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Database: UniProt
Entry: A0A1L7D0K8_9CORY
LinkDB: A0A1L7D0K8_9CORY
Original site: A0A1L7D0K8_9CORY 
ID   A0A1L7D0K8_9CORY        Unreviewed;       305 AA.
AC   A0A1L7D0K8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=NAD-dependent protein deacetylase {ECO:0000313|EMBL:APT91620.1};
GN   ORFNames=CPHO_00265 {ECO:0000313|EMBL:APT91620.1};
OS   Corynebacterium phocae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=161895 {ECO:0000313|EMBL:APT91620.1, ECO:0000313|Proteomes:UP000185491};
RN   [1] {ECO:0000313|EMBL:APT91620.1, ECO:0000313|Proteomes:UP000185491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M408/89/1 {ECO:0000313|EMBL:APT91620.1,
RC   ECO:0000313|Proteomes:UP000185491};
RA   Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT   44612(T)), isolated from the common seal (Phoca vitulina).";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP009249; APT91620.1; -; Genomic_DNA.
DR   RefSeq; WP_075732221.1; NZ_VXKJ01000053.1.
DR   AlphaFoldDB; A0A1L7D0K8; -.
DR   STRING; 161895.CPHO_00265; -.
DR   KEGG; cpho:CPHO_00265; -.
DR   OrthoDB; 9800582at2; -.
DR   Proteomes; UP000185491; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 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   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR11085:SF2; NAD-DEPENDENT PROTEIN LIPOAMIDASE SIRTUIN-4, MITOCHONDRIAL; 1.
DR   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00236}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185491};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          24..305
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   ACT_SITE        144
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   305 AA;  32668 MW;  C48894A899962722 CRC64;
     MDPAVKLAHE SALRSIARVV EETTPPTADA PTKVTRLIAQ GGVMVLTGAG VSTDSGVPDY
     RGPRGSLSRH RPMTYQEFSH DPAASHRYWA RSFVGWRVMN RAQPNRTHYA LVELERAGLV
     GGIVTQNVDG LHAQAGTGNL VTLHGNLDHV ACLDCGALES RPNLDARLEG LNPRFLERWA
     VADDQVNPDG DVDLTPAAVA QFVMAGCLNC GSKKLKPDVV YFGEPVPPAR RDAAFEMLDG
     SKSLLVAGSS LAVMSGYRFM LHALKTGKEV AVINGGPGRG DAKATYLWRT AVGPAFDYVL
     DELGL
//
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