6.3.1.19: prokaryotic ubiquitin-like protein ligase
This is an abbreviated version!
For detailed information about prokaryotic ubiquitin-like protein ligase, go to the full flat file.
Word Map on EC 6.3.1.19
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6.3.1.19
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mycobacterium
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tuberculosis
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depupylation
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pup-proteasome
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actinobacteria
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depupylase
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deamidation
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ligases
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deamidase
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smegmatis
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ubiquitin-proteasome
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tcmsp
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cytoscape
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isopeptide
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genecards
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nitrospirae
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drug development
- 6.3.1.19
- mycobacterium
- tuberculosis
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depupylation
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pup-proteasome
- actinobacteria
- depupylase
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deamidation
- ligases
- deamidase
- smegmatis
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ubiquitin-proteasome
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tcmsp
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cytoscape
-
isopeptide
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genecards
- nitrospirae
- drug development
Reaction
Synonyms
PafA, proteasome accessory factor A, Pup ligase, Pup-protein ligase, Rv2097c, ubiquitin-like protein ligase
ECTree
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Reaction
Reaction on EC 6.3.1.19 - prokaryotic ubiquitin-like protein ligase
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
PafA catalyzes a two-step reaction by forming a gamma-glutamyl phosphate-mixed anhydride intermediate on the C-terminal glutamate of PupE by hydrolyzing ATP, followed by attaching it to nucleophilic substrates by catalyzing the formation of isopeptide bonds between PupE C-terminal glutamate gamma-carboxylate and the side chain of protein substrate lysine residues, mechanism of PafA self-pupylation, overview. K320 is the major target residue for the pupylation of PafA. During the self-pupylation of PafA, the attachment of the first Pup to PafA is catalyzed by the other PafA molecule through an intermolecular reaction, while the formation of the polymeric Pup chain is carried out in an intramolecular manner through the internal ligase activity of the already pupylated PafA. Among the three lysine residues, K7, K31 and K61, in Mycobacterium smegmatis Pup, K7 and K31 are involved in the formation of the poly-Pup chain in PafA poly-pupylation. Poly-pupylation of PafA can be reversibly regulated by depupylase Dop
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Bifidobacterium adolescentis ATCC 15703 / DSM 20083 / NCTC 11814 / E194a
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Acidothermus cellulolyticus ATCC 43068 / 11B
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Renibacterium salmoninarum ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Kocuria rhizophila ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Salinispora tropica ATCC BAA-916 / DSM 44818 / CNB-440
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Mycolicibacterium smegmatis ATCC 700084 / mc2155
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
PafA catalyzes a two-step reaction by forming a gamma-glutamyl phosphate-mixed anhydride intermediate on the C-terminal glutamate of PupE by hydrolyzing ATP, followed by attaching it to nucleophilic substrates by catalyzing the formation of isopeptide bonds between PupE C-terminal glutamate gamma-carboxylate and the side chain of protein substrate lysine residues, mechanism of PafA self-pupylation, overview. K320 is the major target residue for the pupylation of PafA. During the self-pupylation of PafA, the attachment of the first Pup to PafA is catalyzed by the other PafA molecule through an intermolecular reaction, while the formation of the polymeric Pup chain is carried out in an intramolecular manner through the internal ligase activity of the already pupylated PafA. Among the three lysine residues, K7, K31 and K61, in Mycobacterium smegmatis Pup, K7 and K31 are involved in the formation of the poly-Pup chain in PafA poly-pupylation. Poly-pupylation of PafA can be reversibly regulated by depupylase Dop
Mycolicibacterium smegmatis ATCC 700084 / mc2155
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Rhodococcus erythropolis PR4 / NBRC 100887
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ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine
reaction mechanisms of ligation to substrates and cleavage from pupylated substrates, overview. Pup passes a process of disorder-to-order transition
Micrococcus luteus ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230
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