CATH Classification

Domain Context

CATH Clusters

Superfamily Ubiquitin-activating enzyme E1, SCCH domain
Functional Family Ubiquitin-activating enzyme E1 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.
Lv, Z., Rickman, K.A., Yuan, L., Williams, K., Selvam, S.P., Woosley, A.N., Howe, P.H., Ogretmen, B., Smogorzewska, A., Olsen, S.K.
Mol. Cell