ID   A0A2Z4FL65_9DELT        Unreviewed;       250 AA.
AC   A0A2Z4FL65;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE            EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN   ORFNames=DFR33_102137 {ECO:0000313|EMBL:TDP76506.1}, DN745_10520
GN   {ECO:0000313|EMBL:AWV89747.1};
OS   Bradymonas sediminis.
OC   Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae; Bradymonas.
OX   NCBI_TaxID=1548548 {ECO:0000313|EMBL:AWV89747.1, ECO:0000313|Proteomes:UP000249799};
RN   [1] {ECO:0000313|EMBL:AWV89747.1, ECO:0000313|Proteomes:UP000249799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FA350 {ECO:0000313|EMBL:AWV89747.1,
RC   ECO:0000313|Proteomes:UP000249799};
RA   Guo L.-Y., Li C.-M., Wang S., Du Z.-J.;
RT   "Lujinxingia sediminis gen. nov. sp. nov., a new facultative anaerobic
RT   member of the class Deltaproteobacteria, and proposal of Lujinxingaceae
RT   fam. nov.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TDP76506.1, ECO:0000313|Proteomes:UP000294609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28820 {ECO:0000313|EMBL:TDP76506.1,
RC   ECO:0000313|Proteomes:UP000294609};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP030032; AWV89747.1; -; Genomic_DNA.
DR   EMBL; SNXT01000002; TDP76506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4FL65; -.
DR   KEGG; bsed:DN745_10520; -.
DR   OrthoDB; 9800582at2; -.
DR   Proteomes; UP000249799; Chromosome.
DR   Proteomes; UP000294609; 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:UP000249799};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          1..250
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   ACT_SITE        127
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         135
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         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   250 AA;  27043 MW;  5314D47A4D325917 CRC64;
     MTTSKIATAA RWIRDADHIL VFCGSGLSAE SGVPTFRGED GLYNDSKLLE YAHVDALRDK
     PDEALTWFHK VVDMLEPLRP NAGHFALARI CQSRPCTIVT QNVDRLLEQA IAQSPGSNPP
     AKVWHLHGSL YKAKCMDCDA PLKTMPEDLL GARCPKCGGR LRPDVVLFGE ELPEAPYLQA
     QGAAHVADLV LLLGTSGIVN PAAMLPGLAR SHGAKLIEIN PNPTELSALA HLTLRGPTGE
     LLPAIEKRIR
//