ID A7HID4_ANADF Unreviewed; 289 AA.
AC A7HID4;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN OrderedLocusNames=Anae109_4302 {ECO:0000313|EMBL:ABS28480.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS28480.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS28480.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS28480.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000769; ABS28480.1; -; Genomic_DNA.
DR RefSeq; WP_012099124.1; NC_009675.1.
DR AlphaFoldDB; A7HID4; -.
DR STRING; 404589.Anae109_4302; -.
DR KEGG; afw:Anae109_4302; -.
DR eggNOG; COG0846; Bacteria.
DR HOGENOM; CLU_023643_2_0_7; -.
DR OrthoDB; 9800582at2; -.
DR Proteomes; UP000006382; 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: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:UP000006382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 1..275
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 270..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Proton acceptor"
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 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 289 AA; 31705 MW; 64242593CBF92A96 CRC64;
MRDTHAAAAA ALRSAGALVV TAGAGMGVDS GLPDFRGDQG FWKAYPPYER LGLSFVDAAN
PVHFERDAAF GWGFYGHRAR LYRETTPHAG FALLLRWSQR LGLPCFVVTS NVDGQFQKAG
FAEEQVLEVH GSIHHLQCTE PCCGTIWRNG EDVPVDEASM RARRIPRCIR CHGVARPNIL
MFGDGAWLSS RTEAQALRFE EWLAERGEER LVILELGAGT AVPTIRWHSE RLGARPGATL
VRVNPREPDV RPPHLSIPSG ALEALEGIDA SLDSAPPLTR GRDARDERP
//
