EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.1.19 | recombinant expression of His6-tagged enzyme in Escherichia coli | Mycolicibacterium smegmatis |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.1.19 | Mg2+ | required | Mycolicibacterium smegmatis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Mycolicibacterium smegmatis | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | Mycolicibacterium smegmatis ATCC 700084 / mc2155 | - |
ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.119 | Mycolicibacterium smegmatis | A0QZ49 | - |
- |
3.5.1.119 | Mycolicibacterium smegmatis ATCC 700084 | A0QZ49 | - |
- |
6.3.1.19 | Mycolicibacterium smegmatis | A0QZ42 | - |
- |
6.3.1.19 | Mycolicibacterium smegmatis ATCC 700084 / mc2155 | A0QZ42 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.3.1.19 | recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chormatography | Mycolicibacterium smegmatis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [IdeR]-L-lysine | - |
Mycolicibacterium smegmatis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[IdeR]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [IdeR]-L-lysine | - |
Mycolicibacterium smegmatis ATCC 700084 / mc2155 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[IdeR]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB]-L-lysine | - |
Mycolicibacterium smegmatis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[PanB]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [PanB]-L-lysine | - |
Mycolicibacterium smegmatis ATCC 700084 / mc2155 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[PanB]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Mycolicibacterium smegmatis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup product of the Dop reaction presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA | Mycolicibacterium smegmatis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | - |
Mycolicibacterium smegmatis ATCC 700084 / mc2155 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine | the Pup product of the Dop reaction presents a glutamate at its C-terminus (PupE) and, as such, can be readily conjugated to target proteins by PafA | Mycolicibacterium smegmatis ATCC 700084 / mc2155 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.119 | deamidase of Pup | - |
Mycolicibacterium smegmatis |
3.5.1.119 | Dop | - |
Mycolicibacterium smegmatis |
6.3.1.19 | PafA | - |
Mycolicibacterium smegmatis |
6.3.1.19 | Pup ligase | - |
Mycolicibacterium smegmatis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
6.3.1.19 | ATP | - |
Mycolicibacterium smegmatis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.119 | metabolism | tight Pup binding and the limited degree of interaction of the enzyme (Dop) with high-molecular-weight pupylated proteins results in preferred Pup deamidation over protein depupylation by this enzyme. Under starvation conditions, when accelerated protein pupylation is required, this bias is intensified by depletion of free Dop molecules, thereby minimizing the chance of depupylation. In contrast to Dop (deamidase of Pup), PafA (proteasome accessory factor A), presents a distinct preference for highmolecular-weight protein substrates. As such, PafA and Dop act in concert, rather than canceling each other's activity, to generate a high-molecular-weight pupylome. This bias in pupylome molecular weight distribution is consistent with the proposed nutritional role of the Pup-proteasome system (PPS) under starvation conditions | Mycolicibacterium smegmatis |
6.3.1.19 | metabolism | posttranslational regulation of coordinated enzyme activities in the prokaryotic ubiquitin-like protein (Pup)-proteasome system (PPS), overview. Pup, a ubiquitin analogue, is conjugated to proteins through the activities of two enzymes, Dop (deamidase of Pup) and PafA (proteasome accessory factor A), the Pup ligase. The depupylase activity of Dop counteracts the actions of PafA. tight Pup binding and the limited degree of Dop interaction with high-molecular-weight pupylated proteins results in preferred Pup deamidation over protein depupylation by enzyme Dop. Dop is depleted in the absence of Pup in stationary-phase cells. Pup-PanB and Pup-IdeR act as tight-binding competitors versus Pup binding by Dop. Pup binding stabilizes Dop and prevents its depletion. PafA and Dop generate a high-molecular-weight pupylome | Mycolicibacterium smegmatis |
6.3.1.19 | physiological function | Pup, a ubiquitin analogue, is conjugated to proteins through the activities of two enzymes, Dop (deamidase of Pup) and PafA (proteasome accessory factor A), the Pup ligase. Dop also catalyzes depupylation. Pupylation is a reversible process, with pupylated proteins being rescued from degradation following depupylation by Dop (deamidase of Pup). PafA (proteasome accessory factor A) and Dop are homologous enzymes, both binding Pup through interaction with its extended C-terminal region | Mycolicibacterium smegmatis |