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Database: UniProt
Entry: A0A2N1F7K3_9FLAO
LinkDB: A0A2N1F7K3_9FLAO
Original site: A0A2N1F7K3_9FLAO 
ID   A0A2N1F7K3_9FLAO        Unreviewed;       277 AA.
AC   A0A2N1F7K3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE            EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN   ORFNames=CXF68_09440 {ECO:0000313|EMBL:PKH50896.1};
OS   Tenacibaculum sp. Bg11-29.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=2058306 {ECO:0000313|EMBL:PKH50896.1, ECO:0000313|Proteomes:UP000233844};
RN   [1] {ECO:0000313|EMBL:PKH50896.1, ECO:0000313|Proteomes:UP000233844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bg11-29 {ECO:0000313|EMBL:PKH50896.1,
RC   ECO:0000313|Proteomes:UP000233844};
RA   Collins E., Ducluzeau A.-L.;
RT   "Pharmacopeia of the Arctic Ocean.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKH50896.1}.
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DR   EMBL; PJBB01000003; PKH50896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N1F7K3; -.
DR   OrthoDB; 9800582at2; -.
DR   Proteomes; UP000233844; Unassembled WGS sequence.
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:SF12; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 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|PROSITE-ProRule:PRU00236};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233844};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          1..276
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   ACT_SITE        126
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   277 AA;  32247 MW;  7EE5368040D13193 CRC64;
     MDKLNNIIEE VLLKEKRNKF TFLTGAGISA DSGIPTYRGS DGIWVKGTKF HKPEEFGTYK
     YFTEHQEEVW QYTLFRKKMI ESAKPNKSHK ILADLEKILN DRFHLITQNI DNLHRRAGNE
     NIYEIHGNYR EVKCSKICNK IIPIPNNITG KDIKEELRKD EINALKCTEC GNWLRPNILW
     FDEYYNEKTN KRFSSLKIAK NSGILFIVGT SGATNLPLEI ARTTLKYGGY VIDLNIEDNH
     FTELLKNKKR ALIVRERSSE ILPIIKEQIE KNLKKTI
//
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