ID A0A067XH78_TACFU Unreviewed; 771 AA. AC A0A067XH78; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 27-MAR-2024, entry version 29. DE RecName: Full=Carnitine O-palmitoyltransferase 1, muscle isoform {ECO:0000256|ARBA:ARBA00040569}; DE EC=2.3.1.21 {ECO:0000256|ARBA:ARBA00013243}; DE AltName: Full=Carnitine O-palmitoyltransferase I, muscle isoform {ECO:0000256|ARBA:ARBA00041685}; DE AltName: Full=Carnitine palmitoyltransferase 1B {ECO:0000256|ARBA:ARBA00042959}; OS Tachysurus fulvidraco (Yellow catfish) (Pimelodus fulvidraco). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes; OC Bagridae; Tachysurus. OX NCBI_TaxID=1234273 {ECO:0000313|EMBL:AFO11021.1}; RN [1] {ECO:0000313|EMBL:AFO11021.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver {ECO:0000313|EMBL:AFO11021.1}; RA Zheng J.L., Luo Z., Chen Q.L., Gong Y., Zhu Q.L., Gu Q.H., Hu W., Liu C.X.; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty CC acid-CoA conjugates onto carnitine, an essential step for the CC mitochondrial uptake of long-chain fatty acids and their subsequent CC beta-oxidation in the mitochondrion. {ECO:0000256|ARBA:ARBA00043926}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)- CC carnitine; Xref=Rhea:RHEA:12661, ChEBI:CHEBI:16347, CC ChEBI:CHEBI:17490, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=2.3.1.21; CC Evidence={ECO:0000256|ARBA:ARBA00043805}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12662; CC Evidence={ECO:0000256|ARBA:ARBA00043805}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000256|ARBA:ARBA00005005}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004374}. CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family. CC {ECO:0000256|ARBA:ARBA00005232, ECO:0000256|RuleBase:RU003801}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JN579122; AFO11021.1; -; mRNA. DR AlphaFoldDB; A0A067XH78; -. DR UniPathway; UPA00659; -. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR Gene3D; 6.10.250.1760; -; 1. 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 InterPro; IPR032476; CPT_N. DR PANTHER; PTHR22589; CARNITINE O-ACYLTRANSFERASE; 1. DR PANTHER; PTHR22589:SF69; CARNITINE O-PALMITOYLTRANSFERASE 1, MUSCLE ISOFORM; 1. DR Pfam; PF00755; Carn_acyltransf; 1. DR Pfam; PF16484; CPT_N; 1. DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2. DR PROSITE; PS00439; ACYLTRANSF_C_1; 1. DR PROSITE; PS00440; ACYLTRANSF_C_2; 1. PE 2: Evidence at transcript level; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, KW ECO:0000256|RuleBase:RU003801}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003801}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 54..75 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 104..126 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..46 FT /note="Carnitine O-palmitoyltransferase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16484" FT DOMAIN 174..754 FT /note="Choline/carnitine acyltransferase" FT /evidence="ECO:0000259|Pfam:PF00755" FT ACT_SITE 471 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR600542-1" SQ SEQUENCE 771 AA; 88755 MW; AF6ADB6F89F868AF CRC64; MAEAHQAVAF QFTVTPEGID LRLSREALKH IYLARVTSWR KRVILFRNGI RMGVYPASPS SWLFVVIVIM SSMYARLDPS MGMINSIKKV LPASDHLTSQ AQTVLSAIVF ATGLWFSLIM LLRYILKVLL SYHGWIFEPH GKMSMTTKLW ISLLKMFSGH RPLLYSFQGS LPRLPVPSID DTINRYLESV RPLLDDDRYK QMEIVANEFK KDQAPKLQKY LKLKSWWANN YVSDWWEEYI YLRGRGPIMV NSNFYTMDLL YMIPTHRQAA RAGNVVHAIL QYRRKLERGE HAPMRALGVV PMCSYQYEGM FNTTRIPGIE TDCVQHLRNR KHLVVYHKGR FFKVWLYYGG RHLLPAELEQ QFQHILNDTT EPQSGELKLA SLTAGNRVPW AKARQKHFSD GVNKTSLDTI ETAAFFLTLD DESHGYDPEN PRSMDLYAKS LLHGKCYDRW FDKSFNLIIF KNGTMGLNAE HTWADAPIVG HLWEHVLSMD PITLGYTEDG HCRGKPHPNL PGPLRLQWDI SVECQSVIRS SLKVANALAD DVDMHIFPFN NFGKGLIKKC KTSPDGFIQI ALQLAHFRDK KKFCLTYEAS MTRLFREGRT ETVRSCTMET CDFVRAMMDE KQTREEKLRL LKLAAEKHQE LYRMAMTGKG IDRHIFCLYV VSKYLGDDSA FLKEVLSEPW RLSTSQTPLQ QIELFDLKKH PEYVTSGGGF GPVADDGYGV SYIILGEDLI NFHISSKYSS IETDSHRFGN HIKQAMLDIL ALFELDKKTV K //