位置:首页 > 蛋白库 > NPD4_PSESM
NPD4_PSESM
ID   NPD4_PSESM              Reviewed;         256 AA.
AC   Q87W79;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=NAD-dependent protein deacylase 4 {ECO:0000255|HAMAP-Rule:MF_01121};
DE            EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_01121};
DE   AltName: Full=Regulatory protein SIR2 homolog 4 {ECO:0000255|HAMAP-Rule:MF_01121};
GN   Name=cobB4 {ECO:0000255|HAMAP-Rule:MF_01121}; OrderedLocusNames=PSPTO_4675;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC   -!- FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that
CC       specifically removes acetyl and succinyl groups on target proteins.
CC       Modulates the activities of several proteins which are inactive in
CC       their acylated form. {ECO:0000255|HAMAP-Rule:MF_01121}.
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_01121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC         succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC         Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01121};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01121};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01121};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01121}.
CC   -!- DOMAIN: 2 residues (Tyr-64 and Arg-67) present in a large hydrophobic
CC       pocket are probably involved in substrate specificity. They are
CC       important for desuccinylation activity, but dispensable for
CC       deacetylation activity. {ECO:0000255|HAMAP-Rule:MF_01121}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01121}.
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; AE016853; AAO58121.1; -; Genomic_DNA.
DR   RefSeq; NP_794426.1; NC_004578.1.
DR   AlphaFoldDB; Q87W79; -.
DR   SMR; Q87W79; -.
DR   STRING; 223283.PSPTO_4675; -.
DR   EnsemblBacteria; AAO58121; AAO58121; PSPTO_4675.
DR   KEGG; pst:PSPTO_4675; -.
DR   PATRIC; fig|223283.9.peg.4793; -.
DR   eggNOG; COG0846; Bacteria.
DR   HOGENOM; CLU_023643_3_1_6; -.
DR   OMA; SMQVYPA; -.
DR   OrthoDB; 1264438at2; -.
DR   PhylomeDB; Q87W79; -.
DR   Proteomes; UP000002515; 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:0036054; F:protein-malonyllysine demalonylase activity; IEA:InterPro.
DR   GO; GO:0036055; F:protein-succinyllysine desuccinylase 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_01121; Sirtuin_ClassIII; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
DR   InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR   InterPro; IPR027546; Sirtuin_class_III.
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..256
FT                   /note="NAD-dependent protein deacylase 4"
FT                   /id="PRO_0000110342"
FT   DOMAIN          2..252
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   ACT_SITE        116
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         19..39
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         98..101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         192..194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         218..220
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT   BINDING         236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
SQ   SEQUENCE   256 AA;  27820 MW;  63058F58ED405AAE CRC64;
     MRLPAEALKD ARKIVCFSGA GISAESGILT YLDQMPKLWA PYDPRALETA NAFRESPALV
     WGWYLWRRRQ VDRAQPNAAH LVWPQMVNLG YEVSVVTQNV DDLHERAGST DVIHLHGSLT
     MPKCFACHRP AELTSDQMEI PDEGALVEPP RCKRCRGKLR PGVVWYGEDL PPGTWKNAVS
     LVKNCDALIS VGTSGVVTPA ADLPHIALAS GATVIHVNTV DVGAQAANEL MLVGRATDVL
     AKIHESLSTG KNNDNG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024