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Information on EC 6.2.1.45 - E1 ubiquitin-activating enzyme and Organism(s) Arabidopsis thaliana and UniProt Accession P92974

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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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Arabidopsis thaliana
UNIPROT: P92974
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected 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
Ub-activating enzyme
-
Ubiquitin-activating enzyme
-
Ub-activating enzyme
-
Ubiquitin-activating enzyme
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PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
show the reaction diagram
-
-
-
?
ATP + ubiquitin + [ubiquitin-activating protein UBA2]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBA2]-S-ubiquitinyl-L-cysteine
show the reaction diagram
enzyme forms higher molecular mass intermediates with ubiquitin
the enzyme-ubiquitin intermediates dissociate in presence of 2-mercaptoethanol, indicating thiolester linkage
-
?
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
show the reaction diagram
-
-
-
?
ATP + ubiquitin + [ubiquitin-activating protein UBA1]-L-cysteine
AMP + diphosphate + [ubiquitin-activating protein UBA1]-S-ubiquitinyl-L-cysteine
show the reaction diagram
enzyme forms higher molecular mass intermediates with ubiquitin
the enzyme-ubiquitin intermediates dissociate in presence of 2-mercaptoethanol, indicating thiolester linkage
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
show the reaction diagram
-
-
-
?
ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AtMUB3
the MUB3 protein of Arabidopsis thaliana strongly reduces the E2-ubiquitin formation by E1. Inhibitory effects of wild-type and mutant MUB3 proteins, overview
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AtMUB3
the MUB3 protein of Arabidopsis thaliana strongly reduces the E2-ubiquitin formation by E1. Inhibitory effects of wild-type and mutant MUB3 proteins, overview
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additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
MUB inhibition of E1 is conserved between plants and humans
physiological function
ubiquitin-activating enzyme (E1) activates ubiquitin (Ub) conjugating enzyme (E2)
evolution
MUB inhibition of E1 is conserved between plants and humans
physiological function
ubiquitin-activating enzyme (E1) activates ubiquitin (Ub) conjugating enzyme (E2)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UBE12_ARATH
1077
0
119624
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
119600
x * 12000 and x * 124000, SDS-PAGE, x * 119600, calculated
12000
x * 12000 and x * 124000, SDS-PAGE, x * 119600, calculated
124000
x * 12000 and x * 124000, SDS-PAGE, x * 119600, calculated
120300
x * 123000, SDS-PAGE, x * 120300, calculated
123000
x * 123000, SDS-PAGE, x * 120300, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 12000 and x * 124000, SDS-PAGE, x * 119600, calculated
?
x * 123000, SDS-PAGE, x * 120300, calculated
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene UBA2, sequence comparisons
expression in Escherichia coli
gene UBA1, sequence comparisons
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hatfield, P.M.; Gosink, M.M.; Carpenter, T.B.; Vierstra, R.D.
The ubiquitin-activating enzyme (E1) gene family in Arabidopsis thaliana
Plant J.
11
213-226
1997
Arabidopsis thaliana (P92974), Arabidopsis thaliana (P93028), Arabidopsis thaliana
Manually annotated by BRENDA team
Lu, X.; Malley, K.R.; Brenner, C.C.; Koroleva, O.; Korolev, S.; Downes, B.P.
A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotes
Nat. Commun.
7
12580
2016
Arabidopsis thaliana (P92974), Arabidopsis thaliana (P93028)
Manually annotated by BRENDA team