(data stored in SCRATCH zone)

SWISSPROT: B1VNS5_STRGG

ID   B1VNS5_STRGG            Unreviewed;       296 AA.
AC   B1VNS5;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 63.
DE   RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|HAMAP-Rule:MF_01967};
DE            EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_01967};
DE   AltName: Full=Regulatory protein SIR2 homolog {ECO:0000256|HAMAP-Rule:MF_01967};
GN   Name=cobB {ECO:0000256|HAMAP-Rule:MF_01967};
GN   OrderedLocusNames=SGR_269 {ECO:0000313|EMBL:BAG17098.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17098.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17098.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC       activities of several enzymes which are inactive in their
CC       acetylated form. {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
CC       acetyl-ADP-ribose + a protein. {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01967};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01967};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01967}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01967}.
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DR   EMBL; AP009493; BAG17098.1; -; Genomic_DNA.
DR   RefSeq; WP_012377663.1; NC_010572.1.
DR   ProteinModelPortal; B1VNS5; -.
DR   STRING; 455632.SGR_269; -.
DR   EnsemblBacteria; BAG17098; BAG17098; SGR_269.
DR   GeneID; 6208972; -.
DR   KEGG; sgr:SGR_269; -.
DR   PATRIC; fig|455632.4.peg.248; -.
DR   eggNOG; ENOG4105NDF; Bacteria.
DR   eggNOG; COG0846; LUCA.
DR   HOGENOM; HOG000085953; -.
DR   OMA; ARQRYWA; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   HAMAP; MF_01967; Sirtuin_ClassII; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR003000; Sirtuin.
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;
DR   PRODOM; B1VNS5.
DR   SWISS-2DPAGE; B1VNS5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01967};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01967};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01967};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01967};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   DOMAIN       20    294       Deacetylase sirtuin-type.
FT                                {ECO:0000259|PROSITE:PS50305}.
FT   NP_BIND      39     59       NAD. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   NP_BIND     117    120       NAD. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   NP_BIND     234    236       NAD. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   ACT_SITE    135    135       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01967}.
FT   METAL       143    143       Zinc. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   METAL       146    146       Zinc. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   METAL       194    194       Zinc. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   METAL       197    197       Zinc. {ECO:0000256|HAMAP-Rule:MF_01967}.
FT   BINDING     278    278       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01967}.
SQ   SEQUENCE   296 AA;  31435 MW;  BDECA6EB77E2E41E CRC64;
     MRMRPTLSWT SAEEPLPGTT DLEPVVEALR GGGVLVLSGA GISTESGIPD YRGEGGSLSR
     HTPMTYQDFT ADAGARRRYW ARSHLGWRTF GRARPNAGHR AVAAFGRRGL LSGVITQNVD
     GLHQAAGSAD VVDLHGRLDR VVCLSCGAFG PRSELARRLE EANEGFAPVA AAMNPDGDAD
     LTDEQVGDFR VVPCAVCGGV LKPDVVFFGE SVPPRRVEHC RALVDAASAL LVLGSSLTVM
     SGLRFVRQAE RSGLPVLIVN RDPTRGDRHA LPRIALPLGD ALTTAAGRLG VRVDDD
//

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