CACP_MOUSE
ID CACP_MOUSE Reviewed; 626 AA.
AC P47934; Q3TCG3; Q3V1Y3; Q923A6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 168.
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;
GN Name=Crat {ECO:0000312|MGI:MGI:109501};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9065756; DOI=10.1042/bj3220403;
RA Brunner S., Kramar K., Denhardt D.T., Hofbauer R.;
RT "Cloning and characterization of murine carnitine acetyltransferase:
RT evidence for a requirement during cell cycle progression.";
RL Biochem. J. 322:403-410(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-93 AND LYS-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-626 IN COMPLEX WITH CARNITINE
RP AND COENZYME A.
RX PubMed=12526798; DOI=10.1016/s0092-8674(02)01228-x;
RA Jogl G., Tong L.;
RT "Crystal structure of carnitine acetyltransferase and implications for the
RT catalytic mechanism and fatty acid transport.";
RL Cell 112:113-122(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-626 OF MUTANTS GLY-564 AND
RP ALA-565 IN COMPLEX WITH CARNITINE AND COENZYME A.
RX PubMed=15155726; DOI=10.1074/jbc.m403484200;
RA Hsiao Y.-S., Jogl G., Tong L.;
RT "Structural and biochemical studies of the substrate selectivity of
RT carnitine acetyltransferase.";
RL J. Biol. Chem. 279:31584-31589(2004).
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:0000269|PubMed:12526798,
CC ECO:0000269|PubMed:15155726}.
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; X85983; CAA59971.1; -; mRNA.
DR EMBL; AK132179; BAE21016.1; -; mRNA.
DR EMBL; AK170740; BAE41993.1; -; mRNA.
DR EMBL; AL954299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006668; AAH06668.1; -; mRNA.
DR CCDS; CCDS15882.1; -.
DR PIR; S52782; S52782.
DR RefSeq; NP_031786.2; NM_007760.3.
DR PDB; 1NDB; X-ray; 1.80 A; A/B=30-625.
DR PDB; 1NDF; X-ray; 1.90 A; A/B=30-625.
DR PDB; 1NDI; X-ray; 2.30 A; A/B=30-625.
DR PDB; 1T7N; X-ray; 1.90 A; A=30-626.
DR PDB; 1T7O; X-ray; 2.30 A; A=30-626.
DR PDB; 1T7Q; X-ray; 1.80 A; A/B=30-626.
DR PDB; 2H3P; X-ray; 2.20 A; A/B=30-625.
DR PDB; 2H3U; X-ray; 1.90 A; A/B=30-625.
DR PDB; 2H3W; X-ray; 2.10 A; A/B=30-625.
DR PDBsum; 1NDB; -.
DR PDBsum; 1NDF; -.
DR PDBsum; 1NDI; -.
DR PDBsum; 1T7N; -.
DR PDBsum; 1T7O; -.
DR PDBsum; 1T7Q; -.
DR PDBsum; 2H3P; -.
DR PDBsum; 2H3U; -.
DR PDBsum; 2H3W; -.
DR AlphaFoldDB; P47934; -.
DR SMR; P47934; -.
DR BioGRID; 198871; 21.
DR IntAct; P47934; 3.
DR STRING; 10090.ENSMUSP00000028207; -.
DR iPTMnet; P47934; -.
DR PhosphoSitePlus; P47934; -.
DR jPOST; P47934; -.
DR MaxQB; P47934; -.
DR PaxDb; P47934; -.
DR PRIDE; P47934; -.
DR ProteomicsDB; 273892; -.
DR Antibodypedia; 17825; 236 antibodies from 29 providers.
DR DNASU; 12908; -.
DR Ensembl; ENSMUST00000028207; ENSMUSP00000028207; ENSMUSG00000026853.
DR Ensembl; ENSMUST00000102855; ENSMUSP00000099919; ENSMUSG00000026853.
DR GeneID; 12908; -.
DR KEGG; mmu:12908; -.
DR UCSC; uc008jcl.1; mouse.
DR CTD; 1384; -.
DR MGI; MGI:109501; Crat.
DR VEuPathDB; HostDB:ENSMUSG00000026853; -.
DR eggNOG; KOG3717; Eukaryota.
DR GeneTree; ENSGT01050000244830; -.
DR InParanoid; P47934; -.
DR OMA; YYRMYGH; -.
DR OrthoDB; 559299at2759; -.
DR PhylomeDB; P47934; -.
DR TreeFam; TF313836; -.
DR BRENDA; 2.3.1.7; 3474.
DR Reactome; R-MMU-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 12908; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Crat; mouse.
DR EvolutionaryTrace; P47934; -.
DR PRO; PR:P47934; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P47934; protein.
DR Bgee; ENSMUSG00000026853; Expressed in hindlimb stylopod muscle and 270 other tissues.
DR ExpressionAtlas; P47934; baseline and differential.
DR Genevisible; P47934; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
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:0006631; P:fatty acid metabolic process; ISO:MGI.
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 3D-structure; Acetylation; Acyltransferase; Endoplasmic reticulum;
KW Fatty acid metabolism; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Peroxisome; Reference proteome; Transferase;
KW Transport.
FT CHAIN 1..626
FT /note="Carnitine O-acetyltransferase"
FT /id="PRO_0000210173"
FT MOTIF 624..626
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT BINDING 419
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:12526798,
FT ECO:0000269|PubMed:15155726"
FT BINDING 423..430
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000269|PubMed:12526798,
FT ECO:0000269|PubMed:15155726"
FT BINDING 454
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000269|PubMed:12526798,
FT ECO:0000269|PubMed:15155726"
FT BINDING 456
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:12526798,
FT ECO:0000269|PubMed:15155726"
FT BINDING 465
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000269|PubMed:12526798,
FT ECO:0000269|PubMed:15155726"
FT BINDING 504
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:12526798,
FT ECO:0000269|PubMed:15155726"
FT BINDING 555
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:12526798,
FT ECO:0000269|PubMed:15155726"
FT MOD_RES 93
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 261
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43155"
FT MOD_RES 261
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 268
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43155"
FT MUTAGEN 564
FT /note="M->A: Lowers activity towards short-chain fatty
FT acids."
FT MUTAGEN 564
FT /note="M->G: Lowers activity towards short-chain fatty
FT acids. Strong increase in activity towards medium chain
FT fatty acids."
FT MUTAGEN 565
FT /note="F->A: Increases activity towards short-chain fatty
FT acids."
FT CONFLICT 39
FT /note="P -> S (in Ref. 2; BAE41993)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..112
FT /note="FRQ -> LPDK (in Ref. 1; CAA59971)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="V -> E (in Ref. 1; CAA59971)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="Y -> H (in Ref. 2; BAE41993)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="H -> N (in Ref. 1; CAA59971)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="F -> L (in Ref. 1; CAA59971)"
FT /evidence="ECO:0000305"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1NDB"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 79..93
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:1NDB"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1NDB"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 132..154
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1T7N"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2H3U"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1NDB"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:1NDB"
FT TURN 314..319
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1NDF"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1NDB"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 348..361
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:1T7Q"
FT HELIX 387..405
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 407..414
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 429..445
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 473..483
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:1T7O"
FT HELIX 489..511
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 517..529
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 536..539
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 541..546
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 574..580
FT /evidence="ECO:0007829|PDB:1NDB"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:1NDB"
FT HELIX 600..619
FT /evidence="ECO:0007829|PDB:1NDB"
SQ SEQUENCE 626 AA; 70840 MW; 975EA04403A4F3D9 CRC64;
MLAFAARTVV KPLGLLKPSS LMKVSGRFKA HQDALPRLPV PPLQQSLDYY LKALQPIVSE
EEWAHTKQLV DEFQTSGGVG ERLQKGLERR AKKMENWLSE WWLKTAYLQF RQPVVIYSSP
GVILPKQDFV DLQGQLRFAA KLIEGVLDFK SMIDNETLPV EFLGGQPLCM NQYYQILSSC
RVPGPKQDSV VNFLKSKRPP THITVVHNYQ FFELDVYHSD GTPLTSDQIF VQLEKIWNSS
LQSNKEPVGI LTSNHRNTWA KAYNNLIKDK VNRESVNSIQ KSIFTVCLDK QVPRVSDDVY
RNHVAGQMLH GGGSKFNSGN RWFDKTLQFI VAEDGSCGMV YEHAAAEGPP IVALVDHVME
YTKKPELVRS PMVPLPMPKK LRFNITPEIK NDIEKAKQNL SIMIQDLDIM MLTFHHFGKD
FPKSEKLSPD AFIQVALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASIDSLAFVK
GMGDSTVPEQ QKVELLRKAV QAHRAYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD
TSYAIAMHFN LSTSQVPAKT DCVMFFGPVV PDGYGICYNP MEAHINFSVS AYNSCAETNA
ARMAHYLEKA LLDMRTLLQN HPRAKL
