AC MF_01121; DC Protein; auto c? or TR HAMAP; MF_01121; -; 1; level=0 XX Names: Sirtuin_ClassIII XX ID NPD DE RecName: Full=NAD-dependent protein deacylase; DE EC=2.3.1.286; DE AltName: Full=Regulatory protein SIR2 homolog; GN Name=cobB; XX case and CC -!- FUNCTION: NAD-dependent lysine deacetylase that specifically removes CC acetyl groups on target proteins. Also acts as a protein-lysine CC deacylase by mediating protein desuccinylation and de-2- CC hydroxyisobutyrylation. Modulates the activities of several proteins CC which are inactive in their acylated form. else case and and not CC -!- FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that CC specifically removes acetyl and succinyl groups on target proteins. CC Modulates the activities of several proteins which are inactive in CC their acylated form. else case and CC -!- FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that CC specifically removes acetyl and succinyl groups on target proteins. CC Modulates the activities of several proteins which are inactive in CC their acylated form. Deacetylates the N-terminal lysine residue of CC Alba, the major archaeal chromatin protein and that, in turn, increases CC Alba's DNA binding affinity, thereby repressing transcription. else case and not CC -!- FUNCTION: NAD-dependent protein deacetylase which modulates the CC activities of several proteins which are inactive in their acetylated CC form. else case and not CC -!- FUNCTION: NAD-dependent protein deacetylase which modulates the CC activities of several proteins which are inactive in their acetylated CC form. Deacetylates the N-terminal lysine residue of Alba, the major CC archaeal chromatin protein and that, in turn, increases Alba's DNA CC binding affinity, thereby repressing transcription. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl- CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide; CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; CC EC=2.3.1.286; case CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O- CC succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; CC Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832; end case case and CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + NAD(+) = CC 2''-O-(2-hydroxyisobutanoyl)-ADP-D-ribose + L-lysyl-[protein] + CC nicotinamide; Xref=Rhea:RHEA:24364, Rhea:RHEA-COMP:9752, Rhea:RHEA- CC COMP:15921, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:144968, ChEBI:CHEBI:144969; end case case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. case CC -!- DOMAIN: 2 residues (#{Tyr-64} and #{Arg-67}) present in a large CC hydrophobic pocket are probably involved in substrate specificity. They CC are important for desuccinylation activity, but dispensable for CC deacetylation activity. end case CC -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily. XX DR PROSITE; PS50305; SIRTUIN; 1; trigger=yes DR Pfam; PF02146; SIR2; 1; trigger=no XX KW Cytoplasm KW NAD case KW Metal-binding KW Zinc end case case KW Transcription KW Transcription regulation KW Transferase end case XX GO GO:0005737; C:cytoplasm GO GO:0034979; F:NAD-dependent protein deacetylase activity GO GO:0070403; F:NAD+ binding GO GO:0006476; P:protein deacetylation case GO GO:0036055; F:protein-succinyllysine desuccinylase activity GO GO:0036048; P:protein desuccinylation end case case GO GO:0008270; F:zinc ion binding end case XX FT From: NPD1_ARCFU (O28597) FT BINDING 20..39 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: G-A-G-x-S-[AK]-x-S-G-[ILV]-x-T-x(7,8)-W FT BINDING 98..101 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: Q-N-[IV]-[DE] FT BINDING 185..187 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: G-[TS]-S FT BINDING 211..213 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: N-x(2) FT ACT_SITE 116 FT /note="Proton acceptor" FT Condition: H FT BINDING 124 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Optional; Group: 1; Condition: C FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Optional; Group: 2; Condition: C FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Optional; Group: 1; Condition: C FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Optional; Group: 2; Condition: C FT BINDING 64 FT /ligand="substrate" FT Optional; Group: 3; Condition: Y FT BINDING 67 FT /ligand="substrate" FT Optional; Group: 3; Condition: R FT BINDING 229 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" XX Size: 208-262; Related: MF_01967; MF_01968; Template: O28597; Q9NXA8; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in ARCFU, PSESM, P0A2F2 Plasmid: None Comments: The gene name sir2 is used in a few prokaryotes. The gene is subject to alternative promoter usage in Salty, giving rise to 2 proteins with different N-termini. The longer protein is used in the seed alignment. Other Enterobacteriaceae probably do that too, maybe other bacteria as well. XX # Revision 1.37 2022/11/19 //