NPD_CAMJE
ID NPD_CAMJE Reviewed; 233 AA.
AC Q9JN05; Q0P9K2; Q9PNP1;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=NAD-dependent protein deacylase {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 {ECO:0000255|HAMAP-Rule:MF_01121};
GN Name=cobB {ECO:0000255|HAMAP-Rule:MF_01121}; OrderedLocusNames=Cj1050c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-227.
RC STRAIN=P37;
RX PubMed=7607469; DOI=10.1016/0378-1119(94)00668-i;
RA Vitor J.M., Morgan R.D.;
RT "Two novel restriction endonucleases from Campylobacter jejuni.";
RL Gene 157:109-110(1995).
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-53 and Arg-56) 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}.
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DR EMBL; AL111168; CAL35168.1; -; Genomic_DNA.
DR EMBL; AF264911; AAF77189.1; -; Genomic_DNA.
DR PIR; G81307; G81307.
DR RefSeq; WP_002864286.1; NC_002163.1.
DR RefSeq; YP_002344445.1; NC_002163.1.
DR AlphaFoldDB; Q9JN05; -.
DR SMR; Q9JN05; -.
DR IntAct; Q9JN05; 2.
DR STRING; 192222.Cj1050c; -.
DR PaxDb; Q9JN05; -.
DR PRIDE; Q9JN05; -.
DR EnsemblBacteria; CAL35168; CAL35168; Cj1050c.
DR GeneID; 905342; -.
DR KEGG; cje:Cj1050c; -.
DR PATRIC; fig|192222.6.peg.1032; -.
DR eggNOG; COG0846; Bacteria.
DR HOGENOM; CLU_023643_3_1_7; -.
DR OMA; YRIEEIC; -.
DR Proteomes; UP000000799; 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: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: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..233
FT /note="NAD-dependent protein deacylase"
FT /id="PRO_0000110301"
FT DOMAIN 1..233
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 9..28
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 88..91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 172..174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT BINDING 200..202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01121"
FT CONFLICT 10..11
FT /note="AG -> RD (in Ref. 1; AAF77189)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="F -> I (in Ref. 1; AAF77189)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="H -> N (in Ref. 1; AAF77189)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="I -> V (in Ref. 1; AAF77189)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..184
FT /note="QYA -> RYP (in Ref. 1; AAF77189)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> A (in Ref. 1; AAF77189)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..204
FT /note="RY -> WN (in Ref. 1; AAF77189)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="F -> L (in Ref. 1; AAF77189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 233 AA; 26521 MW; AEB7F5880A2A832B CRC64;
MKNIMILSGA GLSAPSGLKT FRDNDGLWEE YDVMEVCSAT GFRKNPKKVL DFYDARRAQL
QNVKPNHAHE KIAQLKEKWG KNLFVITQNV DDLLERAGCK DVVHLHGFLP ELRCLKCEGI
FNIGYEKFTD KQCPKCKSKD LRHNIVMFEE QAPAYATLYS LLHQTSLFIS IGTSGAVLPV
GQYASMCEKS ILNIYEKDVN LERYFDKIYI EDIISAIDKI ALDIENFMKD GNV
