ID   A0A0P0SD79_9PSEU        Unreviewed;       597 AA.
AC   A0A0P0SD79;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Carnitine O-acetyltransferase {ECO:0000313|EMBL:ALL82231.1};
GN   ORFNames=AD017_15490 {ECO:0000313|EMBL:ALL82231.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL82231.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL82231.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL82231.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}.
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DR   EMBL; CP012184; ALL82231.1; -; Genomic_DNA.
DR   RefSeq; WP_060574657.1; NZ_CP012184.1.
DR   AlphaFoldDB; A0A0P0SD79; -.
DR   STRING; 1096856.AD017_15490; -.
DR   KEGG; pecq:AD017_15490; -.
DR   PATRIC; fig|1096856.3.peg.3250; -.
DR   Proteomes; UP000066228; Chromosome.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.70; Choline/Carnitine o-acyltransferase, domain 2; 1.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR039551; Cho/carn_acyl_trans.
DR   InterPro; IPR042231; Cho/carn_acyl_trans_2.
DR   PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066228};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}.
FT   DOMAIN          18..586
FT                   /note="Choline/carnitine acyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00755"
FT   REGION          155..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        315
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600542-1"
SQ   SEQUENCE   597 AA;  64696 MW;  36D6B79963D83ABD CRC64;
     MAVTQPTTFV ADDDLPKVPL PTLAASVDRF LEWCAPLLTP DEYARTEAAA RELLVPGGTA
     EVLQADLERF DASAHSWLDE FWPSRYLGRR DRIALNANFF FQFGPGSADP CERAAELATA
     AIGHKADLDA GTFPPLTARG VPQSMDQSRH VFSTTRIPGD PQDTVRSPHT DAWPGPSAER
     HVVVFSRGRI HRLDVFGPGG DLHTVPEIAD GLRAIRDAYP GRAGLDEAVG SLTTLARAEW
     AGVRDRLAGL DPANAEAVDL VERALFAICL DDDVPADDTA AARTLLAGDS GNRWFDKALS
     VVVLADGTAG VNIEHCELDG TTVLTLVDAM FADPVETHAA RAGAREQGPP AHSELTFVLD
     DDLRATVRRA HDDFAAFLGA TATTLVAFDD FGAQDAKALK CSPDAFVQAA YQVAHRRAKG
     VTGATYESIA TRQFRRGRTE AMRVITPEMV AFVDAMQDPQ AADDDRRAAF RLAAEAHGAR
     AKQCQQGDAP EQHLWELEWI QRRRGAELGA TEPMEVFASP GWTIMRDDWL STSSAPSENV
     RFFGFGSTSS RCIGVAYVLL PDRFHVHLST PADQADGMHA FARELRVAVG ELRNLLA
//