Information on EC 6.3.1.19 - prokaryotic ubiquitin-like protein ligase

Word Map on EC 6.3.1.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.3.1.19
-
RECOMMENDED NAME
GeneOntology No.
prokaryotic ubiquitin-like protein ligase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
[prokaryotic ubiquitin-like protein]:[protein]-L-lysine
The enzyme has been characterized from the bacteria Mycobacterium tuberculosis and Corynebacterium glutamicum. It catalyses the ligation of the prokaryotic ubiquitin-like protein (Pup) to a target protein by forming a bond between an epsilon-amino group of a lysine residue of the target protein and the gamma-carboxylate of the C-terminal glutamate of the ubiquitin-like protein (Pup). The attachment of Pup, also known as Pupylation, marks proteins for proteasomal degradation.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [adenylate kinase-His6]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[adenylate kinase-His6]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [malonyl Co-A acyl carrier protein transacylase]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[malonyl Co-A acyl carrier protein transacylase]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [myo-inositol-1-phosphate synthetase]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[myo-inositol-1-phosphate synthetase]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [phosphoenolpyruvate-protein phosphotransferase I]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[phosphoenolpyruvate-protein phosphotransferase I]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein PanB]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein PanB]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-[[prokaryotic ubiquitin-like protein]-L-glutamate]-[[protein]-L-lysine]
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
show the reaction diagram
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine
ADP + phosphate + N6-[[prokaryotic ubiquitin-like protein]-L-glutamate]-[[protein]-L-lysine]
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0087
ATP
-
25°C, pH 7.4
0.0014
[prokaryotic ubiquitin-like protein]-L-glutamate
-
25°C, pH 7.4
-
0.0142
[protein PanB]-L-lysine
-
25°C, pH 7.4
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023
[prokaryotic ubiquitin-like protein]-L-glutamate
Mycobacterium tuberculosis
-
pH 8.0, 30°C
-
0.023
[protein PanB]-L-lysine
Mycobacterium tuberculosis
-
pH 8,0, 30°C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme with ADP, protein (Pup) ligase PafA and the depupylase/deamidase Dop are are close structural homologues
the enzyme from Corynebacterium glutamicum is C-terminally fused with Pup or N-terminally truncated fragments of prokaryotic ubiquitin-like protein (Pup) from the same organism. Crystals are obtained only with the shortest fragment tested, PupE38-64. The crystal structure of Pup in complex with the enzyme, reveals that a long groove wrapping around the enzyme serves as a docking site for Pup. Upon binding, the C-terminal region of the intrinsically disordered Pup becomes ordered to form two helices connected by a linker, positioning the C-terminal glutamate in the active site of PafA
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expressed in Escherichia coli
-
recombinant His6-tagged enzyme expressed in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of the Mycobacterium tuberculosis pupylation pathway in Escherichia coli
-
the pafA gene is cloned with a C-terminal His6-tag, expression in Escherichia coli
-
Show AA Sequence (1264 entries)
Please use the Sequence Search for a specific query.