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 + [proteasome-interacting ATPase]-L-lysine | Mycobacterium tuberculosis | pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine | Mycobacterium tuberculosis ATCC 25618 | pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.1.19 | Mycobacterium tuberculosis | P9WNU7 | - |
- |
6.3.1.19 | Mycobacterium tuberculosis ATCC 25618 | P9WNU7 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.3.1.19 | - |
Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine | pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive | Mycobacterium tuberculosis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine | pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly at Lys591 | Mycobacterium tuberculosis | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine | pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly on one target lysine. Pupylation at this position prevents interaction of Mpa/prokaryotic ubiquitin-like protein(Pup) with the proteasome core. Ultimately, pupylation leads to deoligomerization of the Mpa hexamer driven by the unfolding activity of Mpa, thereby rendering Mpa-Pup fully inactive | Mycobacterium tuberculosis ATCC 25618 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine | - |
? | |
6.3.1.19 | ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [proteasome-interacting ATPase]-L-lysine | pupylation of proteasome-interacting ATPase (Mpa) occurs predominantly at Lys591 | Mycobacterium tuberculosis ATCC 25618 | ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[proteasome-interacting ATPase]-L-lysine | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.3.1.19 | PafA | ambiguous | Mycobacterium tuberculosis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
6.3.1.19 | metabolism | pupylation is a bacterial post-translational modification of target proteins on lysine residues with prokaryotic ubiquitinlike protein (Pup). Pup-tagged substrates are recognized by a proteasome-interacting ATPase (Mpa) in Mycobacterium tuberculosis. Mpa unfolds pupylated substrates and threads them into the proteasome core particle for degradation | Mycobacterium tuberculosis |