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Database: UniProt
Entry: A4J2H5_DESRM
LinkDB: A4J2H5_DESRM
Original site: A4J2H5_DESRM 
ID   A4J2H5_DESRM            Unreviewed;       282 AA.
AC   A4J2H5;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Beta-lysine acetyltransferase {ECO:0000313|EMBL:ABO49278.1};
DE            EC=2.3.1.- {ECO:0000313|EMBL:ABO49278.1};
GN   OrderedLocusNames=Dred_0739 {ECO:0000313|EMBL:ABO49278.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO49278.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO49278.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO49278.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000612; ABO49278.1; -; Genomic_DNA.
DR   RefSeq; WP_011877114.1; NC_009253.1.
DR   AlphaFoldDB; A4J2H5; -.
DR   STRING; 349161.Dred_0739; -.
DR   KEGG; drm:Dred_0739; -.
DR   eggNOG; COG0456; Bacteria.
DR   HOGENOM; CLU_081246_0_0_9; -.
DR   OMA; SYGMNIT; -.
DR   OrthoDB; 9790652at2; -.
DR   Proteomes; UP000001556; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR022525; GNAT_AblB.
DR   InterPro; IPR000182; GNAT_dom.
DR   NCBIfam; TIGR03827; GNAT_ablB; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:ABO49278.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW   Transferase {ECO:0000313|EMBL:ABO49278.1}.
FT   DOMAIN          129..278
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   282 AA;  32202 MW;  E3F7F78B023BE5D4 CRC64;
     MQTIITTRSE FSLTTQLDMF NRRIWVQDYK VNDATALRCF LLDLAKKQNL EKIIFPVKEA
     DLPLLQGEEF QLEGVINGYF QGSNAYFLTT YLSEKRCNSS SLLREKQMLE KILGQPREYK
     LALPKKYSLE IATSRHAKKM AELFKIVFKS YPTPVYDPKY LNEAIQKGDL YLVCCDGDTL
     AGVATAEIDW KQNHAELTNC ATHPDYRGLG LNTILLKRLE ESCLAKGINC LYSLARASSY
     GINLILHRLG YDSQGTLINN CHIAGDFENM NIWVKPAYDK NK
//
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