GenomeNet

Database: UniProt
Entry: A6TMI7_ALKMQ
LinkDB: A6TMI7_ALKMQ
Original site: A6TMI7_ALKMQ 
ID   A6TMI7_ALKMQ            Unreviewed;       182 AA.
AC   A6TMI7;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=GCN5-related N-acetyltransferase {ECO:0000313|EMBL:ABR47405.1};
GN   OrderedLocusNames=Amet_1197 {ECO:0000313|EMBL:ABR47405.1};
OS   Alkaliphilus metalliredigens (strain QYMF).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Alkaliphilus.
OX   NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR47405.1, ECO:0000313|Proteomes:UP000001572};
RN   [1] {ECO:0000313|Proteomes:UP000001572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX   PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA   Hwang C., 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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA   Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA   Richardson P., Fields M.W.;
RT   "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT   alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT   leachate ponds.";
RL   Genome Announc. 4:0-0(2016).
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; CP000724; ABR47405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6TMI7; -.
DR   STRING; 293826.Amet_1197; -.
DR   KEGG; amt:Amet_1197; -.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_013985_3_2_9; -.
DR   Proteomes; UP000001572; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR43415; SPERMIDINE N(1)-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43415:SF3; SPERMIDINE N(1)-ACETYLTRANSFERASE; 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:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001572};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABR47405.1}.
FT   DOMAIN          21..178
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   182 AA;  21720 MW;  39445838B8616EA3 CRC64;
     MKLKKEGGEN MAEMIIEKDD TVFYVTEPKD LEEIIEIEKV QYDSENRRFV YLWPMERHLE
     SIDCKDELHM TIKHKETQEV IGYVILSGLT EEHDVIEFDR IALKIQGKGY GRKSVQLIKS
     LCFEKLGCNR LWLDVFDYNT KAFELYKSED FIHEGTLRQC KKYNGKYHAM HLMSMLREEY
     FA
//
DBGET integrated database retrieval system