AC MF_01968; DC Protein; auto c? or TR HAMAP; MF_01968; -; 1; level=0 XX Names: Sirtuin_ClassU XX ID NPD DE RecName: Full=NAD-dependent protein deacetylase; DE EC=2.3.1.286; DE AltName: Full=Regulatory protein SIR2 homolog; GN Name=cobB; XX case CC -!- FUNCTION: NAD-dependent protein deacetylase which modulates the CC activities of several enzymes 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. else CC -!- FUNCTION: NAD-dependent protein deacetylase which modulates the CC activities of several enzymes which are inactive in their acetylated CC form. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the sirtuin family. Class U 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 end case KW Transferase 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:0008270; F:zinc ion binding end case XX FT From: NPD_THEMA (Q9WYW0) FT ACT_SITE 116 FT /note="Proton acceptor" FT Condition: H FT BINDING 22 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: A FT BINDING 26 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: T FT BINDING 33 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [FY] FT BINDING 33 FT /ligand="nicotinamide" FT /ligand_id="ChEBI:CHEBI:17154" FT Condition: [FY] FT BINDING 34 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: R FT BINDING 98 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: Q FT BINDING 100 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [IVT] FT BINDING 100 FT /ligand="nicotinamide" FT /ligand_id="ChEBI:CHEBI:17154" FT Condition: [IVT] FT BINDING 101 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: D FT BINDING 101 FT /ligand="nicotinamide" FT /ligand_id="ChEBI:CHEBI:17154" FT Condition: D FT BINDING 116 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: H FT BINDING 124 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 189 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: [ST] FT BINDING 190 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: S FT BINDING 214 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: N FT BINDING 215 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: [LAV] FT BINDING 216 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: G FT BINDING 231 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: [DE] FT BINDING 232 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Optional; Condition: [VGIA] XX Size: 229-260; Related: MF_01121!; MF_01967; Template: Q9WYW0; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in GEOKA Plasmid: None Comments: None XX # Revision 1.11 2022/11/19 //