CACP_COLLI
ID CACP_COLLI Reviewed; 627 AA.
AC P52826;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Carnitine O-acetyltransferase {ECO:0000305};
DE Short=Carnitine acetylase;
DE EC=2.3.1.137 {ECO:0000250|UniProtKB:P43155};
DE EC=2.3.1.7 {ECO:0000250|UniProtKB:P43155};
DE AltName: Full=Carnitine acetyltransferase;
DE Short=CAT;
DE Short=CrAT;
DE Flags: Precursor;
GN Name=CRAT;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver, and Pectoralis muscle;
RX PubMed=7832757; DOI=10.1042/bj3050439;
RA Johnson T.M., Kocher H.P., Anderson R.C., Nemecek G.M.;
RT "Cloning, sequencing and heterologous expression of a cDNA encoding pigeon
RT liver carnitine acetyltransferase.";
RL Biochem. J. 305:439-444(1995).
CC -!- FUNCTION: Catalyzes the reversible transfer of acyl groups from
CC carnitine to coenzyme A (CoA) and regulates the acyl-CoA/CoA ratio.
CC Also plays a crucial role in the transport of fatty acids for beta-
CC oxidation. Responsible for the synthesis of short- and branched-chain
CC acylcarnitines. Active towards some branched-chain amino acid oxidation
CC pathway (BCAAO) intermediates. Trans-2-enoyl-CoAs and 2-methylacyl-CoAs
CC are poor substrates. {ECO:0000250|UniProtKB:P43155}.
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 Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21137;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + propanoyl-CoA = CoA + O-propanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44976, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:53210, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44977;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + butanoyl-CoA = CoA + O-butanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:44980, ChEBI:CHEBI:16347, ChEBI:CHEBI:21949,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57371;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44981;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + hexanoyl-CoA = CoA + O-hexanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:44972, ChEBI:CHEBI:16347, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:84834;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44973;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + octanoyl-CoA = CoA + O-octanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:17177, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; EC=2.3.1.137;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17178;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + decanoyl-CoA = CoA + O-decanoyl-(R)-carnitine;
CC Xref=Rhea:RHEA:44828, ChEBI:CHEBI:16347, ChEBI:CHEBI:28717,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44829;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 3-methylbutanoyl-CoA = CoA + O-3-
CC methylbutanoyl-(R)-carnitine; Xref=Rhea:RHEA:44984,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57345,
CC ChEBI:CHEBI:70819; Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44985;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 2-methylpropanoyl-CoA = CoA + O-isobutanoyl-
CC (R)-carnitine; Xref=Rhea:RHEA:44988, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:84838;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44989;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 2-methylbutanoyl-CoA = CoA + O-2-
CC methylbutanoyl-(R)-carnitine; Xref=Rhea:RHEA:44992,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:57336,
CC ChEBI:CHEBI:84840; Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44993;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + acetoacetyl-CoA = CoA + O-3-oxobutanoyl-(R)-
CC carnitine; Xref=Rhea:RHEA:44996, ChEBI:CHEBI:16347,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:84841;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44997;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 3-hydroxybutanoyl-CoA = CoA + O-3-
CC hydroxybutanoyl-(R)-carnitine; Xref=Rhea:RHEA:45000,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:78611,
CC ChEBI:CHEBI:84842; Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45001;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 4,8-dimethylnonanoyl-CoA = CoA + O-4,8-
CC dimethylnonanoyl-(R)-carnitine; Xref=Rhea:RHEA:44860,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061,
CC ChEBI:CHEBI:84654; Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44861;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-carnitine + 2,6-dimethylheptanoyl-CoA = CoA + O-2,6-
CC dimethylheptanoyl-(R)-carnitine; Xref=Rhea:RHEA:45004,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:57287, ChEBI:CHEBI:84843,
CC ChEBI:CHEBI:84847; Evidence={ECO:0000250|UniProtKB:P43155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45005;
CC Evidence={ECO:0000250|UniProtKB:P43155};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}. Peroxisome
CC {ECO:0000305}. Mitochondrion inner membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U08229; AAA80570.1; -; mRNA.
DR PIR; S53369; S53369.
DR RefSeq; NP_001269768.1; NM_001282839.1.
DR AlphaFoldDB; P52826; -.
DR SMR; P52826; -.
DR STRING; 8932.XP_005514027.1; -.
DR GeneID; 102084317; -.
DR KEGG; clv:102084317; -.
DR CTD; 1384; -.
DR eggNOG; KOG3717; Eukaryota.
DR OrthoDB; 559299at2759; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; ISS:UniProtKB.
DR GO; GO:0004092; F:carnitine O-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; ISS:UniProtKB.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; ISS:UniProtKB.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0046459; P:short-chain fatty acid metabolic process; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Direct protein sequencing;
KW Endoplasmic reticulum; Fatty acid metabolism; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Peroxisome; Transferase;
KW Transport.
FT PROPEP 1..30
FT /id="PRO_0000004428"
FT CHAIN 31..627
FT /note="Carnitine O-acetyltransferase"
FT /id="PRO_0000004429"
FT MOTIF 625..627
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P43155"
FT BINDING 420
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT BINDING 424..431
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT BINDING 453
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P43155"
FT BINDING 455
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P43155"
FT BINDING 457
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT BINDING 466
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250|UniProtKB:P43155"
FT BINDING 556
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT MOD_RES 94
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT MOD_RES 262
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43155"
FT MOD_RES 262
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P47934"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43155"
SQ SEQUENCE 627 AA; 71067 MW; DD42317336AF0D2A CRC64;
MDRKQKQAEK ARPYGLLKPA ALGKIPGRFQ LHQEALPHLP VPPLQQTLDR YLLALQPIIS
EEELNHTQEL VAEFRKPGGV GERLQKGLER RAKKTDNWLS DWWLKTAYLE YRLPVVVHSS
PGVVLPKQDF QDRQGQLRFA AKLIEGILDF KTMIDNETLP VEYMGGKPLC MNQYYQILSS
CRIPGPKRDS IVNYAKGKKQ SRHITVVHNF QFFELDVYNS DGSPLTTDQL FIQLEKIWNT
SLQTNKEPVG ILTTNHRNSW AKAYNNLLKD KTNKESVRTI EKSICTICLD APMPRVSDDI
YKSPVAAQML HGGGSRWNSG NRWFDKTLQF IIAEDGSCGL VYEHAPAEGP PIVALLDHIV
EYTKKPELVR SPMIPLPMPK KLRFNITPEI KSDIEKAKQN LNIMVEDLDV IVLVFHQFGK
NYPKSEKISP DAFIQLALQL AYYRMYGHSC ATYESASLRM FRLGRTDTIR STSIESHKFV
QSMDSPDKSD QEKADLLRRA TQAHKEYTNM AIQGNAIDRH LLGLKLQAIE DLVSIPELFM
DTAYAVAMHF NLSTSQVPAK TDCVMCFGPV VPDGYGICYN PMGEHINFAI SAFNSCADTN
AARMAHYLEK ALLDMRSLLQ SAPKSKL
