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 27-MAR-2024, entry version 88.
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; 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:SF115; CARNITINE O-ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1.
DR Pfam; PF00755; Carn_acyltransf; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
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
//
