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NPD_BDEBA
ID   NPD_BDEBA               Reviewed;         235 AA.
AC   Q6MJJ2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=NAD-dependent protein deacylase {ECO:0000255|HAMAP-Rule:MF_01121};
DE            EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_01121};
DE   AltName: Full=Regulatory protein SIR2 homolog {ECO:0000255|HAMAP-Rule:MF_01121};
GN   Name=cobB {ECO:0000255|HAMAP-Rule:MF_01121}; OrderedLocusNames=Bd2785;
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01121};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01121};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01121};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}.
CC   -!- DOMAIN: 2 residues (Tyr-58 and Arg-61) 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:0000255|HAMAP-Rule:MF_01121}.
CC   -!- MISCELLANEOUS: This protein might be subject to alternative promoter
CC       usage and might also encode a protein with a 13 residue-longer N-
CC       terminus. {ECO:0000250|UniProtKB:P0A2F2, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01121}.
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DR   EMBL; BX842653; CAE80568.1; -; Genomic_DNA.
DR   RefSeq; WP_011165171.1; NC_005363.1.
DR   AlphaFoldDB; Q6MJJ2; -.
DR   SMR; Q6MJJ2; -.
DR   STRING; 264462.Bd2785; -.
DR   EnsemblBacteria; CAE80568; CAE80568; Bd2785.
DR   KEGG; bba:Bd2785; -.
DR   eggNOG; COG0846; Bacteria.
DR   HOGENOM; CLU_023643_3_1_7; -.
DR   OMA; SMQVYPA; -.
DR   OrthoDB; 1264438at2; -.
DR   Proteomes; UP000008080; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036054; F:protein-malonyllysine demalonylase activity; IEA:InterPro.
DR   GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006476; P:protein deacetylation; IEA:UniProtKB-UniRule.
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; Metal-binding; NAD; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..235
FT                   /note="NAD-dependent protein deacylase"
FT                   /id="PRO_0000110296"
FT   DOMAIN          1..235
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   ACT_SITE        113
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         14..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         95..98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         180..182
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         204..206
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         222
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
SQ   SEQUENCE   235 AA;  26853 MW;  8C82A9B2A1EF5378 CRC64;
     MDLRLFKNIV ILTGAGISAE SGIRTFRDQD GLWEDHRIED VATPEAFARN PALVQRFYNL
     RRAQLRDPNL APNPAHQALV DLENLWEGNF LLVTQNVDNL HRRAGSKNLL HMHGRLDRVF
     CLHCDEHFEW LLDLAVDQPC PHCGRKGGVR PDIVWFGEMP HHMEEIYEAL DKADYFISIG
     TSGNVYPAAG FVRLAWKAKK IEINLKDTEI SPAFDEHFVG PASTEVPRFI TQFLE
 
 
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