(data stored in ACNUC1104 zone)

SWISSPROT: B1K3Q3_BURCC

ID   B1K3Q3_BURCC            Unreviewed;       304 AA.
AC   B1K3Q3;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|HAMAP-Rule:MF_01967};
DE            EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_01967};
DE   AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01967};
GN   Name=cobB {ECO:0000256|HAMAP-Rule:MF_01967};
GN   OrderedLocusNames=Bcenmc03_3622 {ECO:0000313|EMBL:ACA92774.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92774.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC       activities of several enzymes which are inactive in their
CC       acetylated form. {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC         acetyl-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         Evidence={ECO:0000256|HAMAP-Rule:MF_01967};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01967};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01967};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01967}.
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DR   EMBL; CP000959; ACA92774.1; -; Genomic_DNA.
DR   EnsemblBacteria; ACA92774; ACA92774; Bcenmc03_3622.
DR   KEGG; bcm:Bcenmc03_3622; -.
DR   HOGENOM; HOG000085953; -.
DR   OMA; RRHYWAR; -.
DR   Proteomes; UP000002169; Chromosome 2.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1600.10; -; 1.
DR   HAMAP; MF_01967; Sirtuin_ClassII; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR   InterPro; IPR026587; Sirtuin_class_II.
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;
DR   PRODOM; B1K3Q3.
DR   SWISS-2DPAGE; B1K3Q3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01967};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01967};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01967};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01967};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   DOMAIN       20    292       Deacetylase sirtuin-type.
FT                                {ECO:0000259|PROSITE:PS50305}.
FT   NP_BIND     115    118       NAD. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   NP_BIND     232    234       NAD. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   NP_BIND     258    260       NAD. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   ACT_SITE    133    133       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01967}.
FT   METAL       141    141       Zinc. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   METAL       144    144       Zinc. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   METAL       192    192       Zinc. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   METAL       195    195       Zinc. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   BINDING     276    276       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01967}.
SQ   SEQUENCE   304 AA;  32278 MW;  116F97002AEDD907 CRC64;
     MNDKALPDSS LADADPAALD ALQTFVERHP RLLVLTGAGI STDSGIPGYR DRNGQWMRSP
     PIQLQEFLGS DAARRRYWAR SMIGWPVVGR ARPNGSHVAL ARLGDAGRIE RLVTQNVDGL
     HQRAGSDDVI ELHGGINGVT CLECGAHHAR ATIQTVLEAD NPELLGAQAE PAADGDAHLE
     WAALDTFRVP ACPACGGLLK PAVVFFGENV PRERVALASQ ALDAADALLV VGSSLMVYSG
     YRFCVWAQAQ HKPVAALNLG HTRADPMLTL KVEAHCAPAL DALVARLGLG RNSASTSDTT
     EHAS
//

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