ID A0A8A6AEE1_9CORY Unreviewed; 227 AA. AC A0A8A6AEE1; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. DE RecName: Full=NAD-dependent protein deacylase {ECO:0000256|HAMAP-Rule:MF_01121}; DE EC=2.3.1.286 {ECO:0000256|HAMAP-Rule:MF_01121}; DE AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01121}; GN Name=cobB {ECO:0000256|HAMAP-Rule:MF_01121}; GN ORFNames=J5O04_08985 {ECO:0000313|EMBL:QTH58947.1}; OS Corynebacterium sp. 1864. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium; unclassified Corynebacterium. OX NCBI_TaxID=2820399 {ECO:0000313|EMBL:QTH58947.1}; RN [1] {ECO:0000313|EMBL:QTH58947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=1864 {ECO:0000313|EMBL:QTH58947.1}; RA Guglielmino C.J.D.; RT "Complete genome of Corynebacterium sp. strain 1864."; RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|HAMAP-Rule:MF_01121}. 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; Evidence={ECO:0000256|HAMAP-Rule:MF_01121}; 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; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01121}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01121}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01121}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01121}. CC -!- DOMAIN: 2 residues (Tyr-68 and Arg-71) present in a large hydrophobic CC pocket are probably involved in substrate specificity. They are CC important for desuccinylation activity, but dispensable for CC deacetylation activity. {ECO:0000256|HAMAP-Rule:MF_01121}. CC -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01121}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01121}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP072111; QTH58947.1; -; Genomic_DNA. DR CDD; cd01412; SIRT5_Af1_CobB; 1. DR Gene3D; 3.30.1600.10; -; 1. DR HAMAP; MF_01121; Sirtuin_ClassIII; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR003000; Sirtuin. DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf. DR InterPro; IPR027546; Sirtuin_class_III. DR InterPro; IPR026590; Ssirtuin_cat_dom. DR Pfam; PF02146; SIR2; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR PROSITE; PS50305; SIRTUIN; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01121}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01121}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01121}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01121}. FT DOMAIN 6..227 FT /note="Deacetylase sirtuin-type" FT /evidence="ECO:0000259|PROSITE:PS50305" FT NP_BIND 95..98 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT NP_BIND 179..181 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT ACT_SITE 113 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT METAL 121 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT METAL 124 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT METAL 139 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT METAL 142 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT BINDING 68 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT BINDING 71 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" FT BINDING 219 FT /note="NAD; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01121" SQ SEQUENCE 227 AA; 25128 MW; 23DB0D4127A65A4F CRC64; MRQVPDPVQA LVDKAQRIVA FTGAGMSAES GLETYRDAET GLWENVDPTA MASIDAWARN PNPMWRWYLE RARRASEAKP NAGHRALASF RVITQNIDNL HERGGSQEVI HLHGSLFDYR CTICSRPYKG KLPHTPPACP LCGNLIRPGV VWFGEMLPTK EWARAEELIQ ECDLLIVVGT SGIVQPAASL PLLARNVLEI SPDETNLTPI ASYSWRTTAA QGLPLLF //