(data stored in ACNUC6288 zone)

SWISSPROT: Q6BM81_DEBHA

ID   Q6BM81_DEBHA            Unreviewed;       354 AA.
AC   Q6BM81;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 94.
DE   RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|PIRNR:PIRNR037938};
DE            EC=3.5.1.- {ECO:0000256|PIRNR:PIRNR037938};
GN   OrderedLocusNames=DEHA2F07656g {ECO:0000313|EMBL:CAG89029.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89029.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89029.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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|PIRNR:PIRNR037938};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR037938};
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC       {ECO:0000256|PIRNR:PIRNR037938}.
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DR   EMBL; CR382138; CAG89029.2; -; Genomic_DNA.
DR   RefSeq; XP_460690.2; XM_460690.1.
DR   STRING; 4959.XP_460690.2; -.
DR   EnsemblFungi; CAG89029; CAG89029; DEHA2F07656g.
DR   GeneID; 2903492; -.
DR   KEGG; dha:DEHA2F07656g; -.
DR   HOGENOM; HOG000085952; -.
DR   InParanoid; Q6BM81; -.
DR   KO; K11121; -.
DR   OMA; EYDMAWM; -.
DR   OrthoDB; 973532at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; Q6BM81.
DR   SWISS-2DPAGE; Q6BM81.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037938};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR037938,
KW   ECO:0000256|PIRSR:PIRSR037938-3};
KW   NAD {ECO:0000256|PIRNR:PIRNR037938, ECO:0000256|PIRSR:PIRSR037938-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Zinc {ECO:0000256|PIRNR:PIRNR037938, ECO:0000256|PIRSR:PIRSR037938-3}.
FT   DOMAIN        9    269       Deacetylase sirtuin-type.
FT                                {ECO:0000259|PROSITE:PS50305}.
FT   NP_BIND      28     32       NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
FT   NP_BIND      38     40       NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
FT   NP_BIND     110    113       NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
FT   NP_BIND     207    208       NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
FT   NP_BIND     231    233       NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
FT   COILED      298    318       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    130    130       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR037938-1}.
FT   METAL       138    138       Zinc. {ECO:0000256|PIRSR:PIRSR037938-3}.
FT   METAL       141    141       Zinc. {ECO:0000256|PIRSR:PIRSR037938-3}.
FT   METAL       166    166       Zinc. {ECO:0000256|PIRSR:PIRSR037938-3}.
FT   METAL       169    169       Zinc. {ECO:0000256|PIRSR:PIRSR037938-3}.
FT   BINDING     253    253       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR037938-2}.
SQ   SEQUENCE   354 AA;  39816 MW;  1BC9EDA67BC92DC4 CRC64;
     MNQLTKILEP IAKAIQAGDK KVTFFEGAGI STAAGIPDFR SPDTGLYSNL AKLDLPYAEA
     VFDIDYFKEN PKAFYTLAHE LYPGKFMPTK FHYLLRLFQD KKLLKRVYTQ NIDTLERVAG
     IEDEYIVEAH GSFARNHCIE CSLEMSTEEL KKQMSDKSVN DGIPICQECG GYVKPDIVFF
     GEALPVKFFD TWDEDADEVE IAIVAGTSLT VYPFASLPSE TTKKSLRLLI NNEVVGDFKH
     GKRKTDILAI SDCDEAAVTL AELLGWSEEL DELINKNKTL FESTYSIGEK TNDEEVSKKS
     LSKASERLAE EIRDVEAEKG TQKPEKTDKQ TESKEEKSKN DTDDLEKDIS NLKI
//

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