UniProt functional annotation for Q9WYW0

UniProt code: Q9WYW0.

Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8).
Taxonomy: Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
 
Function: NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Has also depropionylation activity in vitro. Also able to ADP- ribosylate peptide substrates with Arg or Lys in the +2 position. The role of this function in vivo is not clear. {ECO:0000255|HAMAP- Rule:MF_01968, ECO:0000269|PubMed:16905097, ECO:0000269|PubMed:17684016, ECO:0000269|PubMed:19801667}.
 
Catalytic activity: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl- ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|HAMAP-Rule:MF_01968, ECO:0000269|PubMed:16905097};
Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01968, ECO:0000269|PubMed:15780941, ECO:0000269|PubMed:16768447, ECO:0000269|PubMed:16905097}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01968, ECO:0000269|PubMed:15780941, ECO:0000269|PubMed:16768447, ECO:0000269|PubMed:16905097};
Activity regulation: Non-competitively inhibited by nicotinamide but not by nicotinic acid. {ECO:0000269|PubMed:15780941}.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01968}.
Similarity: Belongs to the sirtuin family. Class U subfamily. {ECO:0000255|HAMAP-Rule:MF_01968}.

Annotations taken from UniProtKB at the EBI.