位置:首页 > 蛋白库 > NPD1_COREF
NPD1_COREF
ID   NPD1_COREF              Reviewed;         281 AA.
AC   Q8FUC8;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=NAD-dependent protein deacetylase 1 {ECO:0000255|HAMAP-Rule:MF_01967};
DE            EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_01967};
DE   AltName: Full=Regulatory protein SIR2 homolog 1 {ECO:0000255|HAMAP-Rule:MF_01967};
GN   Name=cobB1 {ECO:0000255|HAMAP-Rule:MF_01967}; OrderedLocusNames=CE0092;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC       activities of several enzymes which are inactive in their acetylated
CC       form. {ECO:0000255|HAMAP-Rule:MF_01967}.
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_01967};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01967};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01967};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01967}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01967}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC16902.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000035; BAC16902.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8FUC8; -.
DR   SMR; Q8FUC8; -.
DR   STRING; 196164.23491927; -.
DR   EnsemblBacteria; BAC16902; BAC16902; BAC16902.
DR   KEGG; cef:CE0092; -.
DR   eggNOG; COG0846; Bacteria.
DR   HOGENOM; CLU_023643_3_2_11; -.
DR   Proteomes; UP000001409; 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: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_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;
KW   Cytoplasm; Metal-binding; NAD; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..281
FT                   /note="NAD-dependent protein deacetylase 1"
FT                   /id="PRO_0000110308"
FT   DOMAIN          1..281
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   ACT_SITE        120
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         24..44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         102..105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         224..226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         250..252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         268
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
SQ   SEQUENCE   281 AA;  30298 MW;  7EF99C2DE0012680 CRC64;
     MEEGAALEGV VKLLEAGSVL AVTGAGVSTD SGIPDYRSPR GSLNQGRPMT YQEFRFDPVA
     SHRYWARSFV GWRVMADAQP NRTHYALVEL ERAGLLSGIV TQNVDGLHRR AGSENLVALH
     GDLATIVCLQ CGHREARELL DARLDHLNPG YFDSIALDPS AVNPDGDVTL DDHHVQRFTM
     AGCARCGSVL LKPDVVYFGE PVPSIRKTRV AQLLDGADAV VVAGSSLAVM SGYRIVIEAQ
     RAGKPVAVIN GGPGRADHRV DILWRTRVGP AFDQILDALD L
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024