OCTC_BOVIN
ID OCTC_BOVIN Reviewed; 612 AA.
AC O19094;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Peroxisomal carnitine O-octanoyltransferase;
DE Short=COT;
DE EC=2.3.1.137 {ECO:0000250|UniProtKB:Q9UKG9};
GN Name=CROT; Synonyms=COT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
RC TISSUE=Liver;
RX PubMed=9288928; DOI=10.1111/j.1432-1033.1997.01029.x;
RA Cronin C.N.;
RT "cDNA cloning, recombinant expression, and site-directed mutagenesis of
RT bovine liver carnitine octanoyltransferase -- Arg505 binds the carboxylate
RT group of carnitine.";
RL Eur. J. Biochem. 247:1029-1037(1997).
CC -!- FUNCTION: Beta-oxidation of fatty acids. The highest activity concerns
CC the C6 to C10 chain length substrate. {ECO:0000250|UniProtKB:Q9UKG9}.
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:Q9UKG9};
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:Q9UKG9};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U65745; AAC48758.1; -; mRNA.
DR RefSeq; NP_803460.1; NM_177494.2.
DR AlphaFoldDB; O19094; -.
DR SMR; O19094; -.
DR STRING; 9913.ENSBTAP00000028699; -.
DR PaxDb; O19094; -.
DR PeptideAtlas; O19094; -.
DR PRIDE; O19094; -.
DR Ensembl; ENSBTAT00000076118; ENSBTAP00000071426; ENSBTAG00000021535.
DR GeneID; 281092; -.
DR KEGG; bta:281092; -.
DR CTD; 54677; -.
DR VEuPathDB; HostDB:ENSBTAG00000021535; -.
DR VGNC; VGNC:27723; CROT.
DR eggNOG; KOG3718; Eukaryota.
DR GeneTree; ENSGT01050000244969; -.
DR InParanoid; O19094; -.
DR OrthoDB; 559299at2759; -.
DR BRENDA; 2.3.1.137; 908.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000021535; Expressed in liver and 108 other tissues.
DR ExpressionAtlas; O19094; baseline and differential.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008458; F:carnitine O-octanoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0009437; P:carnitine metabolic process; ISS:UniProtKB.
DR GO; GO:0015936; P:coenzyme A metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.275.20; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.30.559.70; -; 1.
DR InterPro; IPR000542; Carn_acyl_trans.
DR InterPro; IPR042572; Carn_acyl_trans_N.
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; Fatty acid metabolism; Lipid metabolism;
KW Peroxisome; Reference proteome; Transferase; Transport.
FT CHAIN 1..612
FT /note="Peroxisomal carnitine O-octanoyltransferase"
FT /id="PRO_0000210168"
FT MOTIF 610..612
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 327
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 410..417
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="(R)-carnitine"
FT /ligand_id="ChEBI:CHEBI:16347"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKG9"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC50"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC50"
FT MOD_RES 406
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DC50"
FT MOD_RES 406
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DC50"
FT MUTAGEN 505
FT /note="R->N: Increase of KM towards carnitine."
FT /evidence="ECO:0000269|PubMed:9288928"
SQ SEQUENCE 612 AA; 70263 MW; 2D5D91A54CF8E2BA CRC64;
MENQLAKSTE ERTFQYQDSL PSLPVPSLEE SLKKYLESVK PFANEEEYKN TEAIVWKFQN
GIGEKLQQKL LQRAKGRRNW LEEWWLNVAY LDVRIPSQLN VNFGGPASHI EHYWPPKEGT
QLERGSISLW HNLNYWQLLR KEKLAVEKVG NTPLDMNQFR MLFSTCKIPG ITRDSIINYF
RTESEGHSPS HLAVLCRGRV FVFDVMHEGY LMTAPEIQRQ LTYIQKKCHS EPDGPGVAAL
TTEERTRWAK AREYLISLNP ENLTILEKIQ SSLLVFCLDD DSPHVTPEDY SQVSAKILNG
DPTVRWGDKS YNLIAFSNGV FGSNCDHAPF DAMVLVKVCY YVDENILENE GRWKGSEKVR
DIPVPEELVF TVDEKVLNDI NQAKAQYFKQ VSDLQLVVYA FTSFGKKLTK EKQLHPDTFI
QLALQLAYYR LHGRPGCCYE TAMTRLFYHG RTETVRPCTV EAVNWCQSMQ NPSTSLLERK
HMMLEAFAKH NKMMKDCSTG KGFDRHLLGL SLIAKEEGLP VPELFTDPLF SRSGGGGNFV
LSTSLVGYLR VQGVMVPMVH NGYGFFYHIR DDRFVVSCSA WKSCPETDAE KLVQQVFHAF
CDMMQLMEMP HL
