HST2_YEAST
ID HST2_YEAST Reviewed; 357 AA.
AC P53686; D6W3Z7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=NAD-dependent protein deacetylase HST2;
DE EC=2.3.1.286;
DE AltName: Full=Homologous to SIR2 protein 2;
DE AltName: Full=Regulatory protein SIR2 homolog 2;
GN Name=HST2; OrderedLocusNames=YPL015C; ORFNames=LPA2C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / YPH1;
RX PubMed=7498786; DOI=10.1101/gad.9.23.2888;
RA Brachmann C.B., Sherman J.M., Devine S.E., Cameron E.E., Pillus L.,
RA Boeke J.D.;
RT "The SIR2 gene family, conserved from bacteria to humans, functions in
RT silencing, cell cycle progression, and chromosome stability.";
RL Genes Dev. 9:2888-2902(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=10811920; DOI=10.1073/pnas.110148297;
RA Landry J., Sutton A., Tafrov S.T., Heller R.C., Stebbins J., Pillus L.,
RA Sternglanz R.;
RT "The silencing protein SIR2 and its homologs are NAD-dependent protein
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5807-5811(2000).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11106374; DOI=10.1073/pnas.250422697;
RA Tanner K.G., Landry J., Sternglanz R., Denu J.M.;
RT "Silent information regulator 2 family of NAD- dependent histone/protein
RT deacetylases generates a unique product, 1-O-acetyl-ADP-ribose.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14178-14182(2000).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11226170; DOI=10.1093/emboj/20.1.197;
RA Perrod S., Cockell M.M., Laroche T., Renauld H., Ducrest A.L., Bonnard C.,
RA Gasser S.M.;
RT "A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and
RT telomeric silencing in yeast.";
RL EMBO J. 20:197-209(2001).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15274642; DOI=10.1021/bi049592e;
RA Borra M.T., Langer M.R., Slama J.T., Denu J.M.;
RT "Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-
RT dependent histone/protein deacetylases.";
RL Biochemistry 43:9877-9887(2004).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17110954; DOI=10.1038/sj.embor.7400829;
RA Wilson J.M., Le V.Q., Zimmerman C., Marmorstein R., Pillus L.;
RT "Nuclear export modulates the cytoplasmic Sir2 homologue Hst2.";
RL EMBO Rep. 7:1247-1251(2006).
RN [12]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16520376; DOI=10.1074/jbc.m511482200;
RA Khan A.N., Lewis P.N.;
RT "Use of substrate analogs and mutagenesis to study substrate binding and
RT catalysis in the Sir2 family of NAD-dependent protein deacetylases.";
RL J. Biol. Chem. 281:11702-11711(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP ACTIVE SITE.
RX PubMed=20726530; DOI=10.1021/jp1054183;
RA Liang Z., Shi T., Ouyang S., Li H., Yu K., Zhu W., Luo C., Jiang H.;
RT "Investigation of the catalytic mechanism of Sir2 enzyme with QM/MM
RT approach: SN1 vs SN2?";
RL J. Phys. Chem. B 114:11927-11933(2010).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PEPTIDE SUBSTRATE;
RP ZINC AND NAD.
RX PubMed=14502267; DOI=10.1038/nsb978;
RA Zhao K., Chai X., Clements A., Marmorstein R.;
RT "Structure and autoregulation of the yeast Hst2 homolog of Sir2.";
RL Nat. Struct. Biol. 10:864-871(2003).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 5-293 IN COMPLEX WITH SUBSTRATE
RP ANALOG; PEPTIDE SUBSTRATE AND ZINC, AND SUBUNIT.
RX PubMed=14604530; DOI=10.1016/j.str.2003.09.016;
RA Zhao K., Chai X., Marmorstein R.;
RT "Structure of the yeast Hst2 protein deacetylase in ternary complex with
RT 2'-O-acetyl ADP ribose and histone peptide.";
RL Structure 11:1403-1411(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-294 IN COMPLEX WITH PEPTIDE
RP SUBSTRATE; ZINC AND NAD.
RX PubMed=15150415; DOI=10.1073/pnas.0401057101;
RA Zhao K., Harshaw R., Chai X., Marmorstein R.;
RT "Structural basis for nicotinamide cleavage and ADP-ribose transfer by
RT NAD(+)-dependent Sir2 histone/protein deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8563-8568(2004).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-294 IN COMPLEX WITH PEPTIDE
RP SUBSTRATE; NICOTINAMIDE AND ZINC, MUTAGENESIS OF 117, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17289592; DOI=10.1016/j.molcel.2006.12.022;
RA Sanders B.D., Zhao K., Slama J.T., Marmorstein R.;
RT "Structural basis for nicotinamide inhibition and base exchange in Sir2
RT enzymes.";
RL Mol. Cell 25:463-472(2007).
CC -!- FUNCTION: NAD-dependent histone deacetylase that is involved in nuclear
CC silencing events. Derepresses subtelomeric silencing and increases
CC repression in nucleolar (rDNA) silencing. Its function is negatively
CC regulated by active nuclear export. {ECO:0000269|PubMed:10811920,
CC ECO:0000269|PubMed:11106374, ECO:0000269|PubMed:11226170,
CC ECO:0000269|PubMed:15274642, ECO:0000269|PubMed:17110954}.
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|PROSITE-ProRule:PRU00236,
CC ECO:0000269|PubMed:16520376};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by ADP-ribose and nicotinamide.
CC {ECO:0000269|PubMed:16520376}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.2 uM for NAD(+) {ECO:0000269|PubMed:11106374,
CC ECO:0000269|PubMed:15274642, ECO:0000269|PubMed:16520376,
CC ECO:0000269|PubMed:17289592};
CC KM=0.92 uM for acetylated poly-L-lysine {ECO:0000269|PubMed:11106374,
CC ECO:0000269|PubMed:15274642, ECO:0000269|PubMed:16520376,
CC ECO:0000269|PubMed:17289592};
CC KM=0.5 uM for a synthetic histone H3K14 acetyllysine peptide
CC {ECO:0000269|PubMed:11106374, ECO:0000269|PubMed:15274642,
CC ECO:0000269|PubMed:16520376, ECO:0000269|PubMed:17289592};
CC -!- SUBUNIT: Homotrimer. Monomer. Homotrimeric in its unliganded state.
CC Undergoes a trimer-monomer transition upon acetyl-lysine substrate
CC binding. {ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530,
CC ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC nucleus and cytoplasm, but is largely cytoplasmic owing to efficient
CC nuclear export. Nuclear exclusion is mediated by the exportin CRM1.
CC -!- MISCELLANEOUS: Present with 5260 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
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DR EMBL; U39063; AAA81035.1; -; Genomic_DNA.
DR EMBL; U33335; AAB68090.1; -; Genomic_DNA.
DR EMBL; AY693204; AAT93223.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11413.1; -; Genomic_DNA.
DR PIR; S59678; S59678.
DR RefSeq; NP_015310.1; NM_001183829.1.
DR PDB; 1Q14; X-ray; 2.50 A; A=1-357.
DR PDB; 1Q17; X-ray; 2.70 A; A/B/C=1-294.
DR PDB; 1Q1A; X-ray; 1.50 A; A=5-293.
DR PDB; 1SZC; X-ray; 1.75 A; A=1-294.
DR PDB; 1SZD; X-ray; 1.50 A; A=1-294.
DR PDB; 2OD2; X-ray; 2.00 A; A=1-294.
DR PDB; 2OD7; X-ray; 2.00 A; A=1-294.
DR PDB; 2OD9; X-ray; 2.05 A; A=1-294.
DR PDB; 2QQF; X-ray; 2.00 A; A=1-294.
DR PDB; 2QQG; X-ray; 2.05 A; A=1-294.
DR PDB; 7F4E; X-ray; 1.78 A; A=8-294.
DR PDB; 7F51; X-ray; 1.98 A; A=8-294.
DR PDBsum; 1Q14; -.
DR PDBsum; 1Q17; -.
DR PDBsum; 1Q1A; -.
DR PDBsum; 1SZC; -.
DR PDBsum; 1SZD; -.
DR PDBsum; 2OD2; -.
DR PDBsum; 2OD7; -.
DR PDBsum; 2OD9; -.
DR PDBsum; 2QQF; -.
DR PDBsum; 2QQG; -.
DR PDBsum; 7F4E; -.
DR PDBsum; 7F51; -.
DR AlphaFoldDB; P53686; -.
DR SMR; P53686; -.
DR BioGRID; 36162; 53.
DR IntAct; P53686; 3.
DR MINT; P53686; -.
DR STRING; 4932.YPL015C; -.
DR BindingDB; P53686; -.
DR ChEMBL; CHEMBL5933; -.
DR DrugCentral; P53686; -.
DR iPTMnet; P53686; -.
DR MaxQB; P53686; -.
DR PaxDb; P53686; -.
DR PRIDE; P53686; -.
DR EnsemblFungi; YPL015C_mRNA; YPL015C; YPL015C.
DR GeneID; 856092; -.
DR KEGG; sce:YPL015C; -.
DR SGD; S000005936; HST2.
DR VEuPathDB; FungiDB:YPL015C; -.
DR eggNOG; KOG2682; Eukaryota.
DR GeneTree; ENSGT00940000157514; -.
DR HOGENOM; CLU_023643_7_2_1; -.
DR InParanoid; P53686; -.
DR OMA; FNMEKVG; -.
DR BioCyc; YEAST:G3O-33934-MON; -.
DR BRENDA; 2.3.1.286; 984.
DR SABIO-RK; P53686; -.
DR EvolutionaryTrace; P53686; -.
DR PRO; PR:P53686; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P53686; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IDA:SGD.
DR GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070933; P:histone H4 deacetylation; IDA:UniProtKB.
DR GO; GO:0045950; P:negative regulation of mitotic recombination; IMP:SGD.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR Gene3D; 3.30.1600.10; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR017328; Sirtuin_class_I.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR PIRSF; PIRSF037938; SIR2_euk; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Metal-binding; NAD; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..357
FT /note="NAD-dependent protein deacetylase HST2"
FT /id="PRO_0000110282"
FT DOMAIN 13..286
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 317..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236,
FT ECO:0000269|PubMed:20726530"
FT BINDING 32..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14502267,
FT ECO:0000269|PubMed:15150415"
FT BINDING 115..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14502267,
FT ECO:0000269|PubMed:15150415"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236,
FT ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530,
FT ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236,
FT ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530,
FT ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236,
FT ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530,
FT ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236,
FT ECO:0000269|PubMed:14502267, ECO:0000269|PubMed:14604530,
FT ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592"
FT BINDING 223..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14502267,
FT ECO:0000269|PubMed:15150415"
FT BINDING 248..250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14502267,
FT ECO:0000269|PubMed:15150415"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:14502267,
FT ECO:0000269|PubMed:15150415"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 117
FT /note="I->A,D,H,W,Y: Nearly or completely catalytically
FT inactive."
FT /evidence="ECO:0000269|PubMed:17289592"
FT MUTAGEN 117
FT /note="I->F,V: Near wild-type activity for deacetylation.
FT Increases slightly the KM for NAD(+) to 25 uM."
FT /evidence="ECO:0000269|PubMed:17289592"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1SZD"
FT HELIX 9..21
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1Q1A"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:1Q1A"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1SZD"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1Q1A"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:1Q1A"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:1Q1A"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:1Q14"
SQ SEQUENCE 357 AA; 39979 MW; ED281E5B8241A4D0 CRC64;
MSVSTASTEM SVRKIAAHMK SNPNAKVIFM VGAGISTSCG IPDFRSPGTG LYHNLARLKL
PYPEAVFDVD FFQSDPLPFY TLAKELYPGN FRPSKFHYLL KLFQDKDVLK RVYTQNIDTL
ERQAGVKDDL IIEAHGSFAH CHCIGCGKVY PPQVFKSKLA EHPIKDFVKC DVCGELVKPA
IVFFGEDLPD SFSETWLNDS EWLREKITTS GKHPQQPLVI VVGTSLAVYP FASLPEEIPR
KVKRVLCNLE TVGDFKANKR PTDLIVHQYS DEFAEQLVEE LGWQEDFEKI LTAQGGMGDN
SKEQLLEIVH DLENLSLDQS EHESADKKDK KLQRLNGHDS DEDGASNSSS SQKAAKE
