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NPD2_BRADU
ID   NPD2_BRADU              Reviewed;         273 AA.
AC   Q89EA6;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=NAD-dependent protein deacetylase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01967};
GN   Name=cobB2 {ECO:0000255|HAMAP-Rule:MF_01967}; OrderedLocusNames=bll7181;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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=BAC52446.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000040; BAC52446.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_773821.2; NC_004463.1.
DR   RefSeq; WP_011089916.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89EA6; -.
DR   SMR; Q89EA6; -.
DR   STRING; 224911.27355463; -.
DR   EnsemblBacteria; BAC52446; BAC52446; BAC52446.
DR   GeneID; 64026939; -.
DR   KEGG; bja:bll7181; -.
DR   PATRIC; fig|224911.44.peg.7248; -.
DR   eggNOG; COG0846; Bacteria.
DR   HOGENOM; CLU_023643_3_2_5; -.
DR   InParanoid; Q89EA6; -.
DR   OMA; RRHYWAR; -.
DR   PhylomeDB; Q89EA6; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..273
FT                   /note="NAD-dependent protein deacetylase 2"
FT                   /id="PRO_0000110300"
FT   DOMAIN          9..273
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   ACT_SITE        122
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         26..46
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         104..107
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         221..223
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         247..249
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
FT   BINDING         265
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01967"
SQ   SEQUENCE   273 AA;  30141 MW;  68398C61D327D079 CRC64;
     MSNAPLANQS LQDFVARHQR LFVLTGAGCS TNSGIPDYRD SHGNWKRTQP VNFQAFMSEE
     HTRRRYWARS LIGWRRFGQA RPNDAHHALA RLEANGRCGM LLTQNVDRLH QSAGHRQVID
     LHGRLDLVRC MGCGAKTPRS EFQDTLGRAN AEWLALDASD APDGDADLEH ADFSSFKVPA
     CEACGGILKP DVVFFGENVP RDVVATAQDH LSQADAMLIV GSSLMVYSGF RFVQAAAQRQ
     IPIAAVNLGR TRADDLLTLK VEERCEAALA FLL
 
 
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