CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.30 | Elongation Factor Tu (Ef-tu); domain 3 |
|
2.40.30.180 | Ubiquitin-activating enzyme E1, FCCH domain |
Domain Context
CATH Clusters
| Superfamily | Ubiquitin-activating enzyme E1, FCCH domain |
| Functional Family | ubiquitin-like modifier-activating enzyme 1 |
Enzyme Information
| 6.2.1.45 |
E1 ubiquitin-activating enzyme.
based on mapping to UniProt O94609
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.
-!- Catalyzes the ATP-dependent activation of ubiquitin through the formation of a thioester bond between the C-terminal glycine of ubiquitin and the sulfhydryl side group of a cysteine residue in the E1 protein. -!- The two-step reaction consists of the ATP-dependent formation of an E1-ubiquitin adenylate intermediate in which the C-terminal glycine of ubiquitin is bound to AMP via an acyl-phosphate linkage, then followed by the conversion to an E1-ubiquitin thioester bond via the cysteine residue on E1 in the second step. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.
|
UniProtKB Entries (2)
| O94609 |
UBA1_SCHPO
Schizosaccharomyces pombe 972h-
Ubiquitin-activating enzyme E1 1
|
| A0A081CEG8 |
A0A081CEG8_PSEA2
Moesziomyces antarcticus
Ubiquitin-60S ribosomal protein L40 fusion protein
|
PDB Structure
| PDB | 5KNL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
S. pombe Uba1-Ubc15 Structure Reveals a Novel Regulatory Mechanism of Ubiquitin E2 Activity.
Mol. Cell
|
