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Information on EC 6.2.1.45 - E1 ubiquitin-activating enzyme

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.45 E1 ubiquitin-activating enzyme
IUBMB Comments
Catalyses 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.
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UNIPROT: P52488
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
[E1 ubiquitin-activating enzyme]-L-cysteine
=
+
+
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
Synonyms
ubiquitin-conjugating enzyme, ube1l, ubiquitin-activating enzyme, ubiquitin-activating enzyme e1, ubiquitin-activating enzyme (e1), ubiquitin activating enzyme, sumo e1, e1 ubiquitin-activating enzyme, ubiquitin e1, ubiquitin activating enzyme e1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
ubiquitin:[E1 ubiquitin-activating enzyme] ligase (AMP-forming)
Catalyses 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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform UBA2
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBA2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
636
0
71259
Swiss-Prot
Secretory Pathway (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the C-terminal ubiquitin fold domain from yeast Uba2 alone and in complex with E2 enzyme Ubc9. Uba2 undergoes remarkable conformational changes during the reaction. The structure of the Uba2 domain-Ubc9 complex reveals interactions unique to Sumo E1 and E2. Comparison with a previous Ubc9-E3 complex structure demonstrates overlap between Uba2 and E3 binding sites on Ubc9, indicating that loading with Sumo and E3-catalyzed transfer to substrates are strictly separate steps
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, J.; Taherbhoy, A.M.; Hunt, H.W.; Seyedin, S.N.; Miller, D.W., Miller, D.J.; Huang, D.T.; Schulman, B.A.
Crystal structure of UBA2ufd-Ubc9: Insights into E1-E2 interactions in Sumo pathways
PLoS ONE
1
e15805
2010
Saccharomyces cerevisiae (P52488), Saccharomyces cerevisiae
Manually annotated by BRENDA team