.17]
(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate.
  • The enzyme catalyzes an early step in the biosynthesis of the molybdenum cofactor (MoCo).
  • Formerly EC 4.1.99.18.
 2 P59014 Q56208
Nicotinamide-nucleotide amidase. [EC: 3.5.1.42]
Beta-nicotinamide D-ribonucleotide + H(2)O = beta-nicotinate D-ribonucleotide + NH(3).
  • Also acts more slowly on beta-nicotinamide D-ribonucleoside.
 1 Q8EK32