CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Ubiquitin-activating enzyme E1 1

Enzyme Information

6.2.1.45
E1 ubiquitin-activating enzyme.
based on mapping to UniProt P22314
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 (1)

P22314
UBA1_HUMAN
Homo sapiens
Ubiquitin-like modifier-activating enzyme 1

PDB Structure

PDB 4P22
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1).
Xie, S.T.
Biosci.Biotechnol.Biochem.