ID   CACP_CANTR              Reviewed;         627 AA.
AC   Q00614;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Carnitine O-acetyltransferase, mitochondrial;
DE            Short=Carnitine acetylase;
DE            EC=2.3.1.7;
DE   Flags: Precursor;
GN   Name=CAT2; Synonyms=CAT;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   PubMed=8706689; DOI=10.1111/j.1432-1033.1996.0845w.x;
RA   Kawachi H., Atomi H., Ueda M., Tanaka A.;
RT   "Peroxisomal and mitochondrial carnitine acetyltransferases of the n-
RT   alkane-assimilating yeast Candida tropicalis. Analysis of gene structure
RT   and translation products.";
RL   Eur. J. Biochem. 238:845-852(1996).
CC   -!- FUNCTION: Carnitine acetylase is specific for short chain fatty acids.
CC       Carnitine acetylase seems to affect the flux through the pyruvate
CC       dehydrogenase complex. It may be involved as well in the transport of
CC       acetyl-CoA into mitochondria (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-carnitine + acetyl-CoA = CoA + O-acetyl-(R)-carnitine;
CC         Xref=Rhea:RHEA:21136, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57589; EC=2.3.1.7;
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Mitochondrion inner
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Matrix side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; D84549; BAA12696.1; -; Genomic_DNA.
DR   PIR; S68958; S68958.
DR   AlphaFoldDB; Q00614; -.
DR   SMR; Q00614; -.
DR   VEuPathDB; FungiDB:CTMYA2_034660; -.
DR   VEuPathDB; FungiDB:CTRG_00243; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004092; F:carnitine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009437; P:carnitine metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 3.30.559.70; -; 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; PTHR22589; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Fatty acid metabolism; Lipid metabolism; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Peroxisome; Transferase;
KW   Transit peptide; Transport.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..627
FT                   /note="Carnitine O-acetyltransferase, mitochondrial"
FT                   /id="PRO_0000004430"
FT   MOTIF           625..627
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        336
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         418
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         422..429
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000250"
FT   BINDING         453
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="(R)-carnitine"
FT                   /ligand_id="ChEBI:CHEBI:16347"
FT                   /evidence="ECO:0000250"
FT   BINDING         553
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   627 AA;  70762 MW;  B00878F37CC7D84B CRC64;
     MFNFKLSQQV LKNSTKSIMP ILKKPFSTSH AKGDLFKYQS QLPKLPVPTL EETASKYLKT
     VEPFLNQEQL ESTKAKVAEF VRPGGAGEAL QARLNNFAAD KDNWLAEFWD DYAYMSYRDP
     VVPYVSYFFS HKDVKNIIGQ DQLLKATLIA YYTIEFQEKV LDESLDPEVI KGNPFCMNAF
     KYMFNNSRVP AEGSDITQHY NGEENQFFVV IYKNNFYKVP THKNGQRLTK GEIYSYLQEI
     KNDATPKGLG LGALTSLNRD EWLSAYNNLL KSPINEASLG SIFASSFVIA LDSNNPVTIE
     EKSKNCWHGD GQNRFFDKPL EFFVSANGNS GFLGEHSRMD ATPTVQLNNT IYKQILETNP
     NDLIVEIGSS APRFGNAEIL PFDINPTTRA NIKDAIAKFD ATIAAHDEEI FQHYGYGKGL
     IKKFKVSPDA YVQLLMQLAY FKYTGKIRPT YESAATRKFL KGRTETGRTV SNESKKFVET
     WSDPNASSAD KVATFQAAAK QHVAYLSAAA DGKGVDRHLF GLKQMIQPGE PIPEIFTDPI
     FSYSQTWYIS SSQVPSEFFQ SWGWSQVIDD GFGLAYLINN DWIHVHISCK RGNGLQSDHL
     KWYLVDSANE MKDVLTKGLL TDAKPKL