AC MF_02111; DC Protein; auto TR HAMAP; MF_02111; -; 1; level=0 XX Names: Pup_ligase XX ID PAFA DE RecName: Full=Pup--protein ligase; DE EC=6.3.1.19; DE AltName: Full=Proteasome accessory factor A; DE AltName: Full=Pup-conjugating enzyme; GN Name=pafA; XX CC -!- FUNCTION: Catalyzes the covalent attachment of the prokaryotic CC ubiquitin-like protein modifier Pup to the proteasomal substrate CC proteins, thereby targeting them for proteasomal degradation. This CC tagging system is termed pupylation. The ligation reaction involves the CC side-chain carboxylate of the C-terminal glutamate of Pup and the side- CC chain amino group of a substrate lysine. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + CC [protein]-L-lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin- CC like protein]-gamma-L-glutamyl)-[protein]-L-lysine.; EC=6.3.1.19; CC -!- PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. CC -!- PATHWAY: Protein modification; protein pupylation. CC -!- MISCELLANEOUS: The reaction mechanism probably proceeds via the CC activation of Pup by phosphorylation of its C-terminal glutamate, which CC is then subject to nucleophilic attack by the substrate lysine, CC resulting in an isopeptide bond and the release of phosphate as a good CC leaving group. CC -!- SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup- CC conjugating enzyme subfamily. XX DR Pfam; PF03136; Pup_ligase; 1; trigger=no DR NCBIfam; TIGR03686; Pupylate_PafA; 1; trigger=no DR PIRSF; PIRSF018077; UCP018077; 1; trigger=no XX KW ATP-binding KW Ligase KW Magnesium KW Metal-binding KW Nucleotide-binding KW Ubl conjugation pathway XX GO GO:0000287; F:magnesium ion binding GO GO:0005524; F:ATP binding GO GO:0019787; F:ubiquitin-like protein transferase activity GO GO:0010498; P:proteasomal protein catabolic process GO GO:0019941; P:modification-dependent protein catabolic process GO GO:0070490; P:protein pupylation XX FT From: PAFA_CORGL (Q8NQE1) FT ACT_SITE 64 FT /note="Proton acceptor" FT Condition: D FT BINDING 16 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: E FT BINDING 62 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: Y FT BINDING 70 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: E FT BINDING 60 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: R FT BINDING 73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [TS] FT BINDING 440 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: W XX Size: 447-504; Related: None; Template: P9WNU7; A0QZ42; Q8NQE1; Scope: Bacteria; Actinomycetota Fusion: Nter: None Cter: None Duplicate: in RHOER Plasmid: None Comments: None XX # Revision 1.18 2023/06/01 //