NPD2_PSEAE
ID NPD2_PSEAE Reviewed; 256 AA.
AC Q9I4E1;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=NAD-dependent protein deacylase 2;
DE EC=2.3.1.286;
DE AltName: Full=Regulatory protein SIR2 homolog 2;
GN Name=cobB2; OrderedLocusNames=PA1197;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC activities of several proteins which are inactive in their acetylated
CC form. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04586.1; -; Genomic_DNA.
DR PIR; A83495; A83495.
DR RefSeq; NP_249888.1; NC_002516.2.
DR RefSeq; WP_003112457.1; NZ_QZGE01000006.1.
DR AlphaFoldDB; Q9I4E1; -.
DR SMR; Q9I4E1; -.
DR STRING; 287.DR97_737; -.
DR PaxDb; Q9I4E1; -.
DR PRIDE; Q9I4E1; -.
DR EnsemblBacteria; AAG04586; AAG04586; PA1197.
DR GeneID; 879533; -.
DR KEGG; pae:PA1197; -.
DR PATRIC; fig|208964.12.peg.1243; -.
DR PseudoCAP; PA1197; -.
DR HOGENOM; CLU_023643_3_0_6; -.
DR InParanoid; Q9I4E1; -.
DR OMA; ERDCHGL; -.
DR PhylomeDB; Q9I4E1; -.
DR BioCyc; PAER208964:G1FZ6-1222-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0061697; F:protein-glutaryllysine deglutarylase activity; IBA:GO_Central.
DR GO; GO:0036054; F:protein-malonyllysine demalonylase activity; IBA:GO_Central.
DR GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0036047; P:peptidyl-lysine demalonylation; IBA:GO_Central.
DR GO; GO:0036049; P:peptidyl-lysine desuccinylation; IBA:GO_Central.
DR GO; GO:0061698; P:protein deglutarylation; IBA:GO_Central.
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; 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 2"
FT /id="PRO_0000110337"
FT DOMAIN 8..256
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 25..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 108..111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 199..201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 225..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 256 AA; 27687 MW; 6BE44DA7FE320563 CRC64;
MDSHSPIATV AQALRRAERI LVITGAGLSA DSGMPTYRGL GGLYNGRTEE GLPIEAALSG
PMLRRDPALC WKYLAELGKA CLAARPNAGH EAIAELQKHK PECWVLTQNI DGFHRQAGSP
AERLIEIHGE LAPLYCQSCG AESGGLEEHL HGQLPPRCAA CGGVLRPPVV LFEEMLPEEA
IDTLYRELRK GFDAVLVVGT TASFPYIVEP VLRTRQAGGF TAEVNPGVTD LSERVDVKMT
GRALDIMPQV VSHIYR
