NPD_SACS2
ID NPD_SACS2 Reviewed; 247 AA.
AC Q97VX5;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=NAD-dependent protein deacetylase {ECO:0000255|HAMAP-Rule:MF_01968};
DE EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_01968};
DE AltName: Full=Regulatory protein SIR2 homolog {ECO:0000255|HAMAP-Rule:MF_01968};
DE AltName: Full=ssSir2;
GN Name=cobB {ECO:0000255|HAMAP-Rule:MF_01968}; OrderedLocusNames=SSO2478;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF HIS-116.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11935028; DOI=10.1126/science.1070506;
RA Bell S.D., Botting C.H., Wardleworth B.N., Jackson S.P., White M.F.;
RT "The interaction of Alba, a conserved archaeal chromatin protein, with Sir2
RT and its regulation by acetylation.";
RL Science 296:148-151(2002).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01968, ECO:0000269|PubMed:11935028}.
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_01968};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01968};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01968};
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01968}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class U subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01968}.
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DR EMBL; AE006641; AAK42615.1; -; Genomic_DNA.
DR PIR; H90419; H90419.
DR RefSeq; WP_010923883.1; NC_002754.1.
DR AlphaFoldDB; Q97VX5; -.
DR SMR; Q97VX5; -.
DR STRING; 273057.SSO2478; -.
DR EnsemblBacteria; AAK42615; AAK42615; SSO2478.
DR GeneID; 1453942; -.
DR KEGG; sso:SSO2478; -.
DR PATRIC; fig|273057.12.peg.2556; -.
DR eggNOG; arCOG04248; Archaea.
DR HOGENOM; CLU_023643_3_1_2; -.
DR OMA; SMQVYPA; -.
DR PhylomeDB; Q97VX5; -.
DR BRENDA; 2.3.1.B42; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IBA:GO_Central.
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 Gene3D; 3.30.1600.10; -; 1.
DR HAMAP; MF_01968; Sirtuin_ClassU; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR028628; Sirtuin_class_U.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; NAD; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..247
FT /note="NAD-dependent protein deacetylase"
FT /id="PRO_0000110388"
FT DOMAIN 4..246
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT ACT_SITE 116
FT /note="Proton acceptor"
FT BINDING 21..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 98..101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 186..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 212..214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT MUTAGEN 116
FT /note="H->Y: Loss of function."
FT /evidence="ECO:0000269|PubMed:11935028"
SQ SEQUENCE 247 AA; 27594 MW; A509E4132914E6AD CRC64;
MIYEKVAEEL ISSSYTIAFT GAGISTASGI PDFRGPQGLW KKYSPELASI EYFEKDPKNF
WGFYSLRMRG LFEAQPNKAH YSLAELEKMG IIKVIITQNI DGLHQKAGSK NVIELHGTMR
RSYCVLCLRT YDSLNVLSMI EKGNLPPRCD CGGIIRPDVV LFGEPVKNIY EALSIAYESD
LVISIGSSLT VYPANLIPQT VKERGGKLII LNMEETPLDS IADYVVREPV EISLPKILEN
VRQKILS
