CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.720 | NAD(P)-binding Rossmann-like Domain |
Domain Context
CATH Clusters
| Superfamily | NAD(P)-binding Rossmann-like Domain |
| Functional Family | Adenylyltransferase and sulfurtransferase MOCS3 |
Enzyme Information
| 2.7.7.80 |
Molybdopterin-synthase adenylyltransferase.
based on mapping to UniProt P12282
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.
|
UniProtKB Entries (1)
| P12282 |
MOEB_ECOLI
Escherichia coli K-12
Molybdopterin-synthase adenylyltransferase
|
PDB Structure
| PDB | 1JWB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
Nature
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