CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.980 | Molybdenum Cofactor Biosythetic Enzyme; Chain A |
|
3.40.980.10 | MoaB/Mog-like domain |
Domain Context
CATH Clusters
| Superfamily | MoaB/Mog-like domain |
| Functional Family | Molybdopterin biosynthesis mog protein |
Enzyme Information
| 2.7.7.75 |
Molybdopterin adenylyltransferase.
based on mapping to UniProt P0AF03
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.
|
UniProtKB Entries (1)
| P0AF03 |
MOG_ECOLI
Escherichia coli K-12
Molybdopterin adenylyltransferase
|
PDB Structure
| PDB | 1DI7 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli.
J.Biol.Chem.
|