(data stored in ACNUC1104 zone)

SWISSPROT: A1SDC5_NOCSJ

ID   A1SDC5_NOCSJ            Unreviewed;       232 AA.
AC   A1SDC5;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 87.
DE   RecName: Full=NAD-dependent protein deacylase {ECO:0000256|HAMAP-Rule:MF_01121};
DE            EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_01121};
DE   AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01121};
GN   Name=cobB {ECO:0000256|HAMAP-Rule:MF_01121};
GN   OrderedLocusNames=Noca_0265 {ECO:0000313|EMBL:ABL79810.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79810.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL79810.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- FUNCTION: NAD-dependent lysine deacetylase and desuccinylase that
CC       specifically removes acetyl and succinyl groups on target
CC       proteins. Modulates the activities of several proteins which are
CC       inactive in their acylated form. {ECO:0000256|HAMAP-
CC       Rule:MF_01121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC         acetyl-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         Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01121};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01121};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01121};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01121}.
CC   -!- DOMAIN: 2 residues (Tyr-54 and Arg-57) present in a large
CC       hydrophobic pocket are probably involved in substrate specificity.
CC       They are important for desuccinylation activity, but dispensable
CC       for deacetylation activity. {ECO:0000256|HAMAP-Rule:MF_01121}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class III subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01121}.
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DR   EMBL; CP000509; ABL79810.1; -; Genomic_DNA.
DR   RefSeq; WP_011753761.1; NC_008699.1.
DR   STRING; 196162.Noca_0265; -.
DR   EnsemblBacteria; ABL79810; ABL79810; Noca_0265.
DR   KEGG; nca:Noca_0265; -.
DR   eggNOG; ENOG4105NDF; Bacteria.
DR   eggNOG; COG0846; LUCA.
DR   HOGENOM; HOG000085950; -.
DR   KO; K12410; -.
DR   OMA; SMQVYPA; -.
DR   OrthoDB; 1264438at2; -.
DR   Proteomes; UP000000640; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01412; SIRT5_Af1_CobB; 1.
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;
DR   PRODOM; A1SDC5.
DR   SWISS-2DPAGE; A1SDC5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01121};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01121};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01121};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01121};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   DOMAIN        1    232       Deacetylase sirtuin-type.
FT                                {ECO:0000259|PROSITE:PS50305}.
FT   NP_BIND      10     29       NAD. {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   NP_BIND      89     92       NAD. {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   NP_BIND     173    175       NAD. {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   NP_BIND     199    201       NAD. {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   ACT_SITE    107    107       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01121}.
FT   METAL       115    115       Zinc. {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   METAL       118    118       Zinc. {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   METAL       134    134       Zinc. {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   METAL       137    137       Zinc. {ECO:0000256|HAMAP-Rule:MF_01121}.
FT   BINDING      54     54       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01121}.
FT   BINDING      57     57       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01121}.
FT   BINDING     217    217       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01121}.
SQ   SEQUENCE   232 AA;  25208 MW;  2015EA80AE0BEB6E CRC64;
     MVVRIVVLTG AGISAESGLP TFRDADGLWH GHRVEEVATP EAFERVPALV HRFYDERRAA
     LATVRPNAAH EALARLEQAL GDDLLVVTQN IDDLHERSGS RQVLHMHGRL RSALCGSCAG
     HFDWVGDLGD APPCPRCGRR ELRPDVVWFG EAPYDMDRIL GAVGRADLFV SVGTSGAVYP
     AAGFVQYAAG QGARTLELNL VPSEGSHLFD ESRHGPASRL VPEWVAEIFD TP
//

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