ID A0A1G1P5P1_9BACT Unreviewed; 254 AA.
AC A0A1G1P5P1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN ORFNames=A3D87_09295 {ECO:0000313|EMBL:OGX37205.1};
OS Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_50_17.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801857 {ECO:0000313|EMBL:OGX37205.1, ECO:0000313|Proteomes:UP000177986};
RN [1] {ECO:0000313|EMBL:OGX37205.1, ECO:0000313|Proteomes:UP000177986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGX37205.1}.
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DR EMBL; MHGQ01000060; OGX37205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1P5P1; -.
DR STRING; 1801857.A3D87_09295; -.
DR Proteomes; UP000177986; 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 CDD; cd01407; SIR2-fam; 1.
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 Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 1..253
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 254 AA; 28251 MW; F5B2F945335396F0 CRC64;
MNDSVSQCAR LIQESRYIAA LTGAGISTSA GIPDFRGPQG LYVTRRYDPD TVFDINYFYH
DPKPFYEFAR DFLLLEEKIN PTFAHKFLSD LEKTGNLKGV VTQNIDSLHQ RAGSQKVYEM
HGSFSLSHCL KCRKEFSFTQ MKEKLAEEDI PRCACPASCG ACGGVLKPDI VFFGENVKCL
AESEDLAARS DLFFVIGTSC VVYPAAMIPQ YVQGKIVVVN QDPVSLDAGN VVLTVREDID
AFFARVAEQL GYRI
//
